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Information on EC 2.7.7.79 - tRNAHis guanylyltransferase
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2.7.7.79 tRNAHis guanylyltransferaseIUBMB Comments
In eukarya an additional guanosine residue is added post-transcriptionally to the 5'-end of tRNAHis molecules. The addition occurs opposite a universally conserved adenosine73 and is thus the result of a non-templated 3'-5' addition reaction. The additional guanosine residue is an important determinant for aminoacylation by EC 6.1.1.21, histidine---tRNA ligase.The enzyme requires a divalent cation for activity . ATP activation is not required when the substrate contains a 5'-triphosphate (ppp-tRNAHis) .
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Word Map
- 2.7.7.79
- guanosine
- polymerases
- polymerization
-
histidyl-trna
- aminoacylation
-
fidelity
-
anticodon
-
post-transcriptionally
-
watson-crick
-
template-dependent
-
nucleotidyl
-
genome-encoded
- methanosarcina
- ntp
- acetivorans
-
phosphodiester
- thuringiensis
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
p-tRNAHis
+
+
+
=
pGp-tRNAHis
+
+
2
p-tRNAHis
+
=
App-tRNAHis
+
App-tRNAHis
+
=
pppGp-tRNAHis
+
Synonyms
trna(his) guanylyltransferase, thg1l, trnahis guanylyltransferase, hsthg1, thg1p, mathg1, hthg1, bttlp, histidine trna guanylyltransferase, pathg1, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BtTLP
CaThg1
DdiTLP3
Igni_0485
IhTLP
MxTLP
PaThg1
PaTLP
RBTH_06728
ScThg1
THG1
Thg1 domain-containing protein
Thg1-like-protein
TLP
tRNA(His) guanylyltransferase
tRNA(His)-5'-guanylyltransferase (Thg1) like protein
UniProt
Thg1 domain-containing protein
UniProt
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pppGp-tRNAHis + H2O = pGp-tRNAHis + diphosphate
(1c)
-
-
-
App-tRNAHis + GTP = pppGp-tRNAHis + AMP
-
-
-
-
p-tRNAHis + ATP + GTP + H2O = pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
p-tRNAHis + ATP + GTP + H2O = pGp-tRNAHis + AMP + 2 diphosphate
-
-
-
-
p-tRNAHis + ATP = App-tRNAHis + diphosphate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
p-tRNAHis:GTP guanylyltransferase (ATP-hydrolysing)
In eukarya an additional guanosine residue is added post-transcriptionally to the 5'-end of tRNAHis molecules. The addition occurs opposite a universally conserved adenosine73 and is thus the result of a non-templated 3'-5' addition reaction. The additional guanosine residue is an important determinant for aminoacylation by EC 6.1.1.21, histidine---tRNA ligase.The enzyme requires a divalent cation for activity [2]. ATP activation is not required when the substrate contains a 5'-triphosphate (ppp-tRNAHis) [3].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
mt-tRNALeuDelta+2 + GTP
? + diphosphate
substrate mimics the presumed in vivo substrate for 5'-end repair, in which the two 5'-mismatched nucleotides have been removed and the resulting tRNA transcript begins with G+3. TLP1 and TLP2 catalyse robust addition of the missing 5'-G nucleotides to this substrate
-
-
?
p-ctRNAHis + ATP + GTP + H2O
pGp-ctRNAHis + AMP + 2 diphosphate
cytoplasmic tRNAHis
-
-
?
p-mtRNAHis + ATP + GTP + H2O
pGp-mtRNAHis + AMP + 2 diphosphate
mitochondrial tRNAHis
-
-
?
p-tRNAHis + ATP + 7-deaza-GTP + H2O
p-7-deaza-Gp-tRNAHis + AMP + 2 diphosphate
-
-
-
?
p-tRNAHis + ATP + dGTP
?
dGTP is almost as efficient as GTP for the guanylylation process. While GDP still serves for the enzymatic reaction, GMP is accepted very poorly by the enzyme
-
-
?
p-tRNAHis + ATP + GDP
?
dGTP is almost as efficient as GTP for the guanylylation process. While GDP still serves for the enzymatic reaction, GMP is accepted very poorly by the enzyme
-
-
?
p-tRNAHis + ATP + GTP
pppG-p-tRNAHis + AMP + diphosphate
the extra nucleotide in position -1 of mitochondrial and eukaryotic cytoplasmic tRNAHis molecules is added posttranscriptionally to the 5' end of the tRNA by a histidine-tRNA specific guanylyltransferase
-
-
?
p-tRNAHis + ATP + ITP + H2O
pIp-tRNAHis + AMP + 2 diphosphate
very high activity
-
-
?
p-tRNAHis + ATP + UTP + H2O
pUp-tRNAHis + AMP + 2 diphosphate
low activity
-
-
?
p-tRNAHis + dATP + GTP
pppGp-tRNAHis + dAMP + diphosphate
30% of the activity compared to ATP
-
-
?
p-tRNAHisC73 + ATP + 7-deaza-GTP + H2O
p-7-deaza-Gp-tRNAHisC73 + AMP + 2 diphosphate
T3C73 tRNAHis variant, low activity
-
-
?
p-tRNAHisC73 + ATP + GTP + H2O
pGp-tRNAHisC73 + AMP + 2 diphosphate
T3C73 tRNAHis variant, slightly reduced activity compared to wild-type T3A73 tRNAHis
-
-
?
p-tRNAHisC73 + ATP + ITP + H2O
pIp-tRNAHisC73 + AMP + 2 diphosphate
T3C73 tRNAHis variant, low activity
-
-
?
p-tRNAHisG73 + ATP + CTP + H2O
pCp-tRNAHisG73 + AMP + 2 diphosphate
T3G73 tRNAHis variant, no activity with CTP and wild-type T3A73 tRNAHis
-
-
?
p-tRNAHisG73 + ATP + GTP + H2O
pGp-tRNAHisG73 + AMP + 2 diphosphate
T3G73 tRNAHis variant, reduced activity compared to wild-type T3A73 tRNAHis
-
-
?
p-tRNAHisG73 + ATP + ITP + H2O
pIp-tRNAHisG73 + AMP + 2 diphosphate
T3G73 tRNAHis variant, reduced activity compared to wild-type T3A73 tRNAHis
-
-
?
p-tRNAHisU73 + ATP + 2-aminopurine + H2O
p-2.aminopurine-p-tRNAHisU73 + AMP + 2 diphosphate
T3U73 tRNAHis variant, activity is similar to wild-type T3A73 tRNAHis
-
-
?
p-tRNAHisU73 + ATP + GTP + H2O
pGp-tRNAHisU73 + AMP + 2 diphosphate
T3U73 tRNAHis variant, reduced activity compared to wild-type T3A73 tRNAHis
-
-
?
p-tRNAHisU73 + ATP + ITP + H2O
pIp-tRNAHisU73 + AMP + 2 diphosphate
T3U73 tRNAHis variant, low activity
-
-
?
ppp-tRNALeu + GTP
?
the D68A mutation causes a dramatic decrease in the rigorous specificity of Thg1 for tRNAHis. This single alteration enhances the kcat/KM for ppp-tRNALeu by 38-fold relative to that of wild-type Thg1
-
-
?
ppp-tRNAPhe + GTP
?
the D68A mutation causes a dramatic decrease in the rigorous specificity of Thg1 for tRNAHis. This single alteration enhances the kcat/KM for ppp-tRNAPhe by nearly 100-fold relative to that of wild-type Thg1
-
-
?
p-tRNAHis + ATP
App-tRNAHis + diphosphate
-
-
-
?
p-tRNAHis + ATP
App-tRNAHis + diphosphate
-
-
-
?
p-tRNAHis + ATP + 2-aminopurine + H2O
p-2-aminopurine-p-tRNAHis + AMP + 2 diphosphate
-
-
-
?
p-tRNAHis + ATP + 2-aminopurine + H2O
p-2-aminopurine-p-tRNAHis + AMP + 2 diphosphate
-
-
-
?
p-tRNAHis + ATP + 5'-triphosphorylated P4 + H2O
pUp-tRNAHis + AMP + 2 diphosphate
pppP4, neither ATP nor CTP is incorporated onto pppP4
-
-
?
p-tRNAHis + ATP + 5'-triphosphorylated P4 + H2O
pUp-tRNAHis + AMP + 2 diphosphate
pppP4, neither ATP nor CTP is incorporated onto pppP4
-
-
?
p-tRNAHis + ATP + GTP
pppGp-tRNAHis + AMP + diphosphate
-
overall reaction
-
?
p-tRNAHis + ATP + GTP
pppGp-tRNAHis + AMP + diphosphate
-
overall reaction
-
?
p-tRNAHis + ATP + GTP
pppGp-tRNAHis + AMP + diphosphate
-
-
-
?
p-tRNAHis + ATP + GTP
pppGp-tRNAHis + AMP + diphosphate
the G(-1) residue is both necessary and sufficient for aminoacylation of tRNA by histidyl-tRNA synthetase in vitro and is required for aminoacylation in vivo
-
-
?
p-tRNAHis + ATP + GTP
pppGp-tRNAHis + AMP + diphosphate
among all acceptor tRNAs in unfractionatedt RNA only tRNAHis is a substrate for the purified enzyme. tRNA from plant and prokaryotes are better substrates than mammalian and insect tRNAs
-
-
?
p-tRNAHis + ATP + GTP
pppGp-tRNAHis + AMP + diphosphate
during the first step ATP is cleaved to AMP and diphosphate creating adenylylated enzyme. In a second step the activated enzyme forms a stable complex with its cognate tRNA substrate. The 5'-phosphate of the tRNA is adenylylated by nucleotide transfer from the adenylylated guanylyltransferase to form A(5')pp(5') at the 5'-end of the tRNA. Finally, the 3'-hydroxyl of GTP adds to the activated 5' terminus of the tRNA with the release of AMP. dGTP is almost as efficient as GTP for the guanylylation process. While GDP still serves for the enzymatic reaction, GMP is accepted very poorly by the enzyme
-
-
?
p-tRNAHis + ATP + GTP
pppGp-tRNAHis + AMP + diphosphate
specific for tRNAHis. No activity with tRNAPhe. No ATP is required when ppp-tRNAHis is used as a substrate
-
-
?
p-tRNAHis + ATP + GTP
pppGp-tRNAHis + AMP + diphosphate
Thg1 is more than 10000-fold more selective for its cognate substrate tRNAHis than for the noncognate substrate tRNAPhe. Alteration of this anticodon in tRNAHis completely abrogates Thg1 activity, and the introduction of this GUG anticodon to tRNAPhe or tRNAGly results in significant Thg1 activity
-
-
?
p-tRNAHis + ATP + GTP
pppGp-tRNAHis + AMP + diphosphate
-
all tRNAHis possess an essential extra G1 guanosine residue at their 5' end. This extra guanylate residue can be generated via two different processes. In Escherichia coli and in chloroplasts, the G1 is genome-encoded and retained during tRNA maturation because of an unusual cleavage of the pre-tRNAHis at the (-1) position by RNase P. In Saccharomyces cerevisiae as well as in Drosophila melanogaster the G1 is not genome-encoded and must be post-transcriptionally added at the 5' terminus of the nuclear-encoded tRNAHis by a specific tRNAHis guanylyltransferase. In plant mitochondria, although trnH genes possess a G1 tRNAHis guanylyltransferase activity is present in plant mitochondria
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction, GTP is incorporated at the -1 position opposite the highly conserved A73 residue in eukaryotic tRNAHis
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction, GTP is incorporated at the -1 position opposite the highly conserved A73 residue in eukaryotic tRNAHis
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
-
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
-
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
-
-
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
-
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
-
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
-
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
Saccharomyces cerevisiae ATCC 2045083
overall reaction
-
-
?
additional information
?
-
the TLP from Bacillus thuringiensis (BtTLP) can utilize GTP to activate the 5'-end of tRNAHis in vitro, whereas bona fide Thg1 enzymes are so far strictly ATP-dependent for catalyzing this reaction
-
-
-
additional information
?
-
when full-length tRNAHis (lacking the G-1 residue) is used as a substrate, TLP exhibits a strong preference for use of GTP over ATP for 5'-end activation. Product formation is extremely slow in the presence of only ATP. With a 5'-truncated substrate missing the +1 nucleotide, both ATP and GTP are used with relatively equal efficiency for activation
-
-
?
additional information
?
-
TLPs exhibit a strong preference for adding WC-base paired nucleotides to RNA substrates
-
-
-
additional information
?
