FEBS Letters | |
Study of phosphorylation of translation elongation factor 2 (EF‐2) from wheat germ | |
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
【 预 览 】
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