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  • Title: Study of phosphorylation of translation elongation factor 2 (EF-2) from wheat germ.
    Author: Smailov SK, Lee AV, Iskakov BK.
    Journal: FEBS Lett; 1993 Apr 26; 321(2-3):219-23. PubMed ID: 8386679.
    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.
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