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S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
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S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
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S-adenosyl-L-methionine + cytosine40 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA precursor
mini-tRNAPhe (composed of the anticodon stem-loop extended by the intron) is used to test the formation of m5C40. The formation of m5C40 is strictly intron dependent
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?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
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cf. EC 2.1.1.203
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?
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
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the entire intron, or the total precursor tRNA structure, is required for efficient suppressor function of the resultant mature tRNA. The reduced suppressor phenotype is correlated with lack of a 5-methylcytosine modification of the anticodon wobble base
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S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
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?
S-adenosyl-L-methionine + cytosine40 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA precursor
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the enzymatic formation of m5C at position 40 in the anticodon stem is strictly dependent on the presence of the intron. Enzymatic formation of m5C40 is independent of the whole architecture of the tRNA molecule and takes place on a minisubstrate composed of the anticodon stem nd loop of yeast tRNAPhe prolonged by its natural 19 nt intron
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S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
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?
S-adenosyl-L-methionine + cytosine48 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAHis
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
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yeast tRNA(GAA)
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?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
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S-adenosyl-L-methionine + cytosine50 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAHis
additional information
?
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S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
mini-tRNALeu (composed of the anticodon stem-loop extended by the intron) is used to test the formation of m5C34. The formation of m5C34 is strictly intron dependent
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?
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
yeast pre-tRNALeu
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?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
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?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
tRNATyr(GUA), tRNASer(AGA), and tRNAIle(UAU) are used to test the formation of m5C48
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?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
yeast tRNASer(AGE)
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?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
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?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
tRNAPhe(GAA) and tRNAAsp(GUC) are used to test the formation of m5C49
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?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
yeast tRNAAsp(GUC)
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?
S-adenosyl-L-methionine + cytosine48 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAHis
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S-adenosyl-L-methionine + cytosine48 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAHis
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purified tRNAHis, secondary structure of mature Saccharomyces cerevisiae tRNAHis, overview
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?
S-adenosyl-L-methionine + cytosine50 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAHis
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?
S-adenosyl-L-methionine + cytosine50 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAHis
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purified tRNAHis, secondary structure of mature Saccharomyces cerevisiae tRNAHis, overview
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?
additional information
?
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a catalytic model for the RNA m5C methyltransferases that utilizes both conserved cysteines. The TC-Cys is proposed to perform covalent catalysis while the PC-Cys plays an important role in product release
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additional information
?
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Cys310 of motif VI is likely the nucleophilic catalyst of Trm4p
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?
additional information
?
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the enzyme Trm4 fabricate 5-methylcytosine (m5C) in RNA molecules utilizing a dual-cysteine catalytic mechanism
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?
additional information
?
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the enzyme forms covalent complexes with previously methylated RNA requiring S-adenosyl-L-homocysteine, the removal of this metabolite results in the disassembly of preexisting complexes
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
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?
S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
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?
S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
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-
?
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
the enzyme is responsible for complete m5C methylation of yeast tRNA. The frequency of modification depends on the cytosine position in tRNA. At positions 34 and 40, m5C is found only in two yeast tRNAs (tRNALeu (CUA) and tRNAPhe (GAA), respectively), whereas most other elongator yeast tRNAs bear either m5C48 or m5C49, but never both in the same tRNA molecule
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?
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA
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cf. EC 2.1.1.203
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S-adenosyl-L-methionine + cytosine40 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine40 in tRNA
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S-adenosyl-L-methionine + cytosine48 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNA
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S-adenosyl-L-methionine + cytosine48 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine48 in tRNAHis
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S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
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?
S-adenosyl-L-methionine + cytosine50 in tRNAHis
S-adenosyl-L-homocysteine + 5-methylcytosine50 in tRNAHis
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additional information
?
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the enzyme Trm4 fabricate 5-methylcytosine (m5C) in RNA molecules utilizing a dual-cysteine catalytic mechanism
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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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malfunction
disruption of the ORF YBL024w leads to the complete absence of m5C in total yeast tRNA. No tRNA:m5C-methyltransferase activity towards all potential m5C methylation sites is detected in the extract of the disrupted yeast strain. The protein product of a single gene is responsible for complete m5C methylation of yeast tRNA
physiological function
the enzyme is responsible for complete m5C methylation of yeast tRNA
malfunction
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yeast strains depleted of tRNAHis guanylyltransferase accumulate uncharged tRNAHis lacking the G-1 residue and subsequently accumulate additional 5-methylcytidine (m5C) at residues C48 and C50 of tRNAHis, due to the activity of the m5Cmethyltransferase Trm4. The increase in tRNAHis m5C levels does not require loss of Thg1, loss of G-1 of tRNAHis, or cell death but is associated with growth arrest following different stress conditions. Substantially increased tRNAHis m5C levels occur after temperature-sensitive strains are grown at nonpermissive temperature, and after wild-type strains are grown to stationary phase, starved for required amino acids, or treated with rapamycin. More modest accumulations of m5C in tRNAHis occur after starvation for glucose and after starvation for uracil. In virtually all cases examined, the additional m5C on tRNAHis occurs while cells are fully viable, and the increase is neither due to the GCN4 pathway, nor to increased Trm4 levels, phenotypes, overview. The increased amount of m5C is specific to tRNAHis. tRNAVal(AAC), which also normally has unmodified C48 and C50 residues adjacent to m5C49, has only marginally increased levels of m5C 7 h after temperature shift in the fcp1-1ts mutant
metabolism
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formation of a covalent complex between dual-cysteine RNA:m5C methyltransferases and methylated RNA provides a unique means by which metabolic factors can influence RNA. By controlling the degree of formation of the enzyme-RNA covalent complex, S-adenosyl-L-homocysteine and pH are likely to influence the extent of m5C formation and the rate of release of methylated RNA from RNA:m5C methyltransferases. Metabolite-induced covalent complexes could plausibly affect the processing and function of m5C-containing RNAs
metabolism
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the GCN4 pathway is not responsible for additional m5C levels on tRNAHis
additional information
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four active-site residues critical for Trm4p-mediated tRNA methylation are also required for the formation of the denaturant-resistant complexes with m5C-containing RNA
additional information
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tRNAHis m5C levels are unusually responsive to yeast growth conditions
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Motorin, Y.; Grosjean, H.
Multisite-specific tRNA:m5C-methyltransferase (Trm4) in yeast Saccharomyces cerevisiae: identification of the gene and substrate specificity of the enzyme
RNA
5
1105-1118
1999
Saccharomyces cerevisiae (P38205), Saccharomyces cerevisiae
brenda
King, M.Y.; Redman, K.L.
RNA methyltransferases utilize two cysteine residues in the formation of 5-methylcytosine
Biochemistry
41
11218-11225
2002
Saccharomyces cerevisiae
brenda
Redman, K.L.
Assembly of protein-RNA complexes using natural RNA and mutant forms of an RNA cytosine methyltransferase
Biomacromolecules
7
3321-3326
2006
Saccharomyces cerevisiae
brenda
Strobel, M.C.; Abelson, J.
Effect of intron mutations on processing and function of Saccharomyces cerevisiae SUP53 tRNA in vitro and in vivo
Mol. Cell. Biol.
6
2663-2673
1986
Saccharomyces cerevisiae
brenda
Jiang, H.Q.; Motorin, Y.; Jin, Y.X.; Grosjean, H.
Pleiotropic effects of intron removal on base modification pattern of yeast tRNAPhe: an in vitro study
Nucleic Acids Res.
25
2694-2701
1997
Saccharomyces cerevisiae, Saccharomyces cerevisiae Pp1001
brenda
Brzezicha, B.; Schmidt, M.; Makalowska, I.; Jarmolowski, A.; Pienkowska, J.; Szweykowska-Kulinska, Z.
Identification of human tRNA:m5C methyltransferase catalysing intron-dependent m5C formation in the first position of the anticodon of the pre-tRNA Leu(CAA)
Nucleic Acids Res.
34
6034-6043
2006
Saccharomyces cerevisiae (P38205), Saccharomyces cerevisiae
brenda
Walbott, H.; Husson, C.; Auxilien, S.; Golinelli-Pimpaneau, B.
Cysteine of sequence motif VI is essential for nucleophilic catalysis by yeast tRNA m5C methyltransferase
RNA
13
967-973
2007
Saccharomyces cerevisiae
brenda
Moon, H.J.; Redman, K.L.
Trm4 and Nsun2 RNA:m5C methyltransferases form metabolite-dependent, covalent adducts with previously methylated RNA
Biochemistry
53
7132-7144
2014
Saccharomyces cerevisiae
brenda
Preston, M.; DSilva, S.; Kon, Y.; Phizicky, E.
TRNAHis 5-methylcytidine levels increase in response to several growth arrest conditions in Saccharomyces cerevisiae
RNA
19
243-256
2013
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda