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18-mer 2' phosphorylated RNA
?
18-mer 2' phosphorylated RNA + NAD+
?
-
ACAAGACUGUAA-(2-phosphate)AUCUUG
-
-
?
2'-phospho-(ligated tRNA) + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide + H+
-
-
-
-
?
2'-phospho-(ligated tRNA) + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide + H2O
yeasts
-
enzyme catalyzes final step in tRNA splicing
-
-
?
2'-phospho-(ligated tRNA) + NAD+
mature tRNA + ADP-ribose1'',2''-phosphate + nicotinamide + H2O
-
last step in the pre-tRNA splicing process
-
-
ir
2'-phospho-[ligated tRNA]
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
3-mer 2' phosphorylated RNA
?
3-mer 2' phosphorylated RNA + NAD+
?
-
AU-(2-phosphate)U
-
-
?
8-mer 2' phosphorylated RNA
?
8-mer 2' phosphorylated RNA + NAD+
?
-
GUAA-(2-phosphate)AUCU
-
-
?
NAD+ + trinucleotide substrate
ADP-ribosylated RNA
-
requires ca. 0.0004 mM Tpt1 K69A/R71S, only 0.0000003 mM Tpt1p is required for similar or greater product formation
-
-
?
additional information
?
-
18-mer 2' phosphorylated RNA
?
-
-
-
-
?
18-mer 2' phosphorylated RNA
?
-
pACAAGACUCUAA-(2-phosphate)AUCUUG
-
-
?
2'-phospho-[ligated tRNA]
?
-
-
-
-
?
2'-phospho-[ligated tRNA]
?
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
production of a reaction intermediate, nicotinamide release occurs during intermediate formation, KptA can catalyze the conversion of the intermediate to both product and the original substrate
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
minimal substrate is a dinucleotide containing an internal 2' phosphate, 600fold more specific for 2'phosphates than for eihter 5'- or 3'-terminal phosphates, 20fold more specific for internal 2' phosphates than for terminal 2' 3', or 2'3'-cyclic phosphates, at least 50fold more specific for internal 2' phosphates than terminal 2' phosphates
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
mTpt1 can catalyze the conversion of the KptA-generated intermediate to both product and the original substrate
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
minimal substrate is a dinucleotide containing an internal 2'-phosphate
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
specificity for substrates bearing an internal 2'-phosphate
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
Tpt1 can catalyze the conversion of the KptA-generated intermediate to both product and the original substrate
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
tRNA_Leu_UAG, tRNA_SER, tRNA_LEU_CAA, tRNA_TYR, tRNA_LYS, tRNA_PRO1, tRNA_PRO2, tRNA_PHE, unidentified tRNA
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
98% conversion by ApeTpt1
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
98% conversion by ApeTpt1
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
98% conversion by ApeTpt1
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
98% conversion by ApeTpt1
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
98% conversion by ApeTpt1
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
13% conversion by the Archaeoglobus fulgidus enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
13% conversion by the Archaeoglobus fulgidus enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
13% conversion by the Archaeoglobus fulgidus enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
13% conversion by the Archaeoglobus fulgidus enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
13% conversion by the Archaeoglobus fulgidus enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
20% conversion by the Pyrococcus horikoshii enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
20% conversion by the Pyrococcus horikoshii enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
20% conversion by the Pyrococcus horikoshii enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
20% conversion by the Pyrococcus horikoshii enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
20% conversion by the Pyrococcus horikoshii enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
20% conversion by the Pyrococcus horikoshii enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila
21% conversion by the Chaetomium thermophilum enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila CBS 144.50
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila CBS 144.50
21% conversion by the Chaetomium thermophilum enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila CBS 144.50
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila DSM 1495
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila DSM 1495
21% conversion by the Chaetomium thermophilum enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila DSM 1495
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila IMI 039719
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila IMI 039719
21% conversion by the Chaetomium thermophilum enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila IMI 039719
-
-
-
?
3-mer 2' phosphorylated RNA
?
-
pApa-(2-phosphate)pA, pUpU-(2-phosphate)pU, pAAA-(2-phosphate)p and pAAA-(2-phosphate)pOCH3
-
-
?
