Mutational analysis reveals potential phosphorylation sites in eukaryotic elongation factor 1A that are important for its activity
| Autor: | Terri Goss Kinzy, Maria K. Mateyak, Pragati Sharma, Dongming He |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Alanine
Saccharomyces cerevisiae Proteins biology Chemistry DNA Mutational Analysis Mutant Saccharomyces cerevisiae Biophysics Translation (biology) Cell Biology biology.organism_classification Biochemistry Cell biology Elongation factor Peptide Elongation Factor 1 Structural Biology Protein Biosynthesis Genetics Protein biosynthesis Phosphorylation Guanine nucleotide exchange factor Molecular Biology |
| Zdroj: | FEBS Letters. 595:2208-2220 |
| ISSN: | 1873-3468 0014-5793 |
| DOI: | 10.1002/1873-3468.14164 |
| Popis: | Previous studies have suggested that phosphorylation of translation elongation factor 1A (eEF1A) can alter its function, and large-scale phospho-proteomic analyses in Saccharomyces cerevisiae have identified 14 eEF1A residues phosphorylated under various conditions. Here, a series of eEF1A mutations at these proposed sites were created and the effects on eEF1A activity were analyzed. The eEF1A-S53D and eEF1A-T430D phosphomimetic mutant strains were inviable, while corresponding alanine mutants survived but displayed defects in growth and protein synthesis. The activity of an eEF1A-S289D mutant was significantly reduced in the absence of the guanine nucleotide exchange factor eEF1Bα and could be restored by an exchange-deficient form of the protein, suggesting that eEF1Bα promotes eEF1A activity by a mechanism other than nucleotide exchange. Our data show that several of the phosphorylation sites identified by high-throughput analysis are critical for eEF1A function. |
| Databáze: | OpenAIRE |
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