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- W2040484170 abstract "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." @default.
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- W2040484170 date "1993-04-26" @default.
- W2040484170 modified "2023-09-25" @default.
- W2040484170 title "Study of phosphorylation of translation elongation factor 2 (EF-2) from wheat germ" @default.
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- W2040484170 doi "https://doi.org/10.1016/0014-5793(93)80112-8" @default.
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