3-mer 2' phosphorylated RNA
?
-
pApA-(2-phosphate)pA, pApU-(2-phosphate)pA, pUpU-(2-phosphate)pU, pApApA-(2-phosphate),pApApA-(2-phosphate)p, pApApA-(2-phosphate)1OCH3
-
-
?
8-mer 2' phosphorylated RNA
?
-
-
-
-
?
8-mer 2' phosphorylated RNA
?
-
pGUAA-(2-phosphate)AUCU
-
-
?
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
enzyme ApeTpt1 catalyzes a one-step synthesis of a 5'-phospho-ADP-ribosylated cap structure (with no subsequent 5'-phosphotransferase step). ApeTpt1 caps RNA or DNA 5'-phosphate ends with ADP-ribose. pDNA and pRNA substrates are capped quantitatively at saturating enzyme in preence of NAD+. ApeTpt1 with 200 nM 10mer 5' 32P-labeled RNA or DNA oligonucleotides of identical nucleotide sequence (excepting T for U in DNA versus RNA) in the presence of 1 mM NAD+ resulted in the conversion of the substrates into RNA and DNA products of slower electrophoretic mobility. The 32P-labeled capped oligonucleotides are gel-purified and reacted with ApeTpt1 in the presence of 1 mM nicotinamide. This results in decapping of 20% of the ADPR-pDNA substrate to regenerate the pDNA strand
-
-
-
additional information
?
-
-
enzyme ApeTpt1 catalyzes a one-step synthesis of a 5'-phospho-ADP-ribosylated cap structure (with no subsequent 5'-phosphotransferase step). ApeTpt1 caps RNA or DNA 5'-phosphate ends with ADP-ribose. pDNA and pRNA substrates are capped quantitatively at saturating enzyme in preence of NAD+. ApeTpt1 with 200 nM 10mer 5' 32P-labeled RNA or DNA oligonucleotides of identical nucleotide sequence (excepting T for U in DNA versus RNA) in the presence of 1 mM NAD+ resulted in the conversion of the substrates into RNA and DNA products of slower electrophoretic mobility. The 32P-labeled capped oligonucleotides are gel-purified and reacted with ApeTpt1 in the presence of 1 mM nicotinamide. This results in decapping of 20% of the ADPR-pDNA substrate to regenerate the pDNA strand
-
-
-
additional information
?
-
enzyme ApeTpt1 catalyzes a one-step synthesis of a 5'-phospho-ADP-ribosylated cap structure (with no subsequent 5'-phosphotransferase step). ApeTpt1 caps RNA or DNA 5'-phosphate ends with ADP-ribose. pDNA and pRNA substrates are capped quantitatively at saturating enzyme in preence of NAD+. ApeTpt1 with 200 nM 10mer 5' 32P-labeled RNA or DNA oligonucleotides of identical nucleotide sequence (excepting T for U in DNA versus RNA) in the presence of 1 mM NAD+ resulted in the conversion of the substrates into RNA and DNA products of slower electrophoretic mobility. The 32P-labeled capped oligonucleotides are gel-purified and reacted with ApeTpt1 in the presence of 1 mM nicotinamide. This results in decapping of 20% of the ADPR-pDNA substrate to regenerate the pDNA strand
-
-
-
additional information
?
-
enzyme ApeTpt1 catalyzes a one-step synthesis of a 5'-phospho-ADP-ribosylated cap structure (with no subsequent 5'-phosphotransferase step). ApeTpt1 caps RNA or DNA 5'-phosphate ends with ADP-ribose. pDNA and pRNA substrates are capped quantitatively at saturating enzyme in preence of NAD+. ApeTpt1 with 200 nM 10mer 5' 32P-labeled RNA or DNA oligonucleotides of identical nucleotide sequence (excepting T for U in DNA versus RNA) in the presence of 1 mM NAD+ resulted in the conversion of the substrates into RNA and DNA products of slower electrophoretic mobility. The 32P-labeled capped oligonucleotides are gel-purified and reacted with ApeTpt1 in the presence of 1 mM nicotinamide. This results in decapping of 20% of the ADPR-pDNA substrate to regenerate the pDNA strand
-
-
-
additional information
?
