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Ca 2+ /calmodulin‐dependent phosphorylation of elongation factor 2
Author(s) -
Ryazanov Alexey G.
Publication year - 1987
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(87)80081-9
Subject(s) - trifluoperazine , calmodulin , phosphorylation , eukaryotic translation elongation factor 1 alpha 1 , elongation factor , incubation , elongation , ribosome , biochemistry , chemistry , protein phosphorylation , protein biosynthesis , biophysics , biology , protein kinase a , enzyme , rna , gene , materials science , ultimate tensile strength , metallurgy
Incubation of a ribosome‐free extract of rabