eIF5A binds to translational machinery components and affects translation in yeast

Biochem Biophys Res Commun. 2006 Oct 6;348(4):1358-66. doi: 10.1016/j.bbrc.2006.07.195. Epub 2006 Aug 7.

Abstract

The putative translation factor eIF5A is essential for cell viability and is highly conserved from archebacteria to mammals. Although this protein was originally identified as a translation initiation factor, subsequent experiments did not support a role for eIF5A in general translation. In this work, we demonstrate that eIF-5A interacts with structural components of the 80S ribosome, as well as with the translation elongation factor 2 (eEF2). Moreover, eIF5A is further shown to cofractionate with monosomes in a translation-dependent manner. Finally, eIF5A mutants show altered polysome profiles and are sensitive to translation inhibitors. Our results re-establish a function for eIF5A in translation and suggest a role for this factor in translation elongation instead of translation initiation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Eukaryotic Translation Initiation Factor 5A
  • Lysine / analogs & derivatives
  • Lysine / metabolism
  • Mutation
  • Peptide Chain Elongation, Translational
  • Peptide Initiation Factors / chemistry
  • Peptide Initiation Factors / genetics
  • Peptide Initiation Factors / metabolism*
  • Protein Biosynthesis*
  • Protein Synthesis Inhibitors / pharmacology
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism*
  • Ribosomes / metabolism
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*

Substances

  • Peptide Initiation Factors
  • Protein Synthesis Inhibitors
  • RNA-Binding Proteins
  • Saccharomyces cerevisiae Proteins
  • hypusine
  • Lysine