Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A.
J Biol Chem
; 292(39): 16014-16023, 2017 09 29.
Article
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| MEDLINE
| ID: mdl-28801462
ABSTRACT
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.
Palabras clave
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
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Modelos Moleculares
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Procesamiento Proteico-Postraduccional
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Factor 1 de Elongación Peptídica
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Proteínas de Saccharomyces cerevisiae
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Glutamina
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
J Biol Chem
Año:
2017
Tipo del documento:
Article