-
enzyme ApeTpt1 catalyzes a one-step synthesis of a 5'-phospho-ADP-ribosylated cap structure (with no subsequent 5'-phosphotransferase step). ApeTpt1 caps RNA or DNA 5'-phosphate ends with ADP-ribose. pDNA and pRNA substrates are capped quantitatively at saturating enzyme in preence of NAD+. ApeTpt1 with 200 nM 10mer 5' 32P-labeled RNA or DNA oligonucleotides of identical nucleotide sequence (excepting T for U in DNA versus RNA) in the presence of 1 mM NAD+ resulted in the conversion of the substrates into RNA and DNA products of slower electrophoretic mobility. The 32P-labeled capped oligonucleotides are gel-purified and reacted with ApeTpt1 in the presence of 1 mM nicotinamide. This results in decapping of 20% of the ADPR-pDNA substrate to regenerate the pDNA strand
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-
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additional information
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enzyme ApeTpt1 catalyzes a one-step synthesis of a 5'-phospho-ADP-ribosylated cap structure (with no subsequent 5'-phosphotransferase step). ApeTpt1 caps RNA or DNA 5'-phosphate ends with ADP-ribose. pDNA and pRNA substrates are capped quantitatively at saturating enzyme in preence of NAD+. ApeTpt1 with 200 nM 10mer 5' 32P-labeled RNA or DNA oligonucleotides of identical nucleotide sequence (excepting T for U in DNA versus RNA) in the presence of 1 mM NAD+ resulted in the conversion of the substrates into RNA and DNA products of slower electrophoretic mobility. The 32P-labeled capped oligonucleotides are gel-purified and reacted with ApeTpt1 in the presence of 1 mM nicotinamide. This results in decapping of 20% of the ADPR-pDNA substrate to regenerate the pDNA strand
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additional information
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the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2''- to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
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additional information
?
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Comparison of incorporation of 3H-tyrosine and 35S-methionine/cysteine into total proteins confirms that wild-type and Trpt1-/-cells have similar incorporation rates of either amino acid.
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additional information
?
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the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances. Runella Tpt1 (RslTpt1) efficiently removes an internal 2'-phosphate from a DNA substrate. RslTpt1 removes the 2'-phosphate from the 2'-fluoroarabinonucleic acid (2'-FANA) substrate, albeit with about 7fold lower specific activity compared to the 6mer 2'-phosphate RNA control substrate. The 2'-phospho-ADP-ribosylated intermediate accumulates to an extent of 4% of total labeled RNA at low enzyme concentrations. Phosphorothioate (PS) modifications of the 3'-5'-phosphodiester backbone of DNA and 2'-FANA oligonucleotides (PS-DNA and PS-2'-FANA oligos) give substrates that are completely converted to 2'-hydroxy products by RslTpt1 but with reduced activity
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additional information
?
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Thermochaetoides thermophila
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
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additional information
?
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Thermochaetoides thermophila CBS 144.50
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
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additional information
?
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Thermochaetoides thermophila DSM 1495
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
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additional information
?
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Thermochaetoides thermophila IMI 039719
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
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additional information
?
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yeasts
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synthesis of 5'-Lv-2'-DMT-3'-phosphoramidite-G monomer containing an internal 2-phosphate for incorporation in synthetic RNA in order to construct a fluorescent oligoribonucleotide probe for a high throughput screening assay against yeast Tpt1p.
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2'-phospho-(ligated tRNA) + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide + H+
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2'-phospho-(ligated tRNA) + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide + H2O
yeasts
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enzyme catalyzes final step in tRNA splicing
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?
2'-phospho-(ligated tRNA) + NAD+
mature tRNA + ADP-ribose1'',2''-phosphate + nicotinamide + H2O
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last step in the pre-tRNA splicing process
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ir
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
additional information
?
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Comparison of incorporation of 3H-tyrosine and 35S-methionine/cysteine into total proteins confirms that wild-type and Trpt1-/-cells have similar incorporation rates of either amino acid.
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?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
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?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
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?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
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-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
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-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
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-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
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-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
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-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila
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?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila CBS 144.50
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?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila DSM 1495
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?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Thermochaetoides thermophila IMI 039719
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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metabolism
RNA repair enzymes catalyze rejoining of an RNA molecule after cleavage of phosphodiester linkages. RNA repair in budding yeast is catalyzed by two separate enzymes that process tRNA exons during their splicing and HAC1 mRNA exons during activation of the unfolded protein response (UPR). The RNA ligase Trl1 (EC 6.5.1.3) joins 2',3'-cyclic phosphate and 5'-hydroxyl RNA fragments, creating a phosphodiester linkage with a 2'-phosphate at the junction. The 2'-phosphate is removed by the 2'-phosphotransferase Tpt1 (EC 2.7.1.160)
evolution
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
Thermochaetoides thermophila
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
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evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
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evolution
Thermochaetoides thermophila IMI 039719
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
Thermochaetoides thermophila DSM 1495
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
Thermochaetoides thermophila CBS 144.50
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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malfunction
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
malfunction
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
malfunction
Thermochaetoides thermophila
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
malfunction
the essential functions of TRL1 and TPT1 in budding yeast are bypassed by expressing prespliced, intronless versions of the 10 normally intron-containing tRNAs, indicating this repair pathway does not have additional essential functions. Expression of intronless tRNAs fails to rescue the growth of cells with deletions in components of the SEN complex, implying an additional essential role for the splicing endonuclease. The trl1DELTA and tpt1DELTA mutants accumulate tRNA and HAC1 splicing intermediates indicative of RNA repair defects and are hypersensitive to drugs that inhibit translation. RNA repair mutants have defects in translation. tpt1DELTA mutants grow in the presence of tunicamycin despite reduced accumulation of spliced HAC1 mRNA, while failure to induce the unfolded protein response occurs in trl1DELTA cells grown with tunicamycin is lethal owing to their inability to ligate HAC1 after its cleavage by Ire1. Rescued trl1DELTA and tpt1DELTA cells, RNA repair mutants, have unique phenotypes for both tRNA splicing and HAC1 mRNA splicing during the unfolded protein response. The temperature sensitivity of RNA repair mutants at 37°C is not a consequence of tRNA decay pathway (RTD)
malfunction
Thermochaetoides thermophila IMI 039719
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
Thermochaetoides thermophila DSM 1495
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
Thermochaetoides thermophila CBS 144.50
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
physiological function
in bacteria NAD-dependent RNA 2'-phosphotransferase KptA might be an RNA processing enzyme able to repair the RNA damaged by toxic endoribonucleases
physiological function
-
in yeast the NAD-dependent RNA 2'-phosphotransferase KptA is known to participate in tRNA splicing by removing the splice junction 2'-phosphate from ligated tRNA
physiological function
the genomic organization of gene kptA suggests that KptA activity is strictly coordinated with the recycling to NAD of its reaction products
physiological function
-
enzyme Tpt1 catalyzes the transfer of an internal 2'-phosphate moiety (2'-PO4) from a branched 2'-phosphate RNA splice junction to NAD+ to form a clean 2'-hydroxy, 3'-5'-phosphodiester junction, ADP-ribose 1''-2'' cyclic phosphate, and nicotinamide. Recombinant expression of RslTpt1 in a yeast mutant complements a lethal tpt1DELTA knockout phenotype
physiological function
enzyme TPT1 is essential only in the context of the generation of 2'-phosphorylated tRNAs by Trl1
physiological function
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5' phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
physiological function
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
Thermochaetoides thermophila
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
-
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
physiological function
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
physiological function
Thermochaetoides thermophila
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2''- to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
physiological function
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate; and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5' phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5' phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
-
physiological function
Thermochaetoides thermophila IMI 039719
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
Thermochaetoides thermophila IMI 039719
-
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2''- to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
-
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
Thermochaetoides thermophila DSM 1495
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
Thermochaetoides thermophila DSM 1495
-
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2''- to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
-
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
-
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5' phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
-
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
-
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
-
physiological function
-
enzyme Tpt1 catalyzes the transfer of an internal 2'-phosphate moiety (2'-PO4) from a branched 2'-phosphate RNA splice junction to NAD+ to form a clean 2'-hydroxy, 3'-5'-phosphodiester junction, ADP-ribose 1''-2'' cyclic phosphate, and nicotinamide. Recombinant expression of RslTpt1 in a yeast mutant complements a lethal tpt1DELTA knockout phenotype
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
Thermochaetoides thermophila CBS 144.50
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
Thermochaetoides thermophila CBS 144.50
-
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2''- to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5' phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
-
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
physiological function
-
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
-
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
additional information
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologs catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2'- or 3'-terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction
additional information
Thermochaetoides thermophila
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction
additional information
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Runella slithyformis Tpt1 has a Arg-His-Arg-Arg catalytic tetrad in the active site
additional information
Thermochaetoides thermophila IMI 039719
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
additional information
Thermochaetoides thermophila DSM 1495
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
additional information
Thermochaetoides thermophila CBS 144.50
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
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Culver, G.M.; McCraith, S.M.; Consaul, S.A.; Stanford, D.R.; Phizicky, E.M.
A 2'-phosphotransferase implicated in tRNA splicing is essential in Saccharomyces cerevisiae
J. Biol. Chem.
272
13203-13210
1997
Saccharomyces cerevisiae, Saccharomyces cerevisiae (Q12272), Escherichia coli, Homo sapiens, Mus musculus, Schizosaccharomyces pombe
brenda
Steiger, M.A.; Kierzek, R.; Turner, D.H.; Phizicky, E.M.
Substrate recognition by a yeast 2'-phosphotransferase involved in tRNA splicing and by its Escherichia coli homolog
Biochemistry
40
14098-14105
2001
Saccharomyces cerevisiae, Escherichia coli
brenda
Hu, Q.D.; Lu, H.; Huo, K.; Ying, K.; Li, J.; Xie, Y.; Mao, Y.; Li, Y.Y.
A human homolog of the yeast gene encoding tRNA 2'-phosphotransferase: cloning, characterization and complementation analysis
Cell. Mol. Life Sci.
60
1725-1732
2003
Arabidopsis thaliana, Archaeoglobus fulgidus, Saccharomyces cerevisiae, Clostridium perfringens, Escherichia coli, Fusobacterium nucleatum, Homo sapiens, Homo sapiens (Q86TN4), Methanopyrus kandleri, Mus musculus, Rattus norvegicus, Schizosaccharomyces pombe, Streptomyces coelicolor
brenda
Mc Craith, S.M.; Phizicky, E.M.
An enzyme from Saccharomyces cerevisiae uses NAD+ to transfer the splice junction 2'-phosphate from ligated tRNA to an acceptor molecule
J. Biol. Chem.
266
11986-11992
1991
Saccharomyces cerevisiae
brenda
Zillman, M.; Gorovsky, M.A.; Phizicky, E.M.
HeLa cells contain a 2'-phosphate-specific phosphotransferase similar to a yeast enzyme implicated in tRNA splicing
J. Biol. Chem.
267
10289-10294
1992
Saccharomyces cerevisiae, Homo sapiens
brenda
Spinelli, S.L.; Kierzek, R.; Turner, D.H.; Phizicky, E.M.
Transient ADP-ribosylation of a 2'-phosphate implicated in its removal from ligated tRNA during splicing in yeast
J. Biol. Chem.
274
2637-2644
1999
Saccharomyces cerevisiae, Escherichia coli, Mus musculus
brenda
Kato-Murayama, M.; Bessho, Y.; Shirouzu, M.; Yokoyama, S.
Crystal structure of the RNA 2'-phosphotransferase from Aeropyrum pernix K1
J. Mol. Biol.
348
295-305
2005
Aeropyrum pernix, Arabidopsis thaliana, Archaeoglobus fulgidus, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Methanosarcina mazei, Pseudomonas aeruginosa, Pyrococcus horikoshii
brenda
Kierzek, R.; Steiger, M.A.; Spinelli, S.L.; Turner, D.H.; Phizicky, E.M.
