Formation of m $$\texttt{2}$$ G6 in Methanocaldococcus jannaschii tRNA catalyzed by the novel methyltransferase Trm14
- University of California, Santa Barbara, CA (United States); Univ. of California, Santa Barbara, CA (United States)
- University of Cincinnati, OH (United States)
- University of Maryland Baltimore County (UMBC), Baltimore, MD (United States)
- University of California, Santa Barbara, CA (United States)
The modified nucleosides N2 -methylguanosine and N$$^2_2$$-dimethylguanosine in transfer RNA occur at five positions in the D and anticodon arms, and at positions G6 and G7 in the acceptor stem. Trm1 and Trm11 enzymes are known to be responsible for several of the D/anticodon arm modifications, but methylases catalyzing post-transcriptional m2 G synthesis in the acceptor stem are uncharacterized. Here, we report that the MJ0438 gene from Methanocaldococcus jannaschii encodes a novel S-adenosylmethionine-dependent methyltransferase, now identified as Trm14, which generates m2 G at position 6 in tRNACys. The 381 amino acid Trm14 protein possesses a canonical RNA recognition THUMP domain at the amino terminus, followed by a γ-class Rossmann fold amino-methyltransferase catalytic domain featuring the signature NPPY active site motif. Trm14 is associated with cluster of orthologous groups (COG) 0116, and most closely resembles the m2 G10 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. In the archaeal branch, the protein is found exclusively in thermophiles. More distantly related Trm14 homologs were also identified in eukaryotes known to possess the m2 G6 tRNA modification.
- Research Organization:
- University of California, Santa Barbara, CA (United States); University of Maryland, College Park, MD (United States)
- Sponsoring Organization:
- National Institutes of Health (NIH); National Science Foundation (NSF); USDOE Office of Science (SC)
- Grant/Contract Number:
- FG02-93ER20106
- OSTI ID:
- 1904587
- Journal Information:
- Nucleic Acids Research, Journal Name: Nucleic Acids Research Journal Issue: 17 Vol. 39; ISSN 0305-1048
- Publisher:
- Oxford University PressCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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