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S-adenosyl-L-methionine + guanine37 in tRNATrp
S-adenosyl-L-homocysteine + N2-methylguanine37 in tRNATrp
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S-adenosyl-L-methionine + guanine54 in tRNATrp
S-adenosyl-L-homocysteine + N2-methylguanine54 in tRNATrp
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S-adenosyl-L-methionine + guanine6 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA
S-adenosyl-L-methionine + guanine6 in tRNA(Phe)
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA(Phe)
S-adenosyl-L-methionine + guanine6 in tRNACys
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNACys
S-adenosyl-L-methionine + guanine67 in tRNATrp
S-adenosyl-L-homocysteine + N2-methylguanine67 in tRNATrp
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S-adenosyl-L-methionine + guanine8 in tRNATrp
S-adenosyl-L-homocysteine + N2-methylguanine8 in tRNATrp
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additional information
?
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S-adenosyl-L-methionine + guanine6 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA
the enzyme specifically modifies tRNAPhe at guanosine 6 in the tRNA acceptor stem
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S-adenosyl-L-methionine + guanine6 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA
the enzyme specifically modifies tRNAPhe at guanosine 6 in the tRNA acceptor stem. Contribution of the THUMP domain in tRNA recognition and catalysis, substrate binding and ligand-induced conformational changes in the RFM domain
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S-adenosyl-L-methionine + guanine6 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA
the enzyme specifically modifies tRNAPhe at guanosine 6 in the tRNA acceptor stem
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S-adenosyl-L-methionine + guanine6 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA
the enzyme specifically modifies tRNAPhe at guanosine 6 in the tRNA acceptor stem. Contribution of the THUMP domain in tRNA recognition and catalysis, substrate binding and ligand-induced conformational changes in the RFM domain, overview
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S-adenosyl-L-methionine + guanine6 in tRNA(Phe)
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA(Phe)
production of a small amount of N2-dimethylguanine6 in tRNA(Phe)
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?
S-adenosyl-L-methionine + guanine6 in tRNA(Phe)
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA(Phe)
production of a small amount of N2-dimethylguanine6 in tRNA(Phe)
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?
S-adenosyl-L-methionine + guanine6 in tRNA(Phe)
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA(Phe)
production of a small amount of N2-dimethylguanine6 in tRNA(Phe)
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?
S-adenosyl-L-methionine + guanine6 in tRNACys
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNACys
Trm14 generates m2G at position 6 in tRNACys
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?
S-adenosyl-L-methionine + guanine6 in tRNACys
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNACys
wild-type or G6A/C67U tRNACys transcripts as substrates, Trm14 generates m2G at position 6 in tRNACys, i.e. tRNACys m2G6-forming activity
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S-adenosyl-L-methionine + guanine6 in tRNACys
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNACys
Trm14 generates m2G at position 6 in tRNACys
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?
S-adenosyl-L-methionine + guanine6 in tRNACys
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNACys
wild-type or G6A/C67U tRNACys transcripts as substrates, Trm14 generates m2G at position 6 in tRNACys, i.e. tRNACys m2G6-forming activity
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additional information
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active site structure with bound ligands, S-adenosyl-L-methionine, S-adenosyl-L-homocysteine, and sinefungin, overview
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additional information
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active site structure with bound ligands, S-adenosyl-L-methionine, S-adenosyl-L-homocysteine, and sinefungin, overview
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additional information
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docking model of TrmN in complex with tRNAPhe of Thermus thermophilus
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additional information
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docking model of TrmN in complex with tRNAPhe of Thermus thermophilus
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S-adenosyl-L-methionine + guanine6 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA
S-adenosyl-L-methionine + guanine6 in tRNACys
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNACys
S-adenosyl-L-methionine + guanine67 in tRNATrp
S-adenosyl-L-homocysteine + N2-methylguanine67 in tRNATrp
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?
S-adenosyl-L-methionine + guanine6 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA
the enzyme specifically modifies tRNAPhe at guanosine 6 in the tRNA acceptor stem
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?
S-adenosyl-L-methionine + guanine6 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA
the enzyme specifically modifies tRNAPhe at guanosine 6 in the tRNA acceptor stem
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?
S-adenosyl-L-methionine + guanine6 in tRNACys
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNACys
Trm14 generates m2G at position 6 in tRNACys
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?