The chemical synthesis of oligoribonucleotides with selectively placed 2'-O-phosphates
Nucleosides Nucleotides Nucleic Acids
19
917-933
2000
Saccharomyces cerevisiae
brenda
Spinelli, S.L.; Malik, H.S.; Consaul, S.A.; Phizicky, E.M.
A functional homolog of a yeast tRNA splicing enzyme is conserved in higher eukaryotes and in Escherichia coli
Proc. Natl. Acad. Sci. USA
95
14136-14141
1998
Arabidopsis thaliana, Archaeoglobus fulgidus, Saccharomyces cerevisiae, Candida albicans, Escherichia coli, Mus musculus, no activity in Bacillus subtilis, no activity in Haemophilus influenzae, no activity in Mycoplasma genitalium, Pseudomonas aeruginosa, Pyrococcus horikoshii, Schizosaccharomyces pombe, no activity in Helicobacter pylori
brenda
Sawaya, R.; Schwer, B.; Shuman, S.
Structure-function analysis of the yeast NAD+-dependent tRNA 2'-phosphotransferase Tpt1
RNA
11
107-113
2005
Aeropyrum pernix, Archaeoglobus fulgidus, Saccharomyces cerevisiae, Clostridium perfringens, Drosophila melanogaster, Escherichia coli, Homo sapiens, Leishmania major, Nostoc punctiforme, Pyrococcus horikoshii, Schizosaccharomyces pombe, Trypanosoma cruzi
brenda
Steiger, M.A.; Jackman, J.E.; Phizicky, E.M.
Analysis of 2'-phosphotransferase (Tpt1p) from Saccharomyces cerevisiae: evidence for a conserved two-step reaction mechanism
RNA
11
99-106
2005
Saccharomyces cerevisiae
brenda
Spinelli, S.L.; Consaul, S.A.; Phizicky, E.M.
A conditional lethal yeast phosphotransferase (tpt1) mutant accumulates tRNAs with a 2'-phosphate and an undermodified base at the splice junction
RNA
3
1388-1400
1997
Saccharomyces cerevisiae, Escherichia coli
brenda
Englert, M.; Latz, A.; Becker, D.; Gimple, O.; Beier, H.; Akama, K.
Plant pre-tRNA splicing enzymes are targeted to multiple cellular compartments
Biochimie
89
1351-1365
2007
Arabidopsis thaliana
brenda
Lackey, J.G.; Ron, D.; Damha, M.J.; Harding, H.P.
Toward the discovery of new antifungal agents: the design and validation of a novel 2P-RNA probe and high throughput screening assay against 2-phosphotransferase Tpt1p
Nucleic Acids Symp. Ser.
52
475-476
2008
yeasts
brenda
Harding, H.P.; Lackey, J.G.; Hsu, H.C.; Zhang, Y.; Deng, J.; Xu, R.M.; Damha, M.J.; Ron, D.
An intact unfolded protein response in Trpt1 knockout mice reveals phylogenic divergence in pathways for RNA ligation
RNA
14
225-232
2008
Mus musculus
brenda
Sorci, L.; Ruggieri, S.; Raffaelli, N.
NAD homeostasis in the bacterial response to DNA/RNA damage
DNA Repair
23
17-26
2014
Saccharomyces cerevisiae, Brachyspira hyodysenteriae (A0A3B6VB17), Flavobacterium johnsoniae (A5FLZ4), Herpetosiphon aurantiacus (A9B356), Delftia acidovorans (A9C0S5), Deinococcus deserti (C1CZ01), Catenulispora acidiphila (C7QAQ2), Sebaldella termitidis (D1APE3), Deinococcus gobiensis (H8GTD5), Fusobacterium nucleatum subsp. nucleatum (Q8R5N7), Agrobacterium tumefaciens (Q8U9Z2), Deinococcus radiodurans (Q9RRR1), Delftia acidovorans DSM 14801 (A9C0S5), Agrobacterium tumefaciens C58 / ATCC 33970 (Q8U9Z2), Brachyspira hyodysenteriae ATCC 49526 (A0A3B6VB17), Herpetosiphon aurantiacus DSM 785 (A9B356), Deinococcus gobiensis DSM 21396 (H8GTD5), Deinococcus radiodurans ATCC 13939 (Q9RRR1), Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847 (Q8R5N7), Deinococcus deserti DSM 17065 (C1CZ01), Sebaldella termitidis ATCC 33386 (D1APE3)
brenda
Munir, A.; Banerjee, A.; Shuman, S.
NAD+-dependent synthesis of a 5-phospho-ADP-ribosylated RNA/DNA cap by RNA 2-phosphotransferase Tpt1
Nucleic Acids Res.
46
9617-9624
2018
Runella slithyformis, Acetivibrio thermocellus (A3DJX6), Thermochaetoides thermophila (G0S5Z5), Archaeoglobus fulgidus (O29841), Pyrococcus horikoshii (O57899), Saccharomyces cerevisiae (Q12272), Homo sapiens (Q86TN4), Aeropyrum pernix (Q9YFP5), Aeropyrum pernix, Aeropyrum pernix ATCC 700893 (Q9YFP5), Aeropyrum pernix DSM 11879 (Q9YFP5), Thermochaetoides thermophila IMI 039719 (G0S5Z5), Acetivibrio thermocellus DSM 1237 (A3DJX6), Archaeoglobus fulgidus NBRC 100126 (O29841), Archaeoglobus fulgidus ATCC 49558 (O29841), Thermochaetoides thermophila DSM 1495 (G0S5Z5), Pyrococcus horikoshii DSM 12428 (O57899), Acetivibrio thermocellus JCM 9322 (A3DJX6), Acetivibrio thermocellus NBRC 103400 (A3DJX6), Aeropyrum pernix JCM 9820 (Q9YFP5), Pyrococcus horikoshii NBRC 100139 (O57899), Pyrococcus horikoshii JCM 9974 (O57899), Acetivibrio thermocellus ATCC 27405 (A3DJX6), Acetivibrio thermocellus VPI 7372 (A3DJX6), Archaeoglobus fulgidus VC-16 (O29841), Thermochaetoides thermophila CBS 144.50 (G0S5Z5), Aeropyrum pernix NBRC 100138 (Q9YFP5), Pyrococcus horikoshii ATCC 700860 (O57899), Acetivibrio thermocellus NCIMB 10682 (A3DJX6), Pyrococcus horikoshii OT-3 (O57899), Acetivibrio thermocellus NRRL B-4536 (A3DJX6), Archaeoglobus fulgidus JCM 9628 (O29841)
brenda
Munir, A.; Abdullahu, L.; Damha, M.J.; Shuman, S.
Two-step mechanism and step-arrest mutants of Runella slithyformis NAD+-dependent tRNA 2'-phosphotransferase Tpt1
RNA
24
1144-1157
2018
Runella slithyformis, Runella slithyformis ATCC 49304
brenda
Cherry, P.D.; White, L.K.; York, K.; Hesselberth, J.R.
Genetic bypass of essential RNA repair enzymes in budding yeast
RNA
24
313-323
2018
Saccharomyces cerevisiae (Q12272)
brenda
Dantuluri, S.; Abdullahu, L.; Munir, A.; Katolik, A.; Damha, M.J.; Shuman, S.
Substrate analogs that trap the 2'-phospho-ADP-ribosylated RNA intermediate of the Tpt1 (tRNA 2'-phosphotransferase) reaction pathway
RNA
26
373-381
2020
Runella slithyformis, Acetivibrio thermocellus (A3DJX6), Thermochaetoides thermophila (G0S5Z5), Homo sapiens (Q86TN4), Thermochaetoides thermophila IMI 039719 (G0S5Z5), Acetivibrio thermocellus DSM 1237 (A3DJX6), Thermochaetoides thermophila DSM 1495 (G0S5Z5), Acetivibrio thermocellus JCM 9322 (A3DJX6), Acetivibrio thermocellus NBRC 103400 (A3DJX6), Acetivibrio thermocellus ATCC 27405 (A3DJX6), Acetivibrio thermocellus VPI 7372 (A3DJX6), Thermochaetoides thermophila CBS 144.50 (G0S5Z5), Acetivibrio thermocellus NCIMB 10682 (A3DJX6), Acetivibrio thermocellus NRRL B-4536 (A3DJX6)
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