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S-adenosyl-L-methionine + adenine22 in Bacillus subtilis tRNA(Ser)
S-adenosyl-L-homocysteine + N1-methyladenine22 in Bacillus subtilis tRNA(Ser)
crude Escherichia coli tRNA is used, since it does not contain m1A22
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
S-adenosyl-L-methionine + adenine22 in tRNATyr
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNATyr
additional information
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
a methyl group at position N1 prevents Watson-Crick-type base pairing by adenosine and is therefore important for regulation of structure and stability of tRNA molecules
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
crude Escherichia coli tRNA is used, since it does not contain m1A22
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
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S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
interaction of BstRNASer with BsTrmK/SAH is deciphered by NMR. The tRNASer produced in Escherichia coli is less efficiently modified than the unmodified tRNASer
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S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
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S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
interaction of BstRNASer with BsTrmK/SAH is deciphered by NMR. The tRNASer produced in Escherichia coli is less efficiently modified than the unmodified tRNASer
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S-adenosyl-L-methionine + adenine22 in tRNATyr
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNATyr
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S-adenosyl-L-methionine + adenine22 in tRNATyr
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNATyr
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additional information
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the methyltransferase TrmK (BsTrmK) is responsible for the formation of m1A22 in tRNA. BsTrmK displays a broad substrate specificity, and methylates seven out of eight tRNA isoacceptor families of Bacillus subtilis bearing an A22. In addition to a non-Watson-Crick base-pair between the target A22 and a purine at position 13, the formation of m1A22 by BsTrmK requires a full-length tRNA with intact tRNA elbow and anticodon stem. Measurements of the MTase activity using 32P-radiolabelled Bacillus subtilis tRNAs. Interaction between BsTrmK and the cofactor product S-adenosyl-L-homocysteine (SAH) is enthalpy-driven with a single binding site and a dissociation constant (KD) of 0.0017 mM, residues R9, L10, G77, D78, A94 and G95 are involved in SAH binding
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additional information
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the methyltransferase TrmK (BsTrmK) is responsible for the formation of m1A22 in tRNA. BsTrmK displays a broad substrate specificity, and methylates seven out of eight tRNA isoacceptor families of Bacillus subtilis bearing an A22. In addition to a non-Watson-Crick base-pair between the target A22 and a purine at position 13, the formation of m1A22 by BsTrmK requires a full-length tRNA with intact tRNA elbow and anticodon stem. Measurements of the MTase activity using 32P-radiolabelled Bacillus subtilis tRNAs. Interaction between BsTrmK and the cofactor product S-adenosyl-L-homocysteine (SAH) is enthalpy-driven with a single binding site and a dissociation constant (KD) of 0.0017 mM, residues R9, L10, G77, D78, A94 and G95 are involved in SAH binding
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additional information
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the methyltransferase TrmK (BsTrmK) is responsible for the formation of m1A22 in tRNA. BsTrmK displays a broad substrate specificity, and methylates seven out of eight tRNA isoacceptor families of Bacillus subtilis bearing an A22. In addition to a non-Watson-Crick base-pair between the target A22 and a purine at position 13, the formation of m1A22 by BsTrmK requires a full-length tRNA with intact tRNA elbow and anticodon stem. Measurements of the MTase activity using 32P-radiolabelled Bacillus subtilis tRNAs. Interaction between BsTrmK and the cofactor product S-adenosyl-L-homocysteine (SAH) is enthalpy-driven with a single binding site and a dissociation constant (KD) of 0.0017 mM, residues R9, L10, G77, D78, A94 and G95 are involved in SAH binding
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
a methyl group at position N1 prevents Watson-Crick-type base pairing by adenosine and is therefore important for regulation of structure and stability of tRNA molecules
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNA
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S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