S-adenosyl-L-methionine + guanine6 in tRNACys
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNACys
Trm14 generates m2G at position 6 in tRNACys
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evolution
RNA MTases from the TrmN/Trm14 family are present in archaea, bacteria and eukaryota and all specifically modify tRNAPhe at guanosine 6 in the tRNA acceptor stem. RNA MTases can be classified into four superfamilies, overview
evolution
RNA MTases from the TrmN/Trm14 family are present in archaea, bacteria and eukaryota and all specifically modify tRNAPhe at guanosine 6 in the tRNA acceptor stem. RNA MTases can be classified into four superfamilies, overview
evolution
Trm14 is associated with cluster of orthologous groups, COG, 0116, and most closely resembles the m2G10 tRNA methylase Trm11. Phylogenetic analysis reveals a canonical archaeal/bacterial evolutionary separation with 20-30% sequence identities between the two branches, but it is likely that the detailed functions of COG 0116 enzymes differ between the archaeal and bacterial domains. Phylogenetic distribution of Trm14-like proteins, overview
evolution
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a distinct tRNA 2'-O-methyltransferase, which methylates the 2'-OH of ribose at position 6 in tRNA and does not differentiate between adenine and cytosine, may exist in Thermococcus and Pyrococcus genera. In terms of the other enzymes responsible for the observed 2'-O-methylations, Cm56 is a product of Trm56 (EC 2.1.1.206)
evolution
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Trm14 is associated with cluster of orthologous groups, COG, 0116, and most closely resembles the m2G10 tRNA methylase Trm11. Phylogenetic analysis reveals a canonical archaeal/bacterial evolutionary separation with 20-30% sequence identities between the two branches, but it is likely that the detailed functions of COG 0116 enzymes differ between the archaeal and bacterial domains. Phylogenetic distribution of Trm14-like proteins, overview
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malfunction
inactivation of the trmN gene leads to a total absence of N2-methylguanine in tRNA but did not affect cell growth or the formation of other modified nucleosides in tRNA(Phe). Therefore, m2G6 does not appear to be involved in an essential function
malfunction
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the lack of 2-methylguanosine (m2G) at position 67 in the trm11 trm14 double disruptant strain suggests that this methylation is mediated by m2G6 methyltransferase Trm14
malfunction
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inactivation of the trmN gene leads to a total absence of N2-methylguanine in tRNA but did not affect cell growth or the formation of other modified nucleosides in tRNA(Phe). Therefore, m2G6 does not appear to be involved in an essential function
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physiological function
tRNA m2G6 formation may play a role in stabilizing the structure of the RNA and function synergistically with these core-region modifications to stabilize the molecule against thermal stress. Also, Trm14-catalyzed m2G6 formation in tRNACys may play a role in modulating the aminoacylation efficiency of phosphoseryl-tRNA synthetase, i.e. SepRS. Control of SepRS (or CysRS) activity by SAM-dependent methylation of tRNACys might provide the methanogen cell with a regulatory mechanism by which protein synthesis rates can respond to environmental sulfur levels or to concentrations of sulfur metabolites
physiological function
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the trm14 gene is responsible for the m2G67 modification. The modification site (G67) forms a Watson-Crick base pair with C6 in tRNA. Archaeal Trm14 methylates G6 in tRNA and contains a THUMP domain, which often recognizes the CCA terminus in tRNA. But it has not been confirmed that Thermococcus kodakarensis Trm14 methylates G6 in tRNA like Methanocaldococcus jannaschii Trm14. Furthermore, the presence of m2G6 modification in Thermococcus kodakarensis tRNAs is not confirmed. In total, trm14 is responsible for m2G at positions 8, 54, 37, and 67, respectively, as determined by analysis of tRNATrp from gene disruptant strains
physiological function
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tRNA m2G6 formation may play a role in stabilizing the structure of the RNA and function synergistically with these core-region modifications to stabilize the molecule against thermal stress. Also, Trm14-catalyzed m2G6 formation in tRNACys may play a role in modulating the aminoacylation efficiency of phosphoseryl-tRNA synthetase, i.e. SepRS. Control of SepRS (or CysRS) activity by SAM-dependent methylation of tRNACys might provide the methanogen cell with a regulatory mechanism by which protein synthesis rates can respond to environmental sulfur levels or to concentrations of sulfur metabolites
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monomer
1 * 39143, calculated from sequence
monomer
