Saccharomyces cerevisiae elongation factor 2 is phosphorylated by an endorenous kinase

FEBS Letters

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