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Literature summary for 2.1.1.205 extracted from

  • Hirata, A.; Okada, K.; Yoshii, K.; Shiraishi, H.; Saijo, S.; Yonezawa, K.; Shimizu, N.; Hori, H.
    Structure of tRNA methyltransferase complex of Trm7 and Trm734 reveals a novel binding interface for tRNA recognition (2019), Nucleic Acids Res., 47, 10942-10955 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.205

Cloned(Commentary)

Cloned (Comment) Organism
gene trm7, recombinant expression of trm7 in Escherichia coli strain BL21(DE3) Rosetta 2, coexpression of trm732 and trm734, construction of Trm7-Trm734 and Trm7-Trm732 co-expression vectors Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme complexes Trm7-Trm734 and Trm7-Trm734-SAM, hanging drop vapor diffusion technique, mixing of 3 mg/ml protein solution with reservoir solution containing 0.1 M HEPES-NaOH, pH 7.5, 2 M (NH4)2SO4, 2% PEG 400, 2 mM phenol, and 3% ethylene-glycol, and equilibration against 0.2m ml reservoir solution, soaking of the crystals in in the mother liquor containing 1 mM SAM for complex 2, 20°C, 5 days, X-ray diffraction structure determination and analysis at 2.32-3.20 A resolution Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm Trm7, Trm732, and Trm734 are localized to cytoplasm Saccharomyces cerevisiae 5737
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Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNALeu Saccharomyces cerevisiae enzyme complex Trm7-Trm734 S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNALeu
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 ?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNALeu Saccharomyces cerevisiae ATCC 204508 enzyme complex Trm7-Trm734 S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNALeu
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 ?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNAPhe Saccharomyces cerevisiae enzyme complex Trm7-Trm734 S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNAPhe
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 ?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNAPhe Saccharomyces cerevisiae ATCC 204508 enzyme complex Trm7-Trm734 S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNAPhe
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 ?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNATrp Saccharomyces cerevisiae enzyme complex Trm7-Trm734 S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNATrp
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 ?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNATrp Saccharomyces cerevisiae ATCC 204508 enzyme complex Trm7-Trm734 S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNATrp
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 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P38238
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Saccharomyces cerevisiae ATCC 204508 P38238
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzymatic activity of Trm7-Trm734 is measured by incorporation of 14C-methyl groups from [methyl-14C]-SAM into tRNA transcripts. Although these mutant tRNAPhe transcripts are methylated by Trm7-Trm734, the substitution of G34 by C or U (G34C or G34U) strongly enhances the methyl-group acceptance activity. Trm7-Trm734 preferentially methylates pyrimidine nucleoside at position 34 (pyrimidine34) rather than purine nucleoside. Of the 43 tRNA molecular species in Saccharomyces cerevisiae, only tRNAPhe, tRNATrp and tRNALeu possess the combination of Cm32, m1G37 and/or pyrimidine34 in the normal anticodon-loop, which is required for the effective methylation by Trm7-Trm734 Saccharomyces cerevisiae ?
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additional information the enzymatic activity of Trm7-Trm734 is measured by incorporation of 14C-methyl groups from [methyl-14C]-SAM into tRNA transcripts. Although these mutant tRNAPhe transcripts are methylated by Trm7-Trm734, the substitution of G34 by C or U (G34C or G34U) strongly enhances the methyl-group acceptance activity. Trm7-Trm734 preferentially methylates pyrimidine nucleoside at position 34 (pyrimidine34) rather than purine nucleoside. Of the 43 tRNA molecular species in Saccharomyces cerevisiae, only tRNAPhe, tRNATrp and tRNALeu possess the combination of Cm32, m1G37 and/or pyrimidine34 in the normal anticodon-loop, which is required for the effective methylation by Trm7-Trm734 Saccharomyces cerevisiae ATCC 204508 ?
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S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNALeu enzyme complex Trm7-Trm734 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNALeu
-
 ?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNALeu enzyme complex Trm7-Trm734 Saccharomyces cerevisiae ATCC 204508 S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNALeu
-
 ?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNAPhe enzyme complex Trm7-Trm734 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNAPhe
-
 ?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNAPhe enzyme complex Trm7-Trm734 Saccharomyces cerevisiae ATCC 204508 S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNAPhe
-
 ?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNATrp enzyme complex Trm7-Trm734 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNATrp
-
 ?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNATrp enzyme complex Trm7-Trm734 Saccharomyces cerevisiae ATCC 204508 S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNATrp
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 ?

Subunits

Subunits Comment Organism
heterodimer Trm7 forms a heterodimer with Trm734 Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
trm7
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 Saccharomyces cerevisiae
Trm7p
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 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine binding structure with Trm7-Trm734, overview Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution sequence and structure-function comaprisons of yeast Trm7 and Trm7 enzymes from other species. Trm7 has the class I-type Rossmann fold, frequently found in SAM-dependent RNA methyltransferases, and probably employs a 2'-O-methylation mechanism similar to that of Escherichia coli RlmE, given that their overall structures are similar and that catalytic residues and SAM-binding mode are highly conserved Saccharomyces cerevisiae
metabolism the degree of some of the modifications in tRNAs from Saccharomyces cerevisiae may be regulated by the balance between substrate tRNAs and modification enzymes. Because one of key modifications, Cm32, is conferred by Trm7-Trm732, it is clear that the activity of Trm7-Trm734 is regulated by the quantitative balance between Trm732 and Trm734 Saccharomyces cerevisiae
additional information the structure of tRNA methyltransferase complex of Trm7 and Trm734 (regulator of Ty1 transposition protein 10, RTT10, UniProt Q08924) reveals another binding interface for tRNA recognition, crystal structure analysis and substrate tRNA recognition by Trm7-Trm734, and active site structure, overview. Hydrogen bonds and salt bridges between Trm7 and Trm734 are determined Saccharomyces cerevisiae