Example：10.1021/acsami.1c06204 or Chem. Rev., 2007, 107, 2411-2502
Mutational analysis reveals potential phosphorylation sites in eukaryotic elongation factor 1A that are important for its activity FEBS Letters (IF4.124), Pub Date : 2021-07-22, DOI: 10.1002/1873-3468.14164 Maria K. Mateyak, Dongming He, Pragati Sharma, Terri Goss Kinzy
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.