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PMID:16027442
Citation |
Urbonavicius, J, Skouloubris, S, Myllykallio, H and Grosjean, H (2005) Identification of a novel gene encoding a flavin-dependent tRNA:m5U methyltransferase in bacteria--evolutionary implications. Nucleic Acids Res. 33:3955-64 |
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Abstract |
Formation of 5-methyluridine (ribothymidine) at position 54 of the T-psi loop of tRNA is catalyzed by site-specific tRNA methyltransferases (tRNA:m(5)U-54 MTase). In all Eukarya and many Gram-negative Bacteria, the methyl donor for this reaction is S-adenosyl-l-methionine (S-AdoMet), while in several Gram-positive Bacteria, the source of carbon is N(5), N(10)-methylenetetrahydrofolate (CH(2)H(4)folate). We have identified the gene for Bacillus subtilis tRNA:m(5)U-54 MTase. The encoded recombinant protein contains tightly bound flavin and is active in Escherichia coli mutant lacking m(5)U-54 in tRNAs and in vitro using T7 tRNA transcript as substrate. This gene is currently annotated gid in Genome Data Banks and it is here renamed trmFO. TrmFO (Gid) orthologs have also been identified in many other bacterial genomes and comparison of their amino acid sequences reveals that they are phylogenetically distinct from either ThyA or ThyX class of thymidylate synthases, which catalyze folate-dependent formation of deoxyribothymine monophosphate, the universal DNA precursor. |
Links |
PubMed PMC1178002 Online version:10.1093/nar/gki703 |
Keywords |
Bacillus subtilis/enzymology; Bacteria/enzymology; Bacterial Proteins/chemistry; Bacterial Proteins/classification; Escherichia coli/metabolism; Evolution, Molecular; Flavins/metabolism; Genes, Bacterial; Genomics; Phylogeny; RNA, Transfer/metabolism; Uridine/analogs & derivatives; Uridine/metabolism; tRNA Methyltransferases/classification; tRNA Methyltransferases/genetics; tRNA Methyltransferases/metabolism |
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Significance
Annotations
Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
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GO:0008168: methyltransferase activity |
ECO:0000315: |
F |
Figure 2A and B indicate that the wild type cell extract was able to catalyze formation of m^5U-54 in vitro, however the mutant strain lacking the functional Gid protein was unable to catalyze such a methylation reaction. Thus this indicates that the gid gene product is involved in product of m^5Y-54 in tRNA. |
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See also
References
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