-
when full-length tRNAHis (lacking the G-1 residue) is used as a substrate, TLP exhibits a strong preference for use of GTP over ATP for 5'-end activation. Product formation is extremely slow in the presence of only ATP. With a 5'-truncated substrate missing the +1 nucleotide, both ATP and GTP are used with relatively equal efficiency for activation
-
-
?
additional information
?
-
TLPs exhibit a strong preference for adding WC-base paired nucleotides to RNA substrates
-
-
-
additional information
?
-
the TLP from Bacillus thuringiensis (BtTLP) can utilize GTP to activate the 5'-end of tRNAHis in vitro, whereas bona fide Thg1 enzymes are so far strictly ATP-dependent for catalyzing this reaction
-
-
-
additional information
?
-
kinetic analysis and substrate specificity, overview. GTP can be directly conjugated with 5'-triphosphorylated tRNAHis without ATP activation. UTP is a poor substrate. The reaction efficiency of GTP addition is affected by the structure of the opposite base at position 73. No activity with ATP, 8-oxo-GTP, isoGTP, and 8-bromo-GTP instead of GTP. The activity with CTP, 2-aminopurine, 7-deaza-GTP, ITP, and UTP depends on the tRNAHIs substrate identity
-
-
-
additional information
?
-
Thg1 recognizes tRNAHis through its GUG anticodon, as demonstrated by the ability of Thg1 to add G-1 to a mutagenized tRNAPhe that has been altered to contain the His anticodon (tRNAPheGUG) and subsequently validated through a cocrystal structure of Candida albicans Thg1 in complex with tRNAPheGUG. The coordination of tRNA molecules occurs in a molar ratio of 4:2, where two tRNA molecules bind a Thg1 tetramer in parallel orientation, and each tRNA is coordinated by three subunits of the tetramer. The enzyme performs 3' to 5' or reverse polymerization
-
-
-
additional information
?
-
Thg1 recognizes tRNAHis through its GUG anticodon, as demonstrated by the ability of Thg1 to add G-1 to a mutagenized tRNAPhe that has been altered to contain the His anticodon (tRNAPheGUG) and subsequently validated through a cocrystal structure of Candida albicans Thg1 in complex with tRNAPheGUG. The coordination of tRNA molecules occurs in a molar ratio of 4:2, where two tRNA molecules bind a Thg1 tetramer in parallel orientation, and each tRNA is coordinated by three subunits of the tetramer. The enzyme performs 3' to 5' or reverse polymerization
-
-
-
additional information
?
-
kinetic analysis and substrate specificity, overview. GTP can be directly conjugated with 5'-triphosphorylated tRNAHis without ATP activation. UTP is a poor substrate. The reaction efficiency of GTP addition is affected by the structure of the opposite base at position 73. No activity with ATP, 8-oxo-GTP, isoGTP, and 8-bromo-GTP instead of GTP. The activity with CTP, 2-aminopurine, 7-deaza-GTP, ITP, and UTP depends on the tRNAHIs substrate identity
-
-
-
additional information
?
-
TLPs exhibit a strong preference for adding WC-base paired nucleotides to RNA substrates
-
-
-
additional information
?
-
human Thg1 (hThg1) catalyzes the G-1 addition reaction for both human ctRNAHis and mtRNAHis through recognition of the anticodon. While hThg1 catalyzes consecutive GTP additions to mtRNAHis in vitr (consecutive G-2 and G-3 addition to pppG-1-hmtRNAHis), it does not exhibit any activity toward mature pG-1-mtRNAHis. hThg1 can add a GMP directly to the 5'-terminus of mtRNAHis in a template-dependent manner, but not to ctRNAHis. Acceleration of the diphosphate removal activity before or after the G-1 addition reaction is a key feature of hThg1 for maintaining a normal 5'-terminus of mtRNAHis in human mitochondria. The GUG to GAA conversion completely abolishes the ability of hThg1 to catalyze the adenylylation of both tRNAs, anticodon variants of hmtRNAHisGAA and hctRNAHis GAA, respetively, suggesting that hThg1 recognizes both of them in a His anticodon-dependent manner. The mobility of mtRNAHis is significantly faster than that of hctRNAHis on a native-PAGE gel, further suggesting a structural difference between them that is consistent with secondary structure predictions
-
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-
additional information
?
-
-
human Thg1 (hThg1) catalyzes the G-1 addition reaction for both human ctRNAHis and mtRNAHis through recognition of the anticodon. While hThg1 catalyzes consecutive GTP additions to mtRNAHis in vitr (consecutive G-2 and G-3 addition to pppG-1-hmtRNAHis), it does not exhibit any activity toward mature pG-1-mtRNAHis. hThg1 can add a GMP directly to the 5'-terminus of mtRNAHis in a template-dependent manner, but not to ctRNAHis. Acceleration of the diphosphate removal activity before or after the G-1 addition reaction is a key feature of hThg1 for maintaining a normal 5'-terminus of mtRNAHis in human mitochondria. The GUG to GAA conversion completely abolishes the ability of hThg1 to catalyze the adenylylation of both tRNAs, anticodon variants of hmtRNAHisGAA and hctRNAHis GAA, respetively, suggesting that hThg1 recognizes both of them in a His anticodon-dependent manner. The mobility of mtRNAHis is significantly faster than that of hctRNAHis on a native-PAGE gel, further suggesting a structural difference between them that is consistent with secondary structure predictions
-
-
-
additional information
?
-
the enzyme performs 3' to 5' or reverse polymerization
-
-
-
additional information
?
-
-
Thg1 activity assay with 5'-triphosphorylated tRNAHis
-
-
-
additional information
?
-
IhTLP is catalytically active in vitro, and catalyzes a significant tRNA repair reaction in vitro, adding up to 13 nucleotides to restore a truncated tRNAHis
-
-
-
additional information
?
-
the enzyme is active in an in vitro activity assay with radiolabelled Escherichia coli tRNAHisDG-1 and recombinant wild-type IhThg1 enzyme. IhThg1 displays reduced enzyme activity with yeast tRNAHisDG-1, which encodes an A73 discriminator base in compared to Escherichia coli tRNAHisDG-1 with a C73 discriminator base. Radioactive product formation is observed in the presence or absence of ATP, suggesting that IhThg1 does not require ATP-dependent activation, but can utilize GTP, as observed for other archaeal-type Thg1 enzymes. . Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. IhThg1 is active despite lacking conserved RNA recognition motifs. The palm domain of Thg1 is sufficient for catalytic activity
-
-
-
additional information
?
-
-
the enzyme is active in an in vitro activity assay with radiolabelled Escherichia coli tRNAHisDG-1 and recombinant wild-type IhThg1 enzyme. IhThg1 displays reduced enzyme activity with yeast tRNAHisDG-1, which encodes an A73 discriminator base in compared to Escherichia coli tRNAHisDG-1 with a C73 discriminator base. Radioactive product formation is observed in the presence or absence of ATP, suggesting that IhThg1 does not require ATP-dependent activation, but can utilize GTP, as observed for other archaeal-type Thg1 enzymes. . Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. IhThg1 is active despite lacking conserved RNA recognition motifs. The palm domain of Thg1 is sufficient for catalytic activity
-
-
-
additional information
?
-
IhTLP is catalytically active in vitro, and catalyzes a significant tRNA repair reaction in vitro, adding up to 13 nucleotides to restore a truncated tRNAHis
-
-
-
additional information
?
-
IhTLP is catalytically active in vitro, and catalyzes a significant tRNA repair reaction in vitro, adding up to 13 nucleotides to restore a truncated tRNAHis
-
-
-
additional information
?
-
IhTLP is catalytically active in vitro, and catalyzes a significant tRNA repair reaction in vitro, adding up to 13 nucleotides to restore a truncated tRNAHis
-
-
-
additional information
?
-
enzyme activity assay with purified recombinant palm domains from Methanosarcina acetivorans Thg1 (MaPalm, amino acids 1-141) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. The palm domain of Thg1 is sufficient for catalytic activity
-
-
-
additional information
?
-
-
enzyme activity assay with purified recombinant palm domains from Methanosarcina acetivorans Thg1 (MaPalm, amino acids 1-141) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. The palm domain of Thg1 is sufficient for catalytic activity
-
-
-
additional information
?
-
the TLP from Myxococcus xanthus (MxTLP) can utilize GTP to activate the 5'-end of tRNAHis in vitro, whereas bona fide Thg1 enzymes are so far strictly ATP-dependent for catalyzing this reaction
-
-
-
additional information
?
-
the TLP from Myxococcus xanthus (MxTLP) can utilize GTP to activate the 5'-end of tRNAHis in vitro, whereas bona fide Thg1 enzymes are so far strictly ATP-dependent for catalyzing this reaction
-
-
-
additional information
?
-
enzyme activity assay with purified recombinant palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. PaThg1 repairs truncated tRNA substrates. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. PaThg1 adds a single nucleotide to the guide RNAs and also to the control hammerhead ribozyme RNAs in the presence or absence of target RNAs. The palm domain of Thg1 is sufficient for catalytic activity
-
-
-
additional information
?
-
-
enzyme activity assay with purified recombinant palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. PaThg1 repairs truncated tRNA substrates. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. PaThg1 adds a single nucleotide to the guide RNAs and also to the control hammerhead ribozyme RNAs in the presence or absence of target RNAs. The palm domain of Thg1 is sufficient for catalytic activity
-
-
-
additional information
?
-
enzyme activity assay with purified recombinant palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. PaThg1 repairs truncated tRNA substrates. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. PaThg1 adds a single nucleotide to the guide RNAs and also to the control hammerhead ribozyme RNAs in the presence or absence of target RNAs. The palm domain of Thg1 is sufficient for catalytic activity
-
-
-
additional information
?
-
enzyme activity assay with purified recombinant palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. PaThg1 repairs truncated tRNA substrates. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. PaThg1 adds a single nucleotide to the guide RNAs and also to the control hammerhead ribozyme RNAs in the presence or absence of target RNAs. The palm domain of Thg1 is sufficient for catalytic activity
-
-
-
additional information
?
-
enzyme activity assay with purified recombinant palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. PaThg1 repairs truncated tRNA substrates. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. PaThg1 adds a single nucleotide to the guide RNAs and also to the control hammerhead ribozyme RNAs in the presence or absence of target RNAs. The palm domain of Thg1 is sufficient for catalytic activity
-
-
-
additional information
?
-
enzyme activity assay with purified recombinant palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. PaThg1 repairs truncated tRNA substrates. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. PaThg1 adds a single nucleotide to the guide RNAs and also to the control hammerhead ribozyme RNAs in the presence or absence of target RNAs. The palm domain of Thg1 is sufficient for catalytic activity
-
-
-
additional information
?
-
enzyme activity assay with purified recombinant palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150) incubated with radiolabelled Escherichia coli tRNAHisDELTAG-1 and GTP. PaThg1 repairs truncated tRNA substrates. Substrate specificity analysis with tRNAHis substrates differing in the discrimination position 73, and different nucleotides, i.e. radiolabelled GTP and unlabeled GTP, ATP, UTP, and CTP, analysis of Thg1 sequence determinants for extended reverse polymerization. PaThg1 adds a single nucleotide to the guide RNAs and also to the control hammerhead ribozyme RNAs in the presence or absence of target RNAs. The palm domain of Thg1 is sufficient for catalytic activity
-
-
-
additional information
?
-
in vivo Thg1 catalyzes 3'5' polymerization on tRNAHisC73, but not on tRNAHisA73
-
-
?
additional information
?
-
-
in vivo Thg1 catalyzes 3'5' polymerization on tRNAHisC73, but not on tRNAHisA73
-
-
?
additional information
?
-
-
the enzyme also catalyzes 3'-5' extension of a polynucleotude chain by multiple nucleotides. Unlike the addition of G(-1), the reverse polymerisation activity is template-dependent, recognizing G*C WatsonCrick base pairs. Moreover, reverse polymerization is not specific for tRNAHis or for starting at the (-1) position of tRNA, provided that the activated (triphosphorylated) form of the tRNA substrate is used in the assays
-
-
?
additional information
?
-
retention of the 5'-triphosphate is correlated with efficient 3'-5' reverse polymerization. The intrinsic rate of removal of diphosphate from the G-1 residue of base-paired tRNAHis substrates is slow. Rates of diphosphate removal depend on the identity of the NTP included in reactions. The GTP 3'-OH is required to stimulate diphosphate removal
-
-
?
additional information
?
