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Saccharomyces cerevisiae elongation factor 2 is phosphorylated by an endorenous kinase
Author(s) -
Donovan Maura G.,
Bodley James W.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81307-t
Subject(s) - saccharomyces cerevisiae , elongation factor , protein kinase a , biochemistry , phosphorylation , kinase , yeast , biology , cyclin dependent kinase 2 , mitogen activated protein kinase kinase , microbiology and biotechnology , chemistry , rna , ribosome , gene
Mammalian cells contain a Ca 2+ /calmodulin‐dependent protein kinase that specifically phosphorylates and inactivates elongation factor 2 (EF‐2) in response to hormones and other agents which increase intracellular Ca 2+ concentrations. Therefore, it has been proposed that the rate of translation in mammals is regulated by EF‐2 phosphorylation. In the present study, EF‐2 purified from the yeast Saccharomyces cerevisiae is shown to be a substrate for the mammalian EF‐2 kinase. Furthermore, evidence was obtained using two‐dimensional gel electrophoresis and peptide mapping which suggests that yeast EF‐2 is a substrate for an endogenous kinase which phosphorylates the same site as the mammalian EF‐2 kinase. Based on these findings, we propose that in yeast as in higher eukaryotes, the protein synthesis elongation cycle is regulated by phosphorylation of EF‐2.