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Information on EC 2.1.1.205 - tRNA (cytidine32/guanosine34-2'-O)-methyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38238

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IUBMB Comments
The enzyme from Saccharomyces cerevisiae catalyses the formation of 2'-O-methylnucleotides at positions 32 and 34 of the yeast tRNAPhe, tRNATrp and, possibly, tRNALeu.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P38238
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
S-adenosyl-L-methionine
+
cytidine32/guanosine34 in tRNA
=
S-adenosyl-L-homocysteine
+
2'-O-methylcytidine32/2'-O-methylguanosine34 in tRNA
+
cytidine32/guanosine34 in tRNA
=
+
2'-O-methylcytidine32/2'-O-methylguanosine34 in tRNA
Synonyms
trm7p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (cytidine32/guanosine34-2'-O)-methyltransferase
The enzyme from Saccharomyces cerevisiae catalyses the formation of 2'-O-methylnucleotides at positions 32 and 34 of the yeast tRNAPhe, tRNATrp and, possibly, tRNALeu.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O-methylguanosine34 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNALeu
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNALeu
show the reaction diagram
enzyme complex Trm7-Trm734
-
-
?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNAPhe
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNAPhe
show the reaction diagram
enzyme complex Trm7-Trm734
-
-
?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNATrp
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNATrp
show the reaction diagram
enzyme complex Trm7-Trm734
-
-
?
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
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O-methylguanosine34 in tRNA
show the reaction diagram
the enzyme catalyses the formation of 2'-O-methylnucleotides at positions 32 and 34 of the yeast tRNAPhe, tRNATrp and, possibly, tRNALeu
-
-
?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNALeu
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNALeu
show the reaction diagram
enzyme complex Trm7-Trm734
-
-
?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNAPhe
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNAPhe
show the reaction diagram
enzyme complex Trm7-Trm734
-
-
?
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNATrp
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O methylguanosine34 in tRNATrp
show the reaction diagram
enzyme complex Trm7-Trm734
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
binding structure with Trm7-Trm734, overview
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
malfunction
a trm7DELTA strain, which is viable but grows slowly, translation is impaired. Protein synthesis is reduced to 30% in the deleted strain, compared with an isogenic wild-type strain. The formation of 2'-O-methylcytidine32 and guanosine34 is abolished in the trm7DELTA strain
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
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
Trm7 forms a heterodimer with Trm734
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D49A
abolishes almost completely the formation of 2'-O-methylcytidine32, no activity is detected for guanine34
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant strain D49A
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pintard, L.; Lecointe, F.; Bujnicki, J.M.; Bonnerot, C.; Grosjean, H.; Lapeyre, B.
Trm7p catalyses the formation of two 2'-O-methylriboses in yeast tRNA anticodon loop
EMBO J.
21
1811-1820
2002
Saccharomyces cerevisiae (P38238), Saccharomyces cerevisiae
Manually annotated by BRENDA team
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
Nucleic Acids Res.
47
10942-10955
2019
Saccharomyces cerevisiae (P38238), Saccharomyces cerevisiae ATCC 204508 (P38238)
Manually annotated by BRENDA team