Methylation of Elongation Factor 1A: Where, Who, and Why?

Trends Biochem Sci. 2018 Mar;43(3):211-223. doi: 10.1016/j.tibs.2018.01.004. Epub 2018 Feb 1.

Abstract

Eukaryotic elongation factor 1A (eEF1A) is an essential and highly conserved protein involved in diverse cellular processes, including translation, cytoskeleton organisation, nuclear export, and proteasomal degradation. Recently, nine novel and site-specific methyltransferases were discovered that target eEF1A, five in yeast and four in human, making it the eukaryotic protein with the highest number of independent methyltransferases. Some of these methyltransferases show striking evolutionary conservation. Yet, they come from diverse methyltransferase families, indicating they confer competitive advantage through independent origins. As might be expected, the first functional studies of specific methylation sites found them to have distinct effects, notably on eEF1A-related processes of translation and tRNA aminoacylation. Further functional studies of sites will likely reveal other unique roles for this interesting modification.

Keywords: elongation factor 1A; methylation; methyltransferase; translation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Humans
  • Methylation
  • Peptide Elongation Factor 1 / chemistry*
  • Peptide Elongation Factor 1 / metabolism*

Substances

  • EEF1A1 protein, human
  • Peptide Elongation Factor 1