-
-
retention of the 5'-triphosphate is correlated with efficient 3'-5' reverse polymerization. The intrinsic rate of removal of diphosphate from the G-1 residue of base-paired tRNAHis substrates is slow. Rates of diphosphate removal depend on the identity of the NTP included in reactions. The GTP 3'-OH is required to stimulate diphosphate removal
-
-
?
additional information
?
-
the enzyme performs 3' to 5' or reverse polymerization
-
-
-
additional information
?
-
the GTP molecule is clearly bound at the active site, coordinating with two magnesium ions
-
-
-
additional information
?
-
-
the GTP molecule is clearly bound at the active site, coordinating with two magnesium ions
-
-
-
additional information
?
-
tRNAHis guanylyltransferase clearly prefers a substrate carrying a CCA terminus. The 3'-CCA triplet and a discriminator position A73 act as positive elements for G-1 incorporation, ensuring the fidelity of G-1 addition. On the substrate lacking the CCA-end (tRNAHisDELTACCA), the enzyme is less efficient
-
-
-
additional information
?
-
-
tRNAHis guanylyltransferase clearly prefers a substrate carrying a CCA terminus. The 3'-CCA triplet and a discriminator position A73 act as positive elements for G-1 incorporation, ensuring the fidelity of G-1 addition. On the substrate lacking the CCA-end (tRNAHisDELTACCA), the enzyme is less efficient
-
-
-
additional information
?
-
the enzyme performs 3' to 5' or reverse polymerization
-
-
-
additional information
?
-
tRNAHis guanylyltransferase clearly prefers a substrate carrying a CCA terminus. The 3'-CCA triplet and a discriminator position A73 act as positive elements for G-1 incorporation, ensuring the fidelity of G-1 addition. On the substrate lacking the CCA-end (tRNAHisDELTACCA), the enzyme is less efficient
-
-
-
additional information
?
-
Saccharomyces cerevisiae ATCC 2045083
the GTP molecule is clearly bound at the active site, coordinating with two magnesium ions
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
p-ctRNAHis + ATP + GTP + H2O
pGp-ctRNAHis + AMP + 2 diphosphate
cytoplasmic tRNAHis
-
-
?
p-mtRNAHis + ATP + GTP + H2O
pGp-mtRNAHis + AMP + 2 diphosphate
mitochondrial tRNAHis
-
-
?
p-tRNAHis + ATP + GTP
pppG-p-tRNAHis + AMP + diphosphate
the extra nucleotide in position -1 of mitochondrial and eukaryotic cytoplasmic tRNAHis molecules is added posttranscriptionally to the 5' end of the tRNA by a histidine-tRNA specific guanylyltransferase
-
-
?
p-tRNAHis + ATP + GTP
pppGp-tRNAHis + AMP + diphosphate
-
-
-
?
p-tRNAHis + ATP + GTP
pppGp-tRNAHis + AMP + diphosphate
the G(-1) residue is both necessary and sufficient for aminoacylation of tRNA by histidyl-tRNA synthetase in vitro and is required for aminoacylation in vivo
-
-
?
p-tRNAHis + ATP + GTP
pppGp-tRNAHis + AMP + diphosphate
-
all tRNAHis possess an essential extra G1 guanosine residue at their 5' end. This extra guanylate residue can be generated via two different processes. In Escherichia coli and in chloroplasts, the G1 is genome-encoded and retained during tRNA maturation because of an unusual cleavage of the pre-tRNAHis at the (-1) position by RNase P. In Saccharomyces cerevisiae as well as in Drosophila melanogaster the G1 is not genome-encoded and must be post-transcriptionally added at the 5' terminus of the nuclear-encoded tRNAHis by a specific tRNAHis guanylyltransferase. In plant mitochondria, although trnH genes possess a G1 tRNAHis guanylyltransferase activity is present in plant mitochondria
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
-
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
-
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
-
-
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
-
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
-
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
overall reaction
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
-
-
-
?
p-tRNAHis + ATP + GTP + H2O
pGp-tRNAHis + AMP + 2 diphosphate
Saccharomyces cerevisiae ATCC 2045083
overall reaction
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
archaeal-type Thg1 enzymes are ATP-independent. Product formation is observed in the presence or absence of ATP, suggesting that IhThg1 does not require ATP-dependent activation, but can utilize GTP, as observed for other archaeal-type Thg1 enzymes
ATP
eukaryotic Thg1 enzymes require ATP for substrate activation
ATP
GTP can be directly conjugated with 5'-triphosphorylated tRNAHis without ATP activation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
the requirement for a divalent metal ion can be satisfied by Mg2+, Mn2+, and to a lesser extent by Co2+ and Zn2+. Activity in presence of 10 mM Co2+ is 13% compared to the activity in presence of 10 mM Mg2+
Mg2+
Mn2+
the requirement for a divalent metal ion can be satisfied by Mg2+, Mn2+, and to a lesser extent by Co2+ and Zn2+. Activity in presence of 10 mM Mn2+ is 70% compared to the activity in presence of 10 mM Mg2+
Zn2+
the requirement for a divalent metal ion can be satisfied by Mg2+, Mn2+, and to a lesser extent by Co2+ and Zn2+. Activity in presence of 10 mM Zn2+ is 15% compared to the activity in presence of 10 mM Mg2+
Mg2+
the dGTP-bound crystal structure reveales two bound Mg2+ ions associated with the nucleoside triphosphate. The distance between the two metal ions is 4.3 A. The two hTHG1 aspartates (D29 and D76) coordinate the two divalent metal ions, whereas E77 points away from the metals
Mg2+
required for ATPase activity, the 5'-triphosphophate of the incoming GTP is coordinated with a Mg2+ ion
Mg2+
the requirement for a divalent metal ion can be satisfied by Mg2+, Mn2+, and to a lesser extent by Co2+ and Zn2+. Maximal activity by 10 mM Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic)acid
progressive loss of activity with increasing amounts of DTNB. Thus, sulfhydryl groups are involved in maintaining the active state of the enzyme or are involved in the mechanism
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Diseases
Severe epileptic encephalopathy associated with compound heterozygosity of THG1L variants in the Ashkenazi Jewish population.
Cerebellar Ataxia
A mutation in the THG1L gene in a family with cerebellar ataxia and developmental delay.
Cerebellar Ataxia
Refining the phenotype of the THG1L (p.Val55Ala mutation)-related mitochondrial autosomal recessive congenital cerebellar ataxia.
Cerebellar Diseases
Refining the phenotype of the THG1L (p.Val55Ala mutation)-related mitochondrial autosomal recessive congenital cerebellar ataxia.
Cerebellar Diseases
Severe epileptic encephalopathy associated with compound heterozygosity of THG1L variants in the Ashkenazi Jewish population.
Dysarthria
A mutation in the THG1L gene in a family with cerebellar ataxia and developmental delay.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
analysis of G-1 incorporation on tRNAHis A73C variants with and without 3'-CCA-end shows significant preference of Thg1 for tRNAHis containing the 3'-CCA, both in terms of rate and maximal amount of product formed in the reactions, kinetic analysis
-
additional information
additional information
-
analysis of G-1 incorporation on tRNAHis A73C variants with and without 3'-CCA-end shows significant preference of Thg1 for tRNAHis containing the 3'-CCA, both in terms of rate and maximal amount of product formed in the reactions, kinetic analysis
-
additional information
additional information
kinetic analysis and substrate specificity. Observed rate constants (kobs) of natural NTP or GTP analogues to pppP4 complexed with T3 are measured under single turnover conditions. The reaction efficiency of GTP addition is affected by the structure of the opposite base at position 73, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kobs for several substrate analogues, overview
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Caenorhabditis elegans
Caenorhabditis elegans is a Thg1-independent organism, its cytoplasmic tRNAHis (CetRNAnHis) retains a genome-encoded G-1, and ts mitochondrial tRNAHis (CetRNAmHis) uniquely lacks G-1. This eukaryote possesses a histidyl-tRNA synthetase (CeHisRS) gene encoding two distinct HisRS isoforms (EC 6.1.1.21) that differ only at their N-termini
-
-
brenda
cv. TeQing (TQ), cultivated in fields in Shanghai and Hainan
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
mammalian Thg1 is localized to both the cytoplasm and mitochondria
-
brenda
additional information
-
mammalian Thg1 is localized to both the cytoplasm and mitochondria
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
implications for the evolution of eukaryotic Thg1 from a family of ancestral promiscuous RNA repair enzymes to the highly selective enzymes needed for their essential function in tRNAHis maturation. The HisRS requirement for Gx031 is a conserved feature throughout all domains of life, but bacteria and eukaryotes have evolved different mechanisms of incorporating the additionalx031 nucleotide into tRNAHis. Most eukaryotes studied to date incorporate G-1 posttranscriptionally to the processed 5' end of tRNAHis. This posttranscriptional addition of G-1 is performed by the tRNAHis guanylyltransferase (Thg1). Eukaryotic Thg1 enzymes are strictly specific for tRNAHis, and this specificity is accomplished by recognition of the tRNAHis GUG anticodon
evolution
the active site moiety of ScThg1 is highly conserved among members of the Thg1 family, comparisons of structure ana binding modes, overview
evolution
the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1
evolution
the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1. Thg1 is evolutionarily related to canonical 5'-3' forward polymerases but catalyzes reverse 3'-5' polymerization. Similar to its forward polymerase counterparts, Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
evolution
the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1. Thg1 is evolutionarily related to canonical 5'-3' forward polymerases but catalyzes reverse 3'-5' polymerization. Similar to its forward polymerase counterparts, Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
evolution
the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1. Thg1 is evolutionarily related to canonical 5'-3' forward polymerases but catalyzes reverse 3'-5' polymerization. Similar to its forward polymerase counterparts, Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity. Naturally occurring Thg1 enzyme from Ignicoccus hospitalis (IhThg1) lacks several sections of the protein, and aligns poorly with other Thg1 sequences, it is identified in a large Thg1 phylogenetic analysis
evolution
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview
evolution
-
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
evolution
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
evolution
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
evolution
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
evolution
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
evolution
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
evolution
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
evolution
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
evolution
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
evolution
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
evolution
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
evolution
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
evolution
tRNAHis guanylyltransferase (Thg1) specifies eukaryotic tRNAHis identity by catalyzing a 3' to 5' non-Watson Crick (WC) addition of guanosine to the 5'-end of tRNAHis. Thg1 family enzymes in Archaea and Bacteria, called Thg1-like-proteins (TLPs), catalyze a similar but distinct 3' to 5' addition in an exclusively WC-dependent manner
evolution
tRNAHis guanylyltransferase (Thg1) specifies eukaryotic tRNAHis identity by catalyzing a 3' to 5' non-Watson Crick (WC) addition of guanosine to the 5'-end of tRNAHis. Thg1 homologs known as Thg1-like proteins (TLPs) are found in all three domains of life and are biochemically distinct from Thg1. Thg1 family enzymes in Archaea and Bacteria, called Thg1-like-proteins (TLPs), catalyze a similar but distinct 3' to 5' addition in an exclusively WC-dependent manner, alternative non-tRNAHis-related functions for these enzymes , overview
evolution
tRNAHis guanylyltransferase (Thg1) specifies eukaryotic tRNAHis identity by catalyzing a 3' to 5' non-Watson Crick (WC) addition of guanosine to the 5'-end of tRNAHis. Thg1 homologs known as Thg1-like proteins (TLPs) are found in all three domains of life and are biochemically distinct from Thg1. Thg1 family enzymes in Archaea and Bacteria, called Thg1-like-proteins (TLPs), catalyze a similar but distinct 3' to 5' addition in an exclusively WC-dependent manner, alternative non-tRNAHis-related functions for these enzymes, overview
evolution
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the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
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evolution
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the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
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evolution
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the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1. Thg1 is evolutionarily related to canonical 5'-3' forward polymerases but catalyzes reverse 3'-5' polymerization. Similar to its forward polymerase counterparts, Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
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evolution
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the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1. Thg1 is evolutionarily related to canonical 5'-3' forward polymerases but catalyzes reverse 3'-5' polymerization. Similar to its forward polymerase counterparts, Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
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evolution
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the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
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evolution
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the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
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evolution
-
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
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evolution
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the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
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evolution
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the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
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evolution
-
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
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evolution
-
tRNAHis guanylyltransferase (Thg1) specifies eukaryotic tRNAHis identity by catalyzing a 3' to 5' non-Watson Crick (WC) addition of guanosine to the 5'-end of tRNAHis. Thg1 family enzymes in Archaea and Bacteria, called Thg1-like-proteins (TLPs), catalyze a similar but distinct 3' to 5' addition in an exclusively WC-dependent manner
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evolution
-
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
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evolution
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the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1
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evolution
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the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
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evolution
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the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
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evolution
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the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1. Thg1 is evolutionarily related to canonical 5'-3' forward polymerases but catalyzes reverse 3'-5' polymerization. Similar to its forward polymerase counterparts, Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
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evolution
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the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
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evolution
-
the tRNAHis guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity is the reverse of all other known DNA and RNA polymerases. Forward 5' to 3' and reverse 3' to 5' polymerization are mechanistically similar. In bacteria and many archaea, the G-1 residue is genomically encoded and transcribed in the precursor tRNA transcript, and subsequent cleavage of the 5' leader sequence by ribonuclease P (RNase P) yields a mature tRNAHis with its identity-establishing G-1 element (tRNAHisG-1). Different pathways to establish tRNAHis identity, overview. Thg1-like proteins function in tRNA repair, TLPs in bacteria and archaea, structural comparison of Thg1 and TLPs. TLPs exhibit broader RNA recognition properties than Thg1 homologues
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evolution
-
the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1. Thg1 is evolutionarily related to canonical 5'-3' forward polymerases but catalyzes reverse 3'-5' polymerization. Similar to its forward polymerase counterparts, Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
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evolution
-
the archaeal type Thg1, which includes most archaeal and bacterial Thg1 enzymes, is phylogenetically distant from eukaryotic Thg1. Thg1 is evolutionarily related to canonical 5'-3' forward polymerases but catalyzes reverse 3'-5' polymerization. Similar to its forward polymerase counterparts, Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
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evolution
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tRNAHis guanylyltransferase (Thg1) specifies eukaryotic tRNAHis identity by catalyzing a 3' to 5' non-Watson Crick (WC) addition of guanosine to the 5'-end of tRNAHis. Thg1 homologs known as Thg1-like proteins (TLPs) are found in all three domains of life and are biochemically distinct from Thg1. Thg1 family enzymes in Archaea and Bacteria, called Thg1-like-proteins (TLPs), catalyze a similar but distinct 3' to 5' addition in an exclusively WC-dependent manner, alternative non-tRNAHis-related functions for these enzymes , overview
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evolution
Saccharomyces cerevisiae ATCC 2045083
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the active site moiety of ScThg1 is highly conserved among members of the Thg1 family, comparisons of structure ana binding modes, overview
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malfunction
a thg1DELTA strain is only viable in the presence of a functional version of the G-1 addition enzyme supplied on a covering plasmid. Using this system, different archaeal TLPs are not able to support growth of the thg1DELTA strain, and only strains that also simultaneously express a mutant form of tRNAHis (C73-tRNAHis), enabling WC-dependent addition of G-1, are viable. BtTLP is able to carry out the essential activity ScThg1 in vivo in Saccharomyces cerevisiae, but this apparent function contradicts the strong preference for WC base-paired nucleotide addition exhibited by BtTLP in vitro. BtTLP catalyzes its biochemically preferred WC-dependent reaction, possibly adding U-1 to this A73-containing tRNA, mechanism, overview
malfunction
an aet1 mutant shows loss of Thg1 enzyme function, leading to reduced aminoacyl-tRNAHis levels and translational efficiency. The mutant plants display slight phenotype changes under normal conditions. The translational status remains unaffected in the aet1 mutant, but the translational efficiency of OsARF19 and OsARF23 is reduced. Moreover, OsARF23 protein levels are obviously decreased in the aet1 mutant under high temperature, implying that AET1 regulates auxin signaling in response to high temperature
malfunction
Dictyostelium discoideum Ddditlp2 deletion strains are viable, but completely lack the G-1 nucleotide on the mt-tRNAHis
malfunction
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His152Ala and Lys187Ala mutant variants maintain a similar overall interaction with the anticodon region, arguing against the sufficiency of this interaction for driving catalysis. Instead, conservative mutagenesis reveals a distinct direct function for these residues in recognition of a non-Watson-Crick Gx021:A73 bp. tRNAHis anticodon interaction analysis in comparison to the wild-type, overview. The mutant Thg1 variants perform non-WC nucleotidyl transfer on pre-activated tRNA substrate p*pptRNAHis
malfunction
identification of residues in yeast Thg1 that play a part in preventing extended polymerization. Mutation of these residues with alanine results in extended reverse polymerization
malfunction
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a thg1DELTA strain is only viable in the presence of a functional version of the G-1 addition enzyme supplied on a covering plasmid. Using this system, different archaeal TLPs are not able to support growth of the thg1DELTA strain, and only strains that also simultaneously express a mutant form of tRNAHis (C73-tRNAHis), enabling WC-dependent addition of G-1, are viable. BtTLP is able to carry out the essential activity ScThg1 in vivo in Saccharomyces cerevisiae, but this apparent function contradicts the strong preference for WC base-paired nucleotide addition exhibited by BtTLP in vitro. BtTLP catalyzes its biochemically preferred WC-dependent reaction, possibly adding U-1 to this A73-containing tRNA, mechanism, overview
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malfunction
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identification of residues in yeast Thg1 that play a part in preventing extended polymerization. Mutation of these residues with alanine results in extended reverse polymerization
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metabolism
a bona fide Thg1 (DdiThg1), catalyzes the G-1 addition to tRNAHis, and thus establishes tRNAHis identity. The remaining three genes are characterized by sequence similarity and phylogeny as TLPs. Two of these TLPs (DdiTLP2 and DdiTLP3) are mitochondrial enzymes that catalyze distinct and non-redundant functions to add G-1 to mitochondrial tRNAHis (DdiTLP2) or to repair the 5'-end of mitochondrial tRNA (mt-tRNA) during a process known as tRNA 5'-editing (DdiTLP3)
metabolism
a bona fide Thg1 (DdiThg1), catalyzes the G-1 addition to tRNAHis, and thus establishes tRNAHis identity. The remaining three genes are characterized by sequence similarity and phylogeny as TLPs. Two of these TLPs (DdiTLP2 and DdiTLP3) are mitochondrial enzymes that catalyze distinct and non-redundant functions to add G-1 to mitochondrial tRNAHis (DdiTLP2) or to repair the 5'-end of mitochondrial tRNA (mt-tRNA) during a process known as tRNA 5'-editing (DdiTLP3). DdiTLP3's role in tRNA 5'-editing also utilizes 3' to 5' polymerase function, but to repair mt-tRNA that have been truncated at their 5'-ends due to the removal of one or more incorrectly base-paired nucleotides encoded in the precursor tRNA
metabolism
in eukaryotes including yeast, both 3'-CCA and 5'-G-1 are added posttranscriptionally by tRNA nucleotidyltransferase and tRNAHis guanylyltransferase, respectively. These two cytosolic enzymes might compete for the same tRNA, but tRNAHis guanylyltransferase clearly prefers a substrate carrying a CCA terminus. Thus, although many tRNA maturation steps can occur in a rather random order, pathway where CCA-addition precedes G-1 incorporation is likely in Saccharomyces cerevisiae. The 3'-CCA triplet and a discriminator position A73 act as positive elements for G-1 incorporation, ensuring the fidelity of G-1 addition. Sequential order of tRNAHis processing, overview. The enzymes do not compete for the substrate. Instead, the differing substrate preferences lead to a sequential order of nucleotide incorporation at 5'- and 3'-ends, resulting in a mature tRNAHis in the cytosol
metabolism
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in eukaryotes including yeast, both 3'-CCA and 5'-G-1 are added posttranscriptionally by tRNA nucleotidyltransferase and tRNAHis guanylyltransferase, respectively. These two cytosolic enzymes might compete for the same tRNA, but tRNAHis guanylyltransferase clearly prefers a substrate carrying a CCA terminus. Thus, although many tRNA maturation steps can occur in a rather random order, pathway where CCA-addition precedes G-1 incorporation is likely in Saccharomyces cerevisiae. The 3'-CCA triplet and a discriminator position A73 act as positive elements for G-1 incorporation, ensuring the fidelity of G-1 addition. Sequential order of tRNAHis processing, overview. The enzymes do not compete for the substrate. Instead, the differing substrate preferences lead to a sequential order of nucleotide incorporation at 5'- and 3'-ends, resulting in a mature tRNAHis in the cytosol
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physiological function
both isoforms TLP1 and TLP2 lack the ability to catalyze efficient G1 addition to cytosolic tRNAHis in vitro and catalyse template-dependent 3'-5' polymerase activity. Both TLP1 and TLP2 exhibit tRNA repair of 5'-edited mt-tRNAs
physiological function
the diphosphate removal activity under all conditions preferentially acts upon tRNAs containing a U-1:A73 terminating base pair. Although Thg1 can add UTP to create a U:A base pair, it efficiently removes the activated 5'-end from this added nucleotide and effectively terminates subsequent addition reactions. Thg1 exhibits 3'-5' polymerization with some tRNA substrates, but addition of a nucleotide at the -1 position is the preferred reaction
physiological function
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enzyme tRNAHis guanylyltransferase (Thg1) adds a single guanine to the-1 position of tRNAHis as part of its maturation. This seemingly modest addition of one nucleotide to tRNAHis ensures translational fidelity by providing a critical identity element for the histidyl aminoacyl tRNA synthetase (HisRS). Like HisRS, Thg1 utilizes the GUG anticodon for selective tRNAHis recognition, and Thg1-tRNA complex structures have revealed conserved residues that interact with anticodon nucleotides
physiological function
mammalian mitochondrial tRNAHis (mtRNAHis) is matured by tRNAHis guanylyltransferase through posttranscriptional addition of guanosine at the -1 position (G-1), which serves as an identity element for mitochondrial histidyl-tRNA synthetase. In cytoplasmic tRNAHis (ctRNAHis) maturation, tRNAHis guanylyltransferase (Thg1) adds a GTP onto the 5'-terminal of ctRNAHis and then removes the 5'-diphosphate to yield the mature 5'-monophospholylated G-1-ctRNAHis (pG-1-ctRNAHis). Analysis of the differences between tRNAHis maturation in the cytoplasm and mitochondria of humans, overview
physiological function
the eukaryotic slime mold Dictyostelium discoideum is revealed to require a similar tRNA 5'-end repair reaction to repair mitochondrial tRNAs during a process known as tRNA 5'-editing. This reaction is catalyzed by one of the Dictyostelium discoideum TLPs (DdiTLP3) and represents the second established biological function for the 3'-5' polymerase activity of Thg1/TLP enzymes
physiological function
the tRNAHis guanylyltransferase posttranscriptionally adds a 5'-G-1 from GTP to yeast tRNAHis. The presence of this single G at the -1 position is critical for recognition of tRNAHis by the histidyl-tRNA synthetase (HisRS). Thg1 adds a single G-1 residue across from an A73 discriminator nucleotide, forming an unconventional non-Watson Crick base pair. This unusual 3'-5' nucleotidyltransferase protein is a member of a larger family of Watson Crick-dependent 3'-5' polymerase enzymes that share structural similarity with canonical 5'-3' DNA and RNA polymerases
physiological function
TLP homologues differ in terms of the number of nucleotide additions that are observed in vitro with tRNA transcripts mimicking the mature tRNAHis that can be a substrate for this kind of activity in vivo. The ability to add multiple 50-nucleotides to these types of tRNAHis is a direct consequence of the presence of a C73 discriminator, which results in the formation of three consecutive C-nucleotides in the 3'-C73CCA end. These types of substrates are initially shown to cause multiple G-addition reactions even in the context of eukaryotic Thg1, and several bacterial/archaeal homologues
physiological function
TLP homologues differ in terms of the number of nucleotide additions that are observed in vitro with tRNA transcripts mimicking the mature tRNAHis that can be a substrate for this kind of activity in vivo. The ability to add multiple 50-nucleotides to these types of tRNAHis is a direct consequence of the presence of a C73 discriminator, which results in the formation of three consecutive C-nucleotides in the 3'-C73CCA end. These types of substrates are initially shown to cause multiple G-addition reactions even in the context of eukaryotic Thg1, and several bacterial/archaeal homologues
physiological function
TLP homologues differ in terms of the number of nucleotide additions that are observed in vitro with tRNA transcripts mimicking the mature tRNAHis that can be a substrate for this kind of activity in vivo. The ability to add multiple 50-nucleotides to these types of tRNAHis is a direct consequence of the presence of a C73 discriminator, which results in the formation of three consecutive C-nucleotides in the 3'-C73CCA end. These types of substrates are initially shown to cause multiple G-addition reactions even in the context of eukaryotic Thg1, and several bacterial/archaeal homologues
physiological function
TLP homologues differ in terms of the number of nucleotide additions that are observed in vitro with tRNA transcripts mimicking the mature tRNAHis that can be a substrate for this kind of activity in vivo. The ability to add multiple 50-nucleotides to these types of tRNAHis is a direct consequence of the presence of a C73 discriminator, which results in the formation of three consecutive C-nucleotides in the 3'-C73CCA end. These types of substrates are initially shown to cause multiple G-addition reactions even in the context of eukaryotic Thg1, and several bacterial/archaeal homologues
physiological function
TLP homologues differ in terms of the number of nucleotide additions that are observed in vitro with tRNA transcripts mimicking the mature tRNAHis that can be a substrate for this kind of activity in vivo. The ability to add multiple 50-nucleotides to these types of tRNAHis is a direct consequence of the presence of a C73 discriminator, which results in the formation of three consecutive C-nucleotides in the 3'-C73CCA end. These types of substrates are initially shown to cause multiple G-addition reactions even in the context of eukaryotic Thg1, and several bacterial/archaeal homologues. DdiTLP2 does not use the tRNAHis GUG anticodon to recognize the tRNA for the addition of the G-1 nucleotide. The reaction catalyzed by DdiTLP2 is not essential for specifying tRNAHis identity, since Dictyostelium discoideum Ddditlp2 deletion strains are viable, but completely lack the G-1 nucleotide on the mt-tRNAHis
physiological function
TLP homologues differ in terms of the number of nucleotide additions that are observed in vitro with tRNA transcripts mimicking the mature tRNAHis that can be a substrate for this kind of activity in vivo. The ability to add multiple 50-nucleotides to these types of tRNAHis is a direct consequence of the presence of a C73 discriminator, which results in the formation of three consecutive C-nucleotides in the 3'-C73CCA end. These types of substrates are initially shown to cause multiple G-addition reactions even in the context of eukaryotic Thg1, and several bacterial/archaeal homologues. The third TLP encoded in Dictyostelium discoideum (DdiTLP4) catalyzes an essential function
physiological function
translational regulation of plant response to high temperature by a rice dual-function tRNAHis guanylyltransferase AET1, which contributes to the modification of pre-tRNAHis and is required for normal growth under high-temperature conditions in rice. AET1 possibly interacts with both RACK1A and eIF3h in the endoplasmic reticulum. AET1 can directly bind to OsARF mRNAs including the uORFs of OsARF19 and OsARF23, indicating that AET1 is associated with translation regulation. AET1 regulates auxin signaling in response to high temperature. AET1 regulates the environmental temperature response in rice by playing a dual role in tRNA modification and translational control. AET1 modulates auxin signaling through translation regulation associated with tRNA modification under high temperature, molecular mechanism, detailed overview. Under high temperature, AET1 can activate pre-tRNAHis and stabilize tRNA homeostasis. In particular, AET1 interacts with RACK1A and eIF3h and associates with the OsARF19 and OsARF23 mRNAs, which leads to increased translation of these mRNAs and contributes to plant development in response to high temperature
physiological function
tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life
physiological function
tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life
physiological function
tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life. Most eukaryotic Thg1 homologs are essential genes involved in tRNAHis maturation. These enzymes normally catalyze a single 5' guanylation of tRNAHis lacking the essential G-1 identity element required for aminoacylation. G-1 is the critical identity element that histidyl-tRNA synthetase (HisRS) uses to recognize its cognate tRNA, enabling HisRS to differentiate tRNAHis from the pool of other cellular tRNAs
physiological function
tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life. PaThg1 catalyzes extended, template dependent tRNA repair, adding up to 13 nucleotides to a truncated tRNAHis substrate. PaThg1 fully restores the near correct sequence of the D- and acceptor stem, but also produces incompletely and incorrectly repaired tRNA products
physiological function
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. Histidyl-tRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element
physiological function
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. Histidyl-tRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element
physiological function
-
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. Histidyl-tRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element. The enzyme homologue from Methanothermobacter thermoautotrophicus appears to limit nucleotide addition to only a single guanine addition, despite the presence of an extended C-template at the tRNA 3'-end
physiological function
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. Histidyl-tRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element. The enzyme homologue from Methanothermobacter thermoautotrophicus appears to limit nucleotide addition to only a single guanine addition, despite the presence of an extended C-template at the tRNA 3'-end
physiological function
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. Histidyl-tRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element. The enzyme homologue from Methanothermobacter thermoautotrophicus appears to limit nucleotide addition to only a single guanine addition, despite the presence of an extended C-template at the tRNA 3'-end
physiological function
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. HistidyltRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element
physiological function
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. HistidyltRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element
physiological function
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. HistidyltRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element
physiological function
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. HistidyltRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element
physiological function
tRNAHis guanylyltransferase (Thg1) specifies eukaryotic tRNAHis identity by catalyzing a 3' to 5' non-Watson Crick (WC) addition of guanosine to the 5'-end of tRNAHis. Thg1 family enzymes in Archaea and Bacteria, called Thg1-like-proteins (TLPs), catalyze a similar but distinct 3' to 5' addition in an exclusively WC-dependent manner. Bacillus thuringiensis TLP sustains growth of a thg1DELTA strain by maintaining a WC-dependent addition of U-1 across from A73. The bacterial TLP from Bacillus thuringiensis, (BtTLP) repairs 5'-end truncated tRNAs in vitro, adding missing 5'-nucleotides using nucleotides in the 3'-half of the aminoacyl-acceptor stem as a template to restore WC base pairing. BtTLP is able to carry out the essential activity ScThg1 in vivo in Saccharomyces cerevisiae, but this apparent function contradicts the strong preference for WC base-paired nucleotide addition exhibited by BtTLP in vitro. BtTLP catalyzes its biochemically preferred WC-dependent reaction, possibly adding U-1 to this A73-containing tRNA. It is suggested that BtTLP is not catalyzing detectable activity on other RNAs in this system, overview
physiological function
tRNAHis guanylyltransferase (Thg1) specifies eukaryotic tRNAHis identity by catalyzing a 3' to 5' non-Watson Crick (WC) addition of guanosine to the 5'-end of tRNAHis. Thg1 family enzymes in Archaea and Bacteria, called Thg1-like-proteins (TLPs), catalyze a similar but distinct 3' to 5' addition in an exclusively WC-dependent manner. Essential nature of ScThg1
physiological function
tRNAHis guanylyltransferase (Thg1) transfers a guanosine triphosphate (GTP) in the 3'-5' direction onto the 5'-terminal of tRNAHis, opposite adenosine at position 73 (A73). The guanosine at the -1 position (G-1) serves as an identity element for histidyl-tRNA synthetase. Construction of a two-stranded tRNAHis molecule composed of a primer and a template strand through division at the D-loop, and evaluation of the structural requirements of the incoming GTP from the incorporation efficiencies of GTP analogues into the two-piece tRNAHis. Nitrogen at position 7 and the 6-keto oxygen of the guanine base are important for G-1 addition, but the 2-amino group is not essential. Substitution of the conserved A73 in tRNAHis reveals that the G-1 addition reaction is more efficient onto the template containing the opposite A73 than onto the template with cytidine (C73) or other bases forming canonical Watson-Crick base-pairing
physiological function
-
TLP homologues differ in terms of the number of nucleotide additions that are observed in vitro with tRNA transcripts mimicking the mature tRNAHis that can be a substrate for this kind of activity in vivo. The ability to add multiple 50-nucleotides to these types of tRNAHis is a direct consequence of the presence of a C73 discriminator, which results in the formation of three consecutive C-nucleotides in the 3'-C73CCA end. These types of substrates are initially shown to cause multiple G-addition reactions even in the context of eukaryotic Thg1, and several bacterial/archaeal homologues
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. Histidyl-tRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element. The enzyme homologue from Methanothermobacter thermoautotrophicus appears to limit nucleotide addition to only a single guanine addition, despite the presence of an extended C-template at the tRNA 3'-end
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life. PaThg1 catalyzes extended, template dependent tRNA repair, adding up to 13 nucleotides to a truncated tRNAHis substrate. PaThg1 fully restores the near correct sequence of the D- and acceptor stem, but also produces incompletely and incorrectly repaired tRNA products
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life. PaThg1 catalyzes extended, template dependent tRNA repair, adding up to 13 nucleotides to a truncated tRNAHis substrate. PaThg1 fully restores the near correct sequence of the D- and acceptor stem, but also produces incompletely and incorrectly repaired tRNA products
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. Histidyl-tRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. HistidyltRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element
-
physiological function
-
TLP homologues differ in terms of the number of nucleotide additions that are observed in vitro with tRNA transcripts mimicking the mature tRNAHis that can be a substrate for this kind of activity in vivo. The ability to add multiple 50-nucleotides to these types of tRNAHis is a direct consequence of the presence of a C73 discriminator, which results in the formation of three consecutive C-nucleotides in the 3'-C73CCA end. These types of substrates are initially shown to cause multiple G-addition reactions even in the context of eukaryotic Thg1, and several bacterial/archaeal homologues
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. HistidyltRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) transfers a guanosine triphosphate (GTP) in the 3'-5' direction onto the 5'-terminal of tRNAHis, opposite adenosine at position 73 (A73). The guanosine at the -1 position (G-1) serves as an identity element for histidyl-tRNA synthetase. Construction of a two-stranded tRNAHis molecule composed of a primer and a template strand through division at the D-loop, and evaluation of the structural requirements of the incoming GTP from the incorporation efficiencies of GTP analogues into the two-piece tRNAHis. Nitrogen at position 7 and the 6-keto oxygen of the guanine base are important for G-1 addition, but the 2-amino group is not essential. Substitution of the conserved A73 in tRNAHis reveals that the G-1 addition reaction is more efficient onto the template containing the opposite A73 than onto the template with cytidine (C73) or other bases forming canonical Watson-Crick base-pairing
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. HistidyltRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element
-
physiological function
-
TLP homologues differ in terms of the number of nucleotide additions that are observed in vitro with tRNA transcripts mimicking the mature tRNAHis that can be a substrate for this kind of activity in vivo. The ability to add multiple 50-nucleotides to these types of tRNAHis is a direct consequence of the presence of a C73 discriminator, which results in the formation of three consecutive C-nucleotides in the 3'-C73CCA end. These types of substrates are initially shown to cause multiple G-addition reactions even in the context of eukaryotic Thg1, and several bacterial/archaeal homologues
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) specifies eukaryotic tRNAHis identity by catalyzing a 3' to 5' non-Watson Crick (WC) addition of guanosine to the 5'-end of tRNAHis. Thg1 family enzymes in Archaea and Bacteria, called Thg1-like-proteins (TLPs), catalyze a similar but distinct 3' to 5' addition in an exclusively WC-dependent manner. Essential nature of ScThg1
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. Histidyl-tRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element
-
physiological function
-
the tRNAHis guanylyltransferase posttranscriptionally adds a 5'-G-1 from GTP to yeast tRNAHis. The presence of this single G at the -1 position is critical for recognition of tRNAHis by the histidyl-tRNA synthetase (HisRS). Thg1 adds a single G-1 residue across from an A73 discriminator nucleotide, forming an unconventional non-Watson Crick base pair. This unusual 3'-5' nucleotidyltransferase protein is a member of a larger family of Watson Crick-dependent 3'-5' polymerase enzymes that share structural similarity with canonical 5'-3' DNA and RNA polymerases
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life. Most eukaryotic Thg1 homologs are essential genes involved in tRNAHis maturation. These enzymes normally catalyze a single 5' guanylation of tRNAHis lacking the essential G-1 identity element required for aminoacylation. G-1 is the critical identity element that histidyl-tRNA synthetase (HisRS) uses to recognize its cognate tRNA, enabling HisRS to differentiate tRNAHis from the pool of other cellular tRNAs
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. Histidyl-tRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element. The enzyme homologue from Methanothermobacter thermoautotrophicus appears to limit nucleotide addition to only a single guanine addition, despite the presence of an extended C-template at the tRNA 3'-end
-
physiological function
-
TLP homologues differ in terms of the number of nucleotide additions that are observed in vitro with tRNA transcripts mimicking the mature tRNAHis that can be a substrate for this kind of activity in vivo. The ability to add multiple 50-nucleotides to these types of tRNAHis is a direct consequence of the presence of a C73 discriminator, which results in the formation of three consecutive C-nucleotides in the 3'-C73CCA end. These types of substrates are initially shown to cause multiple G-addition reactions even in the context of eukaryotic Thg1, and several bacterial/archaeal homologues
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life. PaThg1 catalyzes extended, template dependent tRNA repair, adding up to 13 nucleotides to a truncated tRNAHis substrate. PaThg1 fully restores the near correct sequence of the D- and acceptor stem, but also produces incompletely and incorrectly repaired tRNA products
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) post-transcriptionally adds G-1. HistidyltRNA synthetase (HisRS) recognizes the Thg1-incorporated G-1 for the accurate histidylation of tRNAHis in eukaryotes. Role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair. G-1 is a tRNAHis identity element
-
physiological function
-
TLP homologues differ in terms of the number of nucleotide additions that are observed in vitro with tRNA transcripts mimicking the mature tRNAHis that can be a substrate for this kind of activity in vivo. The ability to add multiple 50-nucleotides to these types of tRNAHis is a direct consequence of the presence of a C73 discriminator, which results in the formation of three consecutive C-nucleotides in the 3'-C73CCA end. These types of substrates are initially shown to cause multiple G-addition reactions even in the context of eukaryotic Thg1, and several bacterial/archaeal homologues
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life. PaThg1 catalyzes extended, template dependent tRNA repair, adding up to 13 nucleotides to a truncated tRNAHis substrate. PaThg1 fully restores the near correct sequence of the D- and acceptor stem, but also produces incompletely and incorrectly repaired tRNA products
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) has unique reverse (3'-5') polymerase activity occurring in all three domains of life. PaThg1 catalyzes extended, template dependent tRNA repair, adding up to 13 nucleotides to a truncated tRNAHis substrate. PaThg1 fully restores the near correct sequence of the D- and acceptor stem, but also produces incompletely and incorrectly repaired tRNA products
-
physiological function
-
tRNAHis guanylyltransferase (Thg1) specifies eukaryotic tRNAHis identity by catalyzing a 3' to 5' non-Watson Crick (WC) addition of guanosine to the 5'-end of tRNAHis. Thg1 family enzymes in Archaea and Bacteria, called Thg1-like-proteins (TLPs), catalyze a similar but distinct 3' to 5' addition in an exclusively WC-dependent manner. Bacillus thuringiensis TLP sustains growth of a thg1DELTA strain by maintaining a WC-dependent addition of U-1 across from A73. The bacterial TLP from Bacillus thuringiensis, (BtTLP) repairs 5'-end truncated tRNAs in vitro, adding missing 5'-nucleotides using nucleotides in the 3'-half of the aminoacyl-acceptor stem as a template to restore WC base pairing. BtTLP is able to carry out the essential activity ScThg1 in vivo in Saccharomyces cerevisiae, but this apparent function contradicts the strong preference for WC base-paired nucleotide addition exhibited by BtTLP in vitro. BtTLP catalyzes its biochemically preferred WC-dependent reaction, possibly adding U-1 to this A73-containing tRNA. It is suggested that BtTLP is not catalyzing detectable activity on other RNAs in this system, overview
-
additional information
conserved lysine K43 in BtTLP appears to be important specifically for the activation reaction with ATP, and not used for the GTP activation reaction, since the alteration of this residue in the context of the bifunctional BtTLP only affects 5'-adenylylation rates. Structure-function analyses of Thg1 and TLP enzymes, overview
additional information
hThg1 can add a GMP directly to the 5'-terminus of mtRNAHis in a template-dependent manner, while the fungal enzyme from Candida albicans cannot. Acceleration of the diphosphate removal activity before or after the G-1 addition reaction is a key feature of hThg1 for maintaining a normal 5'-terminus of mtRNAHis in human mitochondria
additional information
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hThg1 can add a GMP directly to the 5'-terminus of mtRNAHis in a template-dependent manner, while the fungal enzyme from Candida albicans cannot. Acceleration of the diphosphate removal activity before or after the G-1 addition reaction is a key feature of hThg1 for maintaining a normal 5'-terminus of mtRNAHis in human mitochondria
additional information
identification of residues in yeast Thg1 that play a part in preventing extended polymerization. Mutation of these residues with alanine results in extended reverse polymerization
additional information
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identification of residues in yeast Thg1 that play a part in preventing extended polymerization. Mutation of these residues with alanine results in extended reverse polymerization
additional information
molecular basis for tRNA recognition, and catalytic mechanism, overview. Molecular basis for non-Watson-Crick G-1 addition: tRNA activation, nucleotidyl transfer, diphosphate removal, and maintenance of tRNAHis fidelity
additional information
molecular basis for tRNA recognition, and catalytic mechanism, overview. Molecular basis for non-Watson-Crick G-1 addition: tRNA activation, nucleotidyl transfer, diphosphate removal, and maintenance of tRNAHis fidelity. The superposition of Thg1 with the aforementioned polymerases displays similar positioning of the three conserved carboxylate residues in the polymerase active site to the pol I family, HsThg1 carboxylates D29, D76, and E77 correspond to T7 DNA polymerases D475, D654, and E655. The Thg1 mechanism of reverse polymerization may share features with the forward polymerization of the pol I family. Structure-function analyses of Thg1 and TLP enzymes, overview
additional information
molecular mechanism of substrate recognition and specificity of tRNAHis guanylyltransferase during nucleotide addition in the 3'-5' direction
additional information
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requirement for two critical tRNA-interacting residues, His152 and Lys187, in the context of human Thg1, reaction mechanism, overview. Eukaryotic Thg1 enzymes are strictly specific for tRNAHis, and this specificity is accomplished by recognition of the tRNAHis GUG anticodon. His152 and Lys187 play critical roles in activation of tRNAHis for non-WC addition. Once the 5'-end activation step is completed, the need for His152 and Lys187 is no longer as critical
additional information
structural superposition of a crystal structure of Saccharomyces cerevisiae ScThg1 and CaThg1-tRNAPhe GUG discovers a conserved secondary structure in the fingers domain, and suggests conserved dual RNA-binding surfaces that are originally elucidated in CaThg1. Both the acceptor stem's sugar phosphate backbone and the anticodon loop are coordinated by the fingers domain, the latter fingers-anticodon interaction is base-specific. The G34, U35, and G36 nucleotides that make up the tRNAHis anticodon are all observed to be coordinated by specific residues of CaThg1. All three anticodon bases are tightly coordinated, and mutations of the coordinating amino acids lead to a disruption or reduction in enzyme activity. The anticodon loop structure itself is stabilized by interactions with the Fsugar phosphate backbone of U35. Anticodon base G36 is coordinated in a groove formed by two alpha-helices flanking the central beta-sheet and stabilized by a stacking interaction with H154, which is an essential residue in the eukaryotic-specific sequence motif HINNLYN. Molecular basis for tRNA recognition, and catalytic mechanism, overview. Molecular basis for non-Watson-Crick G-1 addition: tRNA activation, nucleotidyl transfer, diphosphate removal, and maintenance of tRNAHis fidelity
additional information
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structure-function analyses of Thg1 and TLP enzymes, overview
additional information
structure-function analyses of Thg1 and TLP enzymes, overview
additional information
structure-function analyses of Thg1 and TLP enzymes, overview
additional information
structure-function analyses of Thg1 and TLP enzymes, overview
additional information
structure-function analyses of Thg1 and TLP enzymes, overview
additional information
structure-function analyses of Thg1 and TLP enzymes, overview
additional information
structure-function analyses of Thg1 and TLP enzymes, overview
additional information
structure-function analyses of Thg1 and TLP enzymes, overview
additional information
structure-function analyses of Thg1 and TLP enzymes, overview
additional information
structure-function analyses of Thg1 and TLP enzymes, overview
additional information
structure-function analyses of Thg1 and TLP enzymes, overview
additional information
Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
additional information
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Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
additional information
Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
additional information
-
Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
additional information
Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity. The catalytic palm domain of IgThg1 can promote forward or reverse extension of a polynucleotide chain and substrate orientation correlates with the direction of polymerization
additional information
-
Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity. The catalytic palm domain of IgThg1 can promote forward or reverse extension of a polynucleotide chain and substrate orientation correlates with the direction of polymerization
additional information
two flexible protomers at the potential binding site (PBS) for tRNAHis are observed, the PBS of the tetramer could also be one of the sites for interaction with partner proteins
additional information
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two flexible protomers at the potential binding site (PBS) for tRNAHis are observed, the PBS of the tetramer could also be one of the sites for interaction with partner proteins
additional information
yeast two-hybrid assays with the AET1, RACK1A, and eIF3h proteins, and polysome profiling assays
additional information
-
conserved lysine K43 in BtTLP appears to be important specifically for the activation reaction with ATP, and not used for the GTP activation reaction, since the alteration of this residue in the context of the bifunctional BtTLP only affects 5'-adenylylation rates. Structure-function analyses of Thg1 and TLP enzymes, overview
-
additional information
-
structure-function analyses of Thg1 and TLP enzymes, overview
-
additional information
-
Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
-
additional information
-
Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
-
additional information
-
structure-function analyses of Thg1 and TLP enzymes, overview
-
additional information
-
structure-function analyses of Thg1 and TLP enzymes, overview
-
additional information
-
structure-function analyses of Thg1 and TLP enzymes, overview
-
additional information
-
structural superposition of a crystal structure of Saccharomyces cerevisiae ScThg1 and CaThg1-tRNAPhe GUG discovers a conserved secondary structure in the fingers domain, and suggests conserved dual RNA-binding surfaces that are originally elucidated in CaThg1. Both the acceptor stem's sugar phosphate backbone and the anticodon loop are coordinated by the fingers domain, the latter fingers-anticodon interaction is base-specific. The G34, U35, and G36 nucleotides that make up the tRNAHis anticodon are all observed to be coordinated by specific residues of CaThg1. All three anticodon bases are tightly coordinated, and mutations of the coordinating amino acids lead to a disruption or reduction in enzyme activity. The anticodon loop structure itself is stabilized by interactions with the Fsugar phosphate backbone of U35. Anticodon base G36 is coordinated in a groove formed by two alpha-helices flanking the central beta-sheet and stabilized by a stacking interaction with H154, which is an essential residue in the eukaryotic-specific sequence motif HINNLYN. Molecular basis for tRNA recognition, and catalytic mechanism, overview. Molecular basis for non-Watson-Crick G-1 addition: tRNA activation, nucleotidyl transfer, diphosphate removal, and maintenance of tRNAHis fidelity
-
additional information
-
molecular mechanism of substrate recognition and specificity of tRNAHis guanylyltransferase during nucleotide addition in the 3'-5' direction
-
additional information
-
structure-function analyses of Thg1 and TLP enzymes, overview
-
additional information
-
structure-function analyses of Thg1 and TLP enzymes, overview
-
additional information
-
molecular basis for tRNA recognition, and catalytic mechanism, overview. Molecular basis for non-Watson-Crick G-1 addition: tRNA activation, nucleotidyl transfer, diphosphate removal, and maintenance of tRNAHis fidelity
-
additional information
-
identification of residues in yeast Thg1 that play a part in preventing extended polymerization. Mutation of these residues with alanine results in extended reverse polymerization
-
additional information
-
structure-function analyses of Thg1 and TLP enzymes, overview
-
additional information
-
structure-function analyses of Thg1 and TLP enzymes, overview
-
additional information
-
Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
-
additional information
-
structure-function analyses of Thg1 and TLP enzymes, overview
-
additional information
-
structure-function analyses of Thg1 and TLP enzymes, overview
-
additional information
-
Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
-
additional information
-
Thg1 encodes the conserved catalytic palm domain and fingers domain. Naturally occurring minimal Thg1 enzyme from Ignicoccus hospitalis (IhThg1), which lacks parts of the conserved fingers domain, is catalytically active. And adds all four natural nucleotides to RNA substrates. The entire fingers domain of Methanosarcina acetivorans Thg1 and Pyrobaculum aerophilum Thg1 (PaThg1) is dispensable for enzymatic activity
-
additional information
Saccharomyces cerevisiae ATCC 2045083
-
two flexible protomers at the potential binding site (PBS) for tRNAHis are observed, the PBS of the tetramer could also be one of the sites for interaction with partner proteins
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Show AA Sequence and Transmembrane Helices (3843 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
additional information
dimer
Methanosarcina acetivorans TLP forms a dimer coordinating on tRNA. While the dimer binds the acceptor stem and T arm of its tRNA substrate, the anticodon loop is not coordinated by TLP enzymes
tetramer
4 * 32000, SDS-PAGE, a dimer-of-dimers is the active tetrameric form
tetramer
4 * 27800, about, sequence calculation and crystal structure
tetramer
crystal structures of eukaryotic Thg1 enzymes showed that monomeric Thg1 is composed of a six-strand antiparallel beta-sheet flanked by three or four alpha-helices on each side, along with a protruding long arm composed of two antiparallel beta-strands. Each monomer forms a dimer, mediated by salt bridge formation and hydrogen bonding between the beta-sheet and an alpha-helix. Alanine scanning mutagenesis in Saccharomyces cerevisiae Thg1 (ScThg1) of conserved residues responsible for mediating dimer formation has shown strongly diminished G-1 addition activity. Dimer-of-dimer formation stems from initial dimer formation., the alpha-helix of the N-terminus in monomer A interacts with the nucleotide binding site of monomer B and ultimately forms an intertwined N-terminus segment, which again interacts with a symmetrical dimer to form its active tetrameric form
tetramer
-
crystal structures of eukaryotic Thg1 enzymes showed that monomeric Thg1 is composed of a six-strand antiparallel beta-sheet flanked by three or four alpha-helices on each side, along with a protruding long arm composed of two antiparallel beta-strands. Each monomer forms a dimer, mediated by salt bridge formation and hydrogen bonding between the beta-sheet and an alpha-helix. Alanine scanning mutagenesis in Saccharomyces cerevisiae Thg1 (ScThg1) of conserved residues responsible for mediating dimer formation has shown strongly diminished G-1 addition activity. Dimer-of-dimer formation stems from initial dimer formation., the alpha-helix of the N-terminus in monomer A interacts with the nucleotide binding site of monomer B and ultimately forms an intertwined N-terminus segment, which again interacts with a symmetrical dimer to form its active tetrameric form
-
tetramer
Saccharomyces cerevisiae ATCC 2045083
-
4 * 27800, about, sequence calculation and crystal structure
-
additional information
crystal structures of eukaryotic Thg1 enzymes shows that monomeric Thg1 is composed of a six-strand antiparallel beta-sheet flanked by three or four alpha-helices on each side, along with a protruding long arm composed of two antiparallel beta-strands. Each monomer forms a dimer, mediated by salt bridge formation and hydrogen bonding between the beta-sheet and an alpha-helix. Alanine scanning mutagenesis in Saccharomyces cerevisiae Thg1 (ScThg1) of conserved residues responsible for mediating dimer formation has shown strongly diminished G-1 addition activity. Dimer-of-dimer formation stems from initial dimer formation., the alpha-helix of the N-terminus in monomer A interacts with the nucleotide binding site of monomer B and ultimately forms an intertwined N-terminus segment, which again interacts with a symmetrical dimer to form its active tetrameric form. Eukaryotic Thg1 enzymes show monomeric Thg1 that is composed of a six-strand antiparallel beta-sheet flanked by three or four alpha-helices on each side, along with a protruding long arm composed of two antiparallel beta-strands. Structure-function analyses of Thg1 and TLP enzymes, overview
additional information
-
crystal structures of eukaryotic Thg1 enzymes shows that monomeric Thg1 is composed of a six-strand antiparallel beta-sheet flanked by three or four alpha-helices on each side, along with a protruding long arm composed of two antiparallel beta-strands. Each monomer forms a dimer, mediated by salt bridge formation and hydrogen bonding between the beta-sheet and an alpha-helix. Alanine scanning mutagenesis in Saccharomyces cerevisiae Thg1 (ScThg1) of conserved residues responsible for mediating dimer formation has shown strongly diminished G-1 addition activity. Dimer-of-dimer formation stems from initial dimer formation., the alpha-helix of the N-terminus in monomer A interacts with the nucleotide binding site of monomer B and ultimately forms an intertwined N-terminus segment, which again interacts with a symmetrical dimer to form its active tetrameric form. Eukaryotic Thg1 enzymes show monomeric Thg1 that is composed of a six-strand antiparallel beta-sheet flanked by three or four alpha-helices on each side, along with a protruding long arm composed of two antiparallel beta-strands. Structure-function analyses of Thg1 and TLP enzymes, overview
-
additional information
eukaryotic Thg1 enzymes show monomeric Thg1 that is composed of a six-strand antiparallel beta-sheet flanked by three or four alpha-helices on each side, along with a protruding long arm composed of two antiparallel beta-strands
additional information
eukaryotic Thg1 enzymes show monomeric Thg1 that is composed of a six-strand antiparallel beta-sheet flanked by three or four alpha-helices on each side, along with a protruding long arm composed of two antiparallel beta-strands. Structure-function analyses of Thg1 and TLP enzymes, overview
additional information
-
eukaryotic Thg1 enzymes show monomeric Thg1 that is composed of a six-strand antiparallel beta-sheet flanked by three or four alpha-helices on each side, along with a protruding long arm composed of two antiparallel beta-strands. Structure-function analyses of Thg1 and TLP enzymes, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with ATP and with GTP. The enzyme is a tetramer. Catalysis of the 3'-5' reaction with 5'-monophosphorylated tRNA necessitates first an activation step, generating a 5'-adenylylated intermediate prior to a second nucleotidyl transfer step, in which a nucleotide is transferred to the tRNA 5'-end. Distinct binding sites are observed for the nucleotides involved in these two steps
in complex with tRNAHis, ATP and GTP. tRNAHis guanylyltransferase catalyzes reverse (3'-5') nucleotide addition. The directionality of nucleotide polymerization is determined by the orientation of approach of the nucleotide substrate. The tRNA substrate enters the enzyme's active site from the opposite direction (180 degrees flip) compared with similar nucleotide substrates of canonical 5'-3' polymerases, and the finger domains are on opposing sides of the core palm domain. in complexes with ATP and GTP, the adenine base of ATP1 is more deeply embedded into the nucleotide-binding pocket than GTP1 and recognized by hydrogen bonds with the main chain of Asp47, and the side chain of Lys44 interacts directly with ATP1. The base of GTP1 forms hydrogen bonds with the main-chain atoms of Glu43 and Asp47
2.3 A crystal structure of human THG1 shares structural homology with canonical 5'-3' DNA polymerases and adenylyl/guanylyl cyclases, two enzyme families known to use a two-metal-ion mechanism for catalysis
purified GTP-bound Thg1, hanging drop vapor diffusion method, mixing of 0.001 ml of 7 mg/ml protein in 20 mM Tris, pH 8.0, 500 mM NaCl, and 5 mM DTT, with 0.001 ml of reservoir solution consisting of 0.1 M 2-(N-morpholino)ethanesulfonic acid, pH 6.0, and 0.9 M ammonium sulfate, equilibration against 0.5 ml of reservoir solution, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement method, modelling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K43A
the observed rate of adenylylation is decreased by about 10fold, while the rate of guanylylation is virtually unchanged
M158A
no effect on the observed rate of activation
M158N
mutation does not impart the preference for ATP to the enzyme, but it further improves the kinetics for GTP-dependent activation by 10fold relative to the wild-type
K43A
-
the observed rate of adenylylation is decreased by about 10fold, while the rate of guanylylation is virtually unchanged
-
M158A
-
no effect on the observed rate of activation
-
M158N
-
mutation does not impart the preference for ATP to the enzyme, but it further improves the kinetics for GTP-dependent activation by 10fold relative to the wild-type
-
V55A
homozygous mutation identified in three siblings who presented with cerebellar signs, developmental delay, dysarthria, and pyramidal signs and had cerebellar atrophy on brain MRI. A defect in the protein tRNAHis guanylyltransferase activity is excluded in vitro
D153A
poorly expressed. D153A is stable, but its expression is somehow toxic to Escherichia coli. 312% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
D47A
54.7% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
D68A
59% of wild-type G(-1) addition activity. The mutation causes a dramatic decrease in the rigorous specificity of Thg1 for tRNAHis. This single alteration enhances the kcat/KM for ppp-tRNAPhe by nearly 100-fold relative to that of wild-type Thg1. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
D77A
less than 0.1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
E13A
0.1%-1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
E75A
105% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
E78A
less than 0.1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
G74A
44.4% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
H155A
less than 0.1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
K190A
less than 0.1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
K211A
0.1%-1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
K44A
0.1%-1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
K96A
less than 0.1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
N161A
0.1%-1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
N201A
less than 0.1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
N46A
22.6% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
P45A
62.3% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
R133A
0.1%-1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
R150A
0.1%-1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
R27A
0.1%-1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
R93A
0.1%-1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
W113A/I156V
40.1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
Y160A
0.1%-1% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
Y202A
poorly expressed, The Y202A variant is present at very low levels in soluble crude extracts and yields nearly undetectable levels of protein after purification, suggesting that this alteration leads to lack of overall stability
Y40A
42.9% of wild-type G(-1) addition activity. G(-) i.e. the extra nucleotide posttranscriptionally added in position (-1) of tRNA
additional information
additional information
-
the emergence of dual function residues such as His152 and Lys187 would enable a single alteration to affect both catalytic activity and tRNA specificity of the enzyme
additional information
generation of an aet1 mutant, the aet1 mutant is crossed with a japonica variety, Jiahua-1, construction of CRISPR/Cas9 gene-editing constructs for AET1, RACK1A, eIF3h, and OsARF23. The aet1 mutant shows loss of Thg1 enzyme function, leading to reduced aminoacyl-tRNAHis levels and translational efficiency. The mutant plants display slight phenotype changes under normal conditions. In the aet1 mutant, the translation of OsARF19 and OsARF23 mRNAs is downregulated, which results in reduced levels of OsARFs and eventually causes growth arrest
additional information
Saccharomyces cerevisiae tRNAHis transcripts with and without G-1 are generated, carrying a C73 discriminator instead of the wild-type A73 position (tRNAHisDELTAG-1 A73C and tRNAHis+G-1 A73C). Due to the additional base pair G-1/C73, tRNAHis+G-1 A73C carries an extended acceptor stem with a base-paired discriminator position. This situation does not affect CCA-addition catalyzed by the CCA-adding enzyme and results in a similarly efficient CCA incorporation to tRNAHis+G-1 A73C compared to tRNAHisDELTAG-1 A73C. Both tRNAHis substrates with a cytosine at the discriminator position are readily accepted as substrates for CCA-addition, showing comparable band patterns like the wild-type tRNAHis containing an A73. Analysis of G-1 incorporation on tRNAHis A73C variants with and without 3'-CCA-end shows significant preference of Thg1 for tRNAHis containing the 3'-CCA, both in terms of rate and maximal amount of product formed in the reactions, kinetic analysis
additional information
-
Saccharomyces cerevisiae tRNAHis transcripts with and without G-1 are generated, carrying a C73 discriminator instead of the wild-type A73 position (tRNAHisDELTAG-1 A73C and tRNAHis+G-1 A73C). Due to the additional base pair G-1/C73, tRNAHis+G-1 A73C carries an extended acceptor stem with a base-paired discriminator position. This situation does not affect CCA-addition catalyzed by the CCA-adding enzyme and results in a similarly efficient CCA incorporation to tRNAHis+G-1 A73C compared to tRNAHisDELTAG-1 A73C. Both tRNAHis substrates with a cytosine at the discriminator position are readily accepted as substrates for CCA-addition, showing comparable band patterns like the wild-type tRNAHis containing an A73. Analysis of G-1 incorporation on tRNAHis A73C variants with and without 3'-CCA-end shows significant preference of Thg1 for tRNAHis containing the 3'-CCA, both in terms of rate and maximal amount of product formed in the reactions, kinetic analysis
additional information
-
Saccharomyces cerevisiae tRNAHis transcripts with and without G-1 are generated, carrying a C73 discriminator instead of the wild-type A73 position (tRNAHisDELTAG-1 A73C and tRNAHis+G-1 A73C). Due to the additional base pair G-1/C73, tRNAHis+G-1 A73C carries an extended acceptor stem with a base-paired discriminator position. This situation does not affect CCA-addition catalyzed by the CCA-adding enzyme and results in a similarly efficient CCA incorporation to tRNAHis+G-1 A73C compared to tRNAHisDELTAG-1 A73C. Both tRNAHis substrates with a cytosine at the discriminator position are readily accepted as substrates for CCA-addition, showing comparable band patterns like the wild-type tRNAHis containing an A73. Analysis of G-1 incorporation on tRNAHis A73C variants with and without 3'-CCA-end shows significant preference of Thg1 for tRNAHis containing the 3'-CCA, both in terms of rate and maximal amount of product formed in the reactions, kinetic analysis
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme shows a drastically shortened half-life in the absence of divalent metal ions
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain Rosetta(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
-
recombinant N-terminally His6-tagged CaThg1 from Escherichia coli strain BL21 (DE3)-pRARE2 by nickel affinity chromatography, dialysis, and ultrafiltration
recombinnat His-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) pLysS by nickel affinity chromatography, recombinant MBP-tagged enzyme mutant P382S from Escherichia coli strain Rosetta-gami(DE3) by amylose affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene AET1, cloned from var. TQ, recombinant overexpression in Oryza sativa mediated by Agrobacterium tumefaciens strain EHA105 transformation, quantitative RT-PCR enzyme expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS, recombinant expression of MBP-tagged enzyme mutant P382S in Escherichia coli strain Rosetta-gami(DE3)
gene thg1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant enzyme expression
gene thg1, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene thg1, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta(DE3)
gene thg1, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene THG1, recombinant overexpression of N-terminally His6-tagged CaThg1 in Escherichia coli strain BL21 (DE3)-pRARE2
recombinant expression of only the palm domains from Methanosarcina acetivorans Thg1 (MaPalm, amino acids 1-141)
recombinant expression of only the palm domains from Pyrobaculum aerophilum Thg1 (PaPalm, amino acids 1-150)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
homozygosity for the V55A mutation in THG1L is the cause of an abnormal mitochondrial network in the patient fibroblasts, likely by interfering with THG1L activity towards MFN2
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jackman, J.E.; Phizicky, E.M.
Identification of critical residues for G-1 addition and substrate recognition by tRNA(His) guanylyltransferase
Biochemistry
47
4817-4825
2008
Saccharomyces cerevisiae (P53215), Saccharomyces cerevisiae
brenda
Rice, T.S.; Ding, M.; Pederson, D.S.; Heintz, N.H.
The highly conserved tRNAHis guanylyltransferase Thg1p interacts with the origin recognition complex and is required for the G2/M phase transition in the yeast Saccharomyces cerevisiae
Eukaryot. Cell
4
832-835
2005
Saccharomyces cerevisiae (P53215), Saccharomyces cerevisiae
brenda
Gu, W.; Jackman, J.E.; Lohan, A.J.; Gray, M.W.; Phizicky, E.M.
tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNAHis
Genes Dev.
17
2889-2901
2003
Saccharomyces cerevisiae (P53215), Saccharomyces cerevisiae
brenda
Pande, S.; Jahn, D.; Sll, D.
Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and physical properties
J. Biol. Chem.
266
22826-22831
1991
Saccharomyces cerevisiae (P53215), Saccharomyces cerevisiae
brenda
Jahn, D.; Pande, S.
Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic mechanism
J. Biol. Chem.
266
22832-22836
1991
Saccharomyces cerevisiae (P53215), Saccharomyces cerevisiae
brenda
Gu, W.; Hurto, R.L.; Hopper, A.K.; Grayhack, E.J.; Phizicky, E.M.
Depletion of Saccharomyces cerevisiae tRNA(His) guanylyltransferase Thg1p leads to uncharged tRNAHis with additional m(5)C
Mol. Cell. Biol.
25
8191-8201
2005
Saccharomyces cerevisiae (P53215), Saccharomyces cerevisiae
brenda
Placido, A.; Sieber, F.; Gobert, A.; Gallerani, R.; Gieg, P.; Marchal-Drouard, L.
Plant mitochondria use two pathways for the biogenesis of tRNAHis
Nucleic Acids Res.
38
7711-7717
2010
Solanum tuberosum
brenda
Jackman, J.E.; Phizicky, E.M.
tRNAHis guanylyltransferase catalyzes a 3'-5' polymerization reaction that is distinct from G-1 addition
Proc. Natl. Acad. Sci. USA
103
8640-8645
2006
Saccharomyces cerevisiae
brenda
Hyde, S.J.; Eckenroth, B.E.; Smith, B.A.; Eberley, W.A.; Heintz, N.H.; Jackman, J.E.; Doubli, S.
tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases
Proc. Natl. Acad. Sci. USA
107
20305-20310
2010
Homo sapiens (Q9NWX6), Homo sapiens
brenda
Jackman, J.E.; Phizicky, E.M.
tRNAHis guanylyltransferase adds G-1 to the 5' end of tRNAHis by recognition of the anticodon, one of several features unexpectedly shared with tRNA synthetases
RNA
12
1007-1014
2006
Saccharomyces cerevisiae (P53215), Saccharomyces cerevisiae
brenda
Preston, M.A.; Phizicky, E.M.
The requirement for the highly conserved G-1 residue of Saccharomyces cerevisiae tRNAHis can be circumvented by overexpression of tRNAHis and its synthetase
RNA
16
1068-1077
2010
Saccharomyces cerevisiae (P53215), Saccharomyces cerevisiae
brenda
Smith, B.A.; Jackman, J.E.
Saccharomyces cerevisiae Thg1 uses 5-pyrophosphate removal to control addition of nucleotides to tRNA(His.)
Biochemistry
53
1380-1391
2014
Saccharomyces cerevisiae (P53215), Saccharomyces cerevisiae
brenda
Edvardson, S.; Elbaz-Alon, Y.; Jalas, C.; Matlock, A.; Patel, K.; Labbe, K.; Shaag, A.; Jackman, J.E.; Elpeleg, O.
A mutation in the THG1L gene in a family with cerebellar ataxia and developmental delay
Neurogenetics
17
219-225
2016
Homo sapiens (Q9NWX6), Homo sapiens
brenda
Rao, B.; Mohammad, F.; Gray, M.; Jackman, J.
Absence of a universal element for tRNAHis identity in Acanthamoeba castellanii
Nucleic Acids Res.
41
1885-1894
2013
Acanthamoeba castellanii (J9XZJ1), Acanthamoeba castellanii (M1ZML3)
brenda
Hyde, S.J.; Rao, B.S.; Eckenroth, B.E.; Jackman, J.E.; Doublie, S.
Structural studies of a bacterial tRNA(HIS) guanylyltransferase (Thg1)-like protein, with nucleotide in the activation and nucleotidyl transfer sites
PLoS ONE
8
e67465
2013
Bacillus thuringiensis serovar israelensis (Q3F0V8), Bacillus thuringiensis serovar israelensis ATCC 35646 (Q3F0V8)
brenda
Nakamura, A.; Nemoto, T.; Heinemann, I.U.; Yamashita, K.; Sonoda, T.; Komoda, K.; Tanaka, I.; Soell, D.; Yao, M.
Structural basis of reverse nucleotide polymerization
Proc. Natl. Acad. Sci. USA
110
20970-20975
2013
Candida albicans (A0A1D8PQL3), Candida albicans, Candida albicans ATCC MYA-2876 (A0A1D8PQL3)
brenda
Lee, K.; Lee, E.H.; Son, J.; Hwang, K.Y.
Crystal structure of tRNAHis guanylyltransferase from Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
490
400-405
2017
Saccharomyces cerevisiae (P53215), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 2045083 (P53215)
brenda
Nakamura, A.; Wang, D.; Komatsu, Y.
Biochemical analysis of human tRNAHis guanylyltransferase in mitochondrial tRNAHis maturation
Biochem. Biophys. Res. Commun.
503
2015-2021
2018
Homo sapiens (Q9NWX6), Homo sapiens
brenda
Dodbele, S.; Moreland, B.; Gardner, S.; Bundschuh, R.; Jackman, J.
5'-End sequencing in Saccharomycesxa0cerevisiae offers new insights into 5'-ends of tRNAHis and snoRNAs
FEBS Lett.
593
971-981
2019
Saccharomyces cerevisiae (P53215), Bacillus thuringiensis serovar israelensis (Q3F0V8), Dictyostelium discoideum (Q54WD4), Saccharomyces cerevisiae ATCC 204508 (P53215), Bacillus thuringiensis serovar israelensis ATCC 35646 (Q3F0V8)
brenda
Chen, A.; Jayasinghe, M.; Chung, C.; Rao, B.; Kenana, R.; Heinemann, I.; Jackman, J.
The role of 3' to 5' reverse RNA polymerization in tRNA fidelity and repair
Genes (Basel)
10
250
2019
Methanothermobacter thermautotrophicus, no activity in Trypanosoma brucei, no activity in Acanthamoeba castellanii, Methanosarcina acetivorans (A0A1C7D1G9), Candida albicans (A0A1D8PQL3), Bacillus thuringiensis (A0A2A8WD07), Ignicoccus hospitalis (A8A9R6), Saccharomyces cerevisiae (P53215), Myxococcus xanthus (Q1CZS0), Methanosarcina barkeri (Q46BQ4), Dictyostelium discoideum (Q54E29), Dictyostelium discoideum (Q54HW0), Dictyostelium discoideum (Q54WD4), Dictyostelium discoideum (Q86IE7), Methanopyrus kandleri (Q8TZ46), Pyrobaculum aerophilum (Q8ZY97), Homo sapiens (Q9NWX6), Bacillus thuringiensis T01-328 (A0A2A8WD07), Methanosarcina barkeri Fusaro (Q46BQ4), Myxococcus xanthus DK 1622 (Q1CZS0), Ignicoccus hospitalis KIN4/I (A8A9R6), Methanopyrus kandleri DSM 6324 (Q8TZ46), Candida albicans ATCC MYA-2876 (A0A1D8PQL3), Ignicoccus hospitalis JCM 14125 (A8A9R6), Methanopyrus kandleri NBRC 100938 (Q8TZ46), Saccharomyces cerevisiae ATCC 204508 (P53215), Methanosarcina barkeri DSM 804 (Q46BQ4), Methanopyrus kandleri JCM 9639 (Q8TZ46), Ignicoccus hospitalis DSM 18386 (A8A9R6), Pyrobaculum aerophilum ATCC 51768 (Q8ZY97)
brenda
Poehler, M.T.; Roach, T.M.; Betat, H.; Jackman, J.E.; Moerl, M.
A temporal order in 5'-and 3'-processing of eukaryotic tRNAHis
Int. J. Mol. Sci.
20
1384
2019
Saccharomyces cerevisiae (P53215), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P53215)
brenda
Matlock, A.O.; Smith, B.A.; Jackman, J.E.
Chemical footprinting and kinetic assays reveal dual functions for highly conserved eukaryotic tRNAHis guanylyltransferase residues
J. Biol. Chem.
294
8885-8893
2019
Homo sapiens
brenda
Chen, K.; Guo, T.; Li, X.M.; Zhang, Y.M.; Yang, Y.B.; Ye, W.W.; Dong, N.Q.; Shi, C.L.; Kan, Y.; Xiang, Y.H.; Zhang, H.; Li, Y.C.; Gao, J.P.; Huang, X.; Zhao, Q.; Han, B.; Shan, J.X.; Lin, H.X.
Translational regulation of plant response to high temperature by a dual-function tRNAHis guanylyltransferase in rice
Mol. Plant
12
1123-1142
2019
Oryza sativa Japonica Group (A0A0P0WQ58)
brenda
Nakamura, A.; Wang, D.; Komatsu, Y.
Molecular mechanism of substrate recognition and specificity of tRNAHis guanylyltransferase during nucleotide addition in the 3'-5' direction
RNA
24
1583-1593
2018
Candida albicans (A0A1D8PQL3), Candida albicans ATCC MYA-2876 (A0A1D8PQL3)
brenda
Desai, R.; Kim, K.; Buechsenschuetz, H.C.; Chen, A.W.; Bi, Y.; Mann, M.R.; Turk, M.A.; Chung, C.Z.; Heinemann, I.U.
Minimal requirements for reverse polymerization and tRNA repair by tRNAHis guanylyltransferase
RNA Biol.
15
614-622
2018
Methanosarcina acetivorans (A0A1C7D1G9), Methanosarcina acetivorans, Ignicoccus hospitalis (A8A9R6), Ignicoccus hospitalis, Saccharomyces cerevisiae (P53215), Saccharomyces cerevisiae, Pyrobaculum aerophilum (Q8ZY97), Pyrobaculum aerophilum, Pyrobaculum aerophilum DSM 7523 (Q8ZY97), Pyrobaculum aerophilum IM2 (Q8ZY97), Saccharomyces cerevisiae ATCC 204508 (P53215), Pyrobaculum aerophilum NBRC 100827 (Q8ZY97), Pyrobaculum aerophilum ATCC 51768 (Q8ZY97), Pyrobaculum aerophilum JCM 9630 (Q8ZY97)
brenda
Lee, Y.H.; Lo, Y.T.; Chang, C.P.; Yeh, C.S.; Chang, T.H.; Chen, Y.W.; Tseng, Y.K.; Wang, C.C.
Naturally occurring dual recognition of tRNAHis substrates with and without a universal identity element
RNA Biol.
16
1275-1285
2019
no activity in Caenorhabditis elegans
brenda
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Release 2023.1 (January 2023)
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