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

Content Provider	Scilit
Author	Jank, Thomas Belyi, Yury Wirth, Christophe Rospert, Sabine Hu, Zehan Dengjel, Jörn Tzivelekidis, Tina Andersen, Gregers Rom Hunte, Carola Schlosser, Andreas Aktories, Klaus
Copyright Year	2017
Description	Journal: Journal of Biological Chemistry 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 $Glu^{45}$ residue among these organisms. We therefore conclude that eEF1A glutaminylation is a yeast-specific posttranslational modification that appears to influence protein translation.
Related Links	http://www.jbc.org/content/292/39/16014.full.pdf https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5625034/pdf http://www.jbc.org/article/S0021925820339910/pdf
Ending Page	16023
Page Count	10
Starting Page	16014
ISSN	00219258
e-ISSN	1083351X
DOI	10.1074/jbc.m117.801035
Journal	Journal of Biological Chemistry
Issue Number	39
Volume Number	292
Language	English
Publisher	Elsevier BV
Publisher Date	2017-09-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Chemistry Biochemistry and Molecular Biology Saccharomyces Cerevisiae Schizosaccharomyces Pombe Eukaryotic Elongation Factor Eef1a Helix A*–loop–helix A′ Region Posttranslational Modification (ptm) Protein Synthesis Translation Elongation Factor
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology