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Study of phosphorylation of translation elongation factor 2 (EF‐2) from wheat germ
Author(s) -
Smailov Salim K.,
Lee Anatoly V.,
Iskakov Bulat K.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80112-8
Subject(s) - phosphorylation , reticulocyte , elongation factor , protein kinase a , microbiology and biotechnology , kinase , protein phosphorylation , calmodulin , elongation , translation (biology) , biology , biochemistry , eukaryotic translation elongation factor 1 alpha 1 , protein biosynthesis , chemistry , enzyme , messenger rna , ribosome , rna , gene , materials science , ultimate tensile strength , metallurgy
Phosphorylation of elongation factor 2 (EF‐2) by specific Ca 2+ /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.