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1 * 39143, calculated from sequence
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additional information
the 381 amino acid Trm14 protein possesses a canonical RNA recognition THUMP domain at the N-terminus, followed by a gamma-class Rossmann fold amino-methyltransferase catalytic domain featuring the signature NPPY active site motif
additional information
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the 381 amino acid Trm14 protein possesses a canonical RNA recognition THUMP domain at the N-terminus, followed by a gamma-class Rossmann fold amino-methyltransferase catalytic domain featuring the signature NPPY active site motif
additional information
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the 381 amino acid Trm14 protein possesses a canonical RNA recognition THUMP domain at the N-terminus, followed by a gamma-class Rossmann fold amino-methyltransferase catalytic domain featuring the signature NPPY active site motif
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additional information
the enzyme consists of an N-terminal THUMP domain fused to a catalytic Rossmann-fold MTase domain, with the main tRNA binding surface in a groove between the THUMP domain and the MTase domain, secondary sequence comparison, overview
additional information
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the enzyme consists of an N-terminal THUMP domain fused to a catalytic Rossmann-fold MTase domain, with the main tRNA binding surface in a groove between the THUMP domain and the MTase domain, secondary sequence comparison, overview
additional information
the enzyme consists of an N-terminal THUMP domain fused to a catalytic Rossmann-fold MTase domain, with the main tRNA binding surface in a groove between the THUMP domain and the MTase domain, secondary sequence comparison, overview
additional information
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the enzyme consists of an N-terminal THUMP domain fused to a catalytic Rossmann-fold MTase domain, with the main tRNA binding surface in a groove between the THUMP domain and the MTase domain, secondary sequence comparison, overview
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purified recombinant detagged enzyme in complex with S-adenosyl-L-methionine or reaction product S-adenosyl-homocysteine, and inhibitor sinefungin, hanging drop vapor diffusion, protein in 50 mM Tris-HCl, pH 8.0, 10 mM MgCl2, 500 mM NaCl, 280 mM imidazole, and 1 mM DTT, mixing in a 1:1 ratio with crystallization solution containing 100 mM Tris-acetate, pH 8.0, 32% PEG 4000, and 15% glycerol, for the phasing, selenomethionine-derivatized PfTrm14 is crystallized in a crystallization solution containing 100 mM Tris-acetate, pH 8.0, 32% PEG 4000, 15% glycerol, after streak seeding from a native PfTrm14 crystal, crystal soaking in mother liquor containing 1 mM ligand, X-ray diffraction structure determination and analysis at 1.95-2.4 A resolution
purified recombinant His-tagged enzyme in complex with S-adenosyl-L-methionine or reaction product S-adenosyl-homocysteine, and inhibitor sinefungin, hanging drop vapor diffusion, protein in 50 mM Tris-HCl, pH 8.0, 250 mM NaCl, and 350 mM imidazole, mixing in a 1:1 ratio with crystallization solution 100 mM citrate/phosphate, pH 3.5, 15% PEG 6000, 200 mM NaCl, and 100 mM sodium citrate, crystal soaking in mother liquor containing 1 mM ligand, X-ray diffraction structure determination and analysis at 2.16 A resolution, solved in the apo state by molecular replacement to a resolution of 2.05 A
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Menezes, S.; Gaston, K.W.; Krivos, K.L.; Apolinario, E.E.; Reich, N.O.; Sowers, K.R.; Limbach, P.A.; Perona, J.J.
Formation of m2G6 in Methanocaldococcus jannaschii tRNA catalyzed by the novel methyltransferase Trm14
Nucleic Acids Res.
39
7641-7655
2011
Methanocaldococcus jannaschii (Q57880), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii JAL-1 (Q57880)
brenda
Fislage, M.; Roovers, M.; Tuszynska, I.; Bujnicki, J.M.; Droogmans, L.; Versees, W.
Crystal structures of the tRNA:m2G6 methyltransferase Trm14/TrmN from two domains of life
Nucleic Acids Res.
40
5149-5161
2012
Thermus thermophilus (Q72IH5), Thermus thermophilus, Pyrococcus furiosus (Q8U248), Pyrococcus furiosus
brenda
Roovers, M.; Oudjama, Y.; Fislage, M.; Bujnicki, J.; Verses, W.; Droogmans, L.
The open reading frame TTC1157 of Thermus thermophilus HB27 encodes the methyltransferase forming N 2-methylguanosine at position 6 in tRNA
RNA
18
815-824
2012
Thermus thermophilus (Q72IH5), Thermus thermophilus, Pyrococcus furiosus (Q8U248), Pyrococcus furiosus, Thermus thermophilus DSM 7039 (Q72IH5)
brenda
Hirata, A.; Suzuki, T.; Nagano, T.; Fujii, D.; Okamoto, M.; Sora, M.; Lowe, T.M.; Kanai, T.; Atomi, H.; Suzuki, T.; Hori, H.
Distinct modified nucleosides in tRNATrp from thehyperthermophilic archaeon Thermococcus kodakarensis and requirement of tRNA m2G10/m22G10 methyltransferase (archaeal Trm11) for survival at high temperatures
J. Bacteriol.
201
e00448-19
2019
Thermococcus kodakarensis
brenda