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

Jank, Thomas; Belyi, Yury; Wirth, Christophe; Rospert, Sabine; Hu, Zehan; Dengjel, Jörn; Tzivelekidis, Tina; Andersen, Gregers Rom; Hunte, Carola; Schlosser, Andreas; Aktories, Klaus

doi:10.1074/jbc.M117.801035

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Journal article

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

Jank, Thomas Institute for Experimental and Clinical Pharmacology and Toxicology, Faculty of Medicine, University of Freiburg, Germany,
Belyi, Yury Gamaleya Research Centre, Moscow, Russia, - Bioclinicum, Moscow, Russia,
Wirth, Christophe Institute for Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Germany,
Rospert, Sabine Institute for Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Germany, - BIOSS Centre for Biological Signalling Studies, University of Freiburg, Germany,
Hu, Zehan Department of Dermatology, Faculty of Medicine, University of Freiburg, Germany, - Freiburg Institute for Advanced Studies (FRIAS), University of Freiburg, Germany, - Department of Biology, University of Fribourg, Switzerland,
Dengjel, Jörn Department of Dermatology, Faculty of Medicine, University of Freiburg, Germany, - Freiburg Institute for Advanced Studies (FRIAS), University of Freiburg, Germany, - Department of Biology, University of Fribourg, Switzerland,
Tzivelekidis, Tina Institute for Experimental and Clinical Pharmacology and Toxicology, Faculty of Medicine, University of Freiburg, Germany,
Andersen, Gregers Rom Department of Molecular Biology and Genetics, Center for Structural Biology, Aarhus University, Denmark
Hunte, Carola Department of Molecular Biology and Genetics, Center for Structural Biology, Aarhus University, Denmark - BIOSS Centre for Biological Signalling Studies, University of Freiburg, Germany,
Schlosser, Andreas Rudolf Virchow Center for Experimental Biomedicine, University of Würzburg, Germany
Aktories, Klaus Institute for Experimental and Clinical Pharmacology and Toxicology, Faculty of Medicine, University of Freiburg, Germany, - BIOSS Centre for Biological Signalling Studies, University of Freiburg, Germany, - Freiburg Institute for Advanced Studies (FRIAS), University of Freiburg, Germany,

29.09.2017

Published in:

Journal of Biological Chemistry. - 2017, vol. 292, no. 39, p. 16014–16023

English 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 α 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 Glu45 residue among these organisms. We therefore conclude that eEF1A glutaminylation is a yeast-specific posttranslational modification that appears to influence protein translation.

Faculty

Faculté des sciences et de médecine

Department

Département de Biologie

Language