Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A

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  • Thomas Jank, University of Freiburg, Freiburg, Germany.
  • ,
  • Yury Belyi, Gamaleya Research Centre Moscow, Russian Federation.
  • ,
  • Christophe Wirth, University of Freiburg, Freiburg, Germany.
  • ,
  • Sabine Rospert, University of Freiburg, Freiburg, Germany.
  • ,
  • Zehan Hu, University of Freiburg, Freiburg, Germany.
  • ,
  • Joern Dengjel, Department of Biology, University of Fribourg, CH-1700 Fribourg, Switzerland
  • ,
  • Tina Tzivelekidis, Roche Diagnostics GmbH, Mannheim, Germany.
  • ,
  • Gregers Rom Andersen
  • Carola Hunte, University of Freiburg, Freiburg, Germany.
  • ,
  • Andreas Schlosser, University Hospital of Würzburg, Würzburg, Germany.
  • ,
  • Klaus Aktories, University of Freiburg, Germany; klaus.aktories@pharmakol.uni-freiburg.de.

Ribosomal translation factors are fundamental for protein synthesis and highly conserved in all kingdoms of life. The essential eukaryotic elongation factor 1A (eEF1A), delivers aminoacyl tRNAs to the A-site of the translating 80S ribosome. Several studies have revealed that eEF1A is posttranslationally modified. Using MS analysis, site-directed mutagenesis, and X-ray structural data analysis of Saccharomyces cerevisiae eEF1A, we identified a posttranslational modification in which the alpha amino group of mono-L-glutamine is covalently linked to the side chain of glutamate 45 in eEF1A. The MS analysis suggested that all eEF1A molecules are modified by this glutaminylation and that this posttranslational modification occurs at all stages of yeast growth. The mutational studies revealed that this glutaminylation is not essential for the normal functions of eEF1A in S. cerevisiae However, eEF1A glutaminylation slightly reduced growth under antibiotic-induced translational stress conditions. Moreover, we identified the same posttranslational modification in eEF1A from Schizosaccharomyces pombe, but not in various other eukaryotic organisms tested despite strict conservation of the Glu-45 residue among these organisms. We therefore conclude that eEF1A glutaminylation is a yeast-specific posttranslational modification, which appears to influence protein translation.

OriginalsprogEngelsk
TidsskriftJournal of Biological Chemistry
Vol/bind292
Sider (fra-til)16014-16023
Antal sider10
ISSN0021-9258
DOI
StatusUdgivet - 29 sep. 2017

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