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Formation of m $$\texttt{2}$$ G6 in Methanocaldococcus jannaschii tRNA catalyzed by the novel methyltransferase Trm14

Journal Article · · Nucleic Acids Research
DOI:https://doi.org/10.1093/nar/gkr475· OSTI ID:1904587
 [1];  [2];  [2];  [3];  [4];  [3];  [2];  [4]
  1. University of California, Santa Barbara, CA (United States); Univ. of California, Santa Barbara, CA (United States)
  2. University of Cincinnati, OH (United States)
  3. University of Maryland Baltimore County (UMBC), Baltimore, MD (United States)
  4. 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 Maryland, College Park, MD (United States); University of California, Santa Barbara, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC); National Institutes of Health (NIH); National Science Foundation (NSF)
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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Cited By (9)

Base methylations in the double-stranded RNA by a fused methyltransferase bearing unwinding activity journal December 2011
Crystal structures of the tRNA:m 2 G6 methyltransferase Trm14/TrmN from two domains of life journal February 2012
Life without tRNAIle-lysidine synthetase: translation of the isoleucine codon AUA in Bacillus subtilis lacking the canonical tRNA2Ile journal November 2013
Structural basis for S -adenosylmethionine binding and methyltransferase activity by mitochondrial transcription factor B1 journal June 2013
Activation mode of the eukaryotic m2G10tRNA methyltransferase Trm11 by its partner protein Trm112 journal December 2016
Structural and functional analyses of the archaeal tRNA m2G/m22G10 methyltransferase aTrm11 provide mechanistic insights into site specificity of a tRNA methyltransferase that contains common RNA-binding modules journal June 2016
Methylated nucleosides in tRNA and tRNA methyltransferases journal May 2014
Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus journal January 2017
Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA journal October 2018

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