FEBS Letters
Volume 584, Issue 2 , Pages 278-286, 21 January 2010

Stereochemical mechanisms of tRNA methyltransferases

Edited by Michael Ibba

  • Ya-Ming Hou

      Affiliations

    • Department of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10th St., Philadelphia, PA 19107, USA
    • Corresponding Author InformationCorresponding author. Fax: +1 215 503 5393.
    • ,
  • John J. Perona

      Affiliations

    • Department of Chemistry and Biochemistry, University of California at Santa Barbara, Santa Barbara, CA 93106-9510, USA

Received 13 November 2009; received in revised form 18 November 2009; accepted 19 November 2009. published online 25 November 2009.

Abstract 

Methylation of tRNA on the four canonical bases adds structural complexity to the molecule, and improves decoding specificity and efficiency. While many tRNA methylases are known, detailed insight into the catalytic mechanism is only available in a few cases. Of interest among all tRNA methylases is the structural basis for nucleotide selection, by which the specificity is limited to a single site, or broadened to multiple sites. General themes in catalysis include the basis for rate acceleration at highly diverse nucleophilic centers for methyl transfer, using S-adenosylmethionine as a cofactor. Studies of tRNA methylases have also yielded insights into molecular evolution, particularly in the case of enzymes that recognize distinct structures to perform identical reactions at the same target nucleotide.

Keywords: S-adenosylmethionine, SAM-dependent methyl transfer, Rossmann-fold, Methylase, TrmA, Trm5

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PII: S0014-5793(09)00992-2

doi:10.1016/j.febslet.2009.11.075

FEBS Letters
Volume 584, Issue 2 , Pages 278-286, 21 January 2010

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