Elongation factor methyltransferase 3 - a novel eukaryotic lysine methyltransferase

Lelin Zhang, Joshua J. Hamey, Gene Hart-Smith, Melissa A. Erce, Marc R. Wilkins*

*Corresponding author for this work

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Here we describe the discovery of Saccharomyces cerevisiae protein YJR129Cp as a new eukaryotic seven-beta-strand lysine methyltransferase. An immunoblotting screen of 21 putative methyltransferases showed a loss in the methylation of elongation factor 2 (EF2) on knockout of YJR129C. Mass spectrometric analysis of EF2 tryptic peptides localised this loss of methylation to lysine 509, in peptide LVEGLKR. In vitro methylation, using recombinant methyltransferases and purified EF2, validated YJR129Cp as responsible for methylation of lysine 509 and Efm2p as responsible for methylation at lysine 613. Contextualised on previously described protein structures, both sites of methylation were found at the interaction interface between EF2 and the 40S ribosomal subunit. In line with the recently discovered Efm1 and Efm2 we propose that YJR129C be named elongation factor methyltransferase 3 (Efm3). The human homolog of Efm3 is likely to be the putative methyltransferase FAM86A, according to sequence homology and multiple lines of literature evidence.

Original languageEnglish
Pages (from-to)229-234
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume451
Issue number2
DOIs
Publication statusPublished - 22 Aug 2014
Externally publishedYes

Keywords

  • methylation
  • lysine methyltransferase
  • elongation factor 2
  • Saccharomyces cerevisiae

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