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S-adenosyl-L-methionine + adenine22 in tRNASer
S-adenosyl-L-homocysteine + N1-methyladenine22 in tRNASer
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
Bacillus subtilis TrmK belongs to the COG2384 (cluster of orthologous groups). The members of this family are found in Gram-negative and Gram-positive bacteria. Their sequences are well-conserved in many bacterial pathogens
evolution
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the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria
evolution
the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria
evolution
the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria
evolution
the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria
evolution
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Bacillus subtilis TrmK belongs to the COG2384 (cluster of orthologous groups). The members of this family are found in Gram-negative and Gram-positive bacteria. Their sequences are well-conserved in many bacterial pathogens
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evolution
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the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria
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metabolism
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the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding
metabolism
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding
metabolism
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding
metabolism
the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding
metabolism
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the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding
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physiological function
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the enzyme is essential for the bacterial survival
physiological function
the enzyme is essential for the bacterial survival
physiological function
the enzyme is essential for the bacterial survival
physiological function
the enzyme is essential for the bacterial survival
physiological function
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the enzyme is essential for the bacterial survival
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additional information
NMR chemical shift mapping is used to get insight on the protein-RNA recognition mode
additional information
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NMR chemical shift mapping is used to get insight on the protein-RNA recognition mode
additional information
the crystal structure of BsTrmK shows an N-terminal catalytic domain harbouring the typical Rossmann-like fold of Class-I methyltransferases and a C-terminal coiled-coil domain. Docking of BstRNASer to BsTrmK in complex with its methyldonor cofactor S-adenosyl-L-methionine (SAM) by NMR chemical shift mapping, modelling, overview. Both domains of BsTrmK participate in tRNA binding. BsTrmK recognises tRNA with very few structural changes in both partner, the non-Watson-Crick R13-A22 base-pair positioning the A22 N1-atom close to the SAM methyl group. BsTrmK requires the intact three-dimensional structure of tRNA to catalyse m1A22 formation
additional information
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the crystal structure of BsTrmK shows an N-terminal catalytic domain harbouring the typical Rossmann-like fold of Class-I methyltransferases and a C-terminal coiled-coil domain. Docking of BstRNASer to BsTrmK in complex with its methyldonor cofactor S-adenosyl-L-methionine (SAM) by NMR chemical shift mapping, modelling, overview. Both domains of BsTrmK participate in tRNA binding. BsTrmK recognises tRNA with very few structural changes in both partner, the non-Watson-Crick R13-A22 base-pair positioning the A22 N1-atom close to the SAM methyl group. BsTrmK requires the intact three-dimensional structure of tRNA to catalyse m1A22 formation
additional information
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NMR chemical shift mapping is used to get insight on the protein-RNA recognition mode
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additional information
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the crystal structure of BsTrmK shows an N-terminal catalytic domain harbouring the typical Rossmann-like fold of Class-I methyltransferases and a C-terminal coiled-coil domain. Docking of BstRNASer to BsTrmK in complex with its methyldonor cofactor S-adenosyl-L-methionine (SAM) by NMR chemical shift mapping, modelling, overview. Both domains of BsTrmK participate in tRNA binding. BsTrmK recognises tRNA with very few structural changes in both partner, the non-Watson-Crick R13-A22 base-pair positioning the A22 N1-atom close to the SAM methyl group. BsTrmK requires the intact three-dimensional structure of tRNA to catalyse m1A22 formation
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monomer
BsTrmK is active as a monomer, the higher oligomeric states of BsTrmK are formed via disulphide bonds involving the two cysteines in BsTrmK sequence at positions 35 and 152. Such bonds can be broken by addition of a reducing-agent, and addition of DTT to the MTase reaction buffer results in a dramatic increase of the enzymatic activity
monomer
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BsTrmK is active as a monomer, the higher oligomeric states of BsTrmK are formed via disulphide bonds involving the two cysteines in BsTrmK sequence at positions 35 and 152. Such bonds can be broken by addition of a reducing-agent, and addition of DTT to the MTase reaction buffer results in a dramatic increase of the enzymatic activity
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monomer
Sp1610 exists as a monomer both in solution and in the P212121 crystal
additional information
backbone 1H, 15N and 13C chemical shift assignments of TrmK from Bacillus subtilis obtained by heteronuclear multidimensional NMR spectroscopy as well as its secondary structure in solution, overview
additional information
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backbone 1H, 15N and 13C chemical shift assignments of TrmK from Bacillus subtilis obtained by heteronuclear multidimensional NMR spectroscopy as well as its secondary structure in solution, overview
additional information
BsTrmK consists of an N-terminal Class I MTase domain linked to a C-terminal coiled-coil domain, structure comparisons, overview
additional information
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BsTrmK consists of an N-terminal Class I MTase domain linked to a C-terminal coiled-coil domain, structure comparisons, overview
additional information
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backbone 1H, 15N and 13C chemical shift assignments of TrmK from Bacillus subtilis obtained by heteronuclear multidimensional NMR spectroscopy as well as its secondary structure in solution, overview
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additional information
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BsTrmK consists of an N-terminal Class I MTase domain linked to a C-terminal coiled-coil domain, structure comparisons, overview
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
sitting drop vapor diffusion method, mixing of 0.0016 ml of 3 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 500 mM NaCl, and 2% glycerol, with crystallization solution containing 0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate, pH 5.0, 30% w/v PEG 4000, and 8% 2-methyl-2,4-pentanediol, and equuilibration against 0.1 ml reservoir solution, microseeding, 4°C, X-ray diffraction structure determination and analysis, molecular replacement using structures of sp1610 (Streptococcus pneumoniae orthologue of BsTrmK, PDB code 3KR9), LMOf2365 1472 (Listeria Monocytogens, PDB code 3GNL) and of SAG1203 (Streptococcus agalactiae, PDB code: 3LEC) as templates, modelling
crystal structure of Sp1610 in the ligand-free and the AdoMet-bound forms at resolutions of 2.0 and 3.0 A, microbatch method
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Roovers, M.; Kaminska, K.H.; Tkaczuk, K.L.; Gigot, D.; Droogmans, L.; Bujnicki, J.M.
The YqfN protein of Bacillus subtilis is the tRNA: m1A22 methyltransferase (TrmK)
Nucleic Acids Res.
36
3252-3262
2008
Bacillus subtilis (P54471), Bacillus subtilis
brenda
Ta, H.M.; Kim, K.K.
Crystal structure of Streptococcus pneumoniae Sp1610, a putative tRNA methyltransferase, in complex with S-adenosyl-L-methionine
Protein Sci.
19
617-624
2010
Streptococcus pneumoniae (A0A0H2UR54), Streptococcus pneumoniae
brenda
Degut, C.; Barraud, P.; Larue, V.; Tisne, C.
Backbone resonance assignments of the m1A22 tRNA methyltransferase TrmK from Bacillus subtilis
Biomol. NMR Assign.
10
253-257
2016
Bacillus subtilis (P54471), Bacillus subtilis, Bacillus subtilis 168 (P54471)
brenda
Oerum, S.; Degut, C.; Barraud, P.; Tisne, C.
m1A Post-transcriptional modification in tRNAs
Biomolecules
7
20
2017
Streptococcus pneumoniae, Staphylococcus aureus (A0A0D6HIR7), Listeria monocytogenes serotype 4b (A0A0E1R6X8), Vibrio cholerae (A0A0H6U323), Listeria monocytogenes serotype 4b LL195 (A0A0E1R6X8)
brenda
Degut, C.; Roovers, M.; Barraud, P.; Brachet, F.; Feller, A.; Larue, V.; Al Refaii, A.; Caillet, J.; Droogmans, L.; Tisne, C.
Structural characterization of B. subtilis m1A22 tRNA methyltransferase TrmK insights into tRNA recognition
Nucleic Acids Res.
47
4736-4750
2019
no activity in Escherichia coli, Bacillus subtilis (P54471), Bacillus subtilis, Bacillus subtilis 168 (P54471)
brenda