Study of phosphorylation of translation elongation factor 2 (EF‐2) from wheat germ

FEBS Letters

Lee, Anatoly V.¹  Smailov, Salim K.¹  Iskakov, Bulat K.¹ 

[1] Institute of Molecular Biology and Biochemistry, Kazakh Academy of Sciences, Michurin st. 86, Alma-Ata, 480012, Kazakhstan

关键词: Elongation factor 2;    Protein phosphorylation;    Regulation of translation;    Wheat germ;    Triticum aestivum;   

DOI  :  10.1016/0014-5793(93)80112-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphorylation of elongation factor 2 (EF-2) by specific Ca²⁺/calmodulin-dependent kinase is considered as a possible mechanism of regulation of protein biosynthesis in animal cells at the level of polypeptide chain elongation. In this report we show that wheat germ EF-2 can be intensively phosphorylated by the rabbit reticulocyte EF-2 kinase. Phosphorylation results in inhibition of the activity of plant EF-2 in poly(U)-dependent cell-free translation system. Thus, the activity of EF-2 in plant cells can be potentially regulated by phosphorylation. However, we could not detect endogenous EF-2 kinase activity in wheat germ either in vitro or in vivo. Furthermore, EF-2 kinase activity is not displayed in different organs of wheat and other higher plants.

【 授权许可】

Unknown