FEBS Letters | |
Saccharomyces cerevisiae elongation factor 2 is phosphorylated by an endorenous kinase | |
Donovan, Maura G.1  Bodley, James W.1  | |
[1] Department of Biochemistry, University of Minnesota Medical School, 435 Delaware St., S.E. Minneapolis, MN 55455, USA | |
关键词: Elongation factor 2; Protein phosphorylation; Protein synthesis; Protein kinase; Saccharomyces cerevisiae; | |
DOI : 10.1016/0014-5793(91)81307-T | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Mammalian cells contain a Ca2+/calmodulin-dependent protein kinase that specifically phosphorylates and inactivates elongation factor 2 (EF-2) in response to hormones and other agents which increase intracellular Ca2+ 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.
【 授权许可】
Unknown
【 预 览 】
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RO201912020295483ZK.pdf | 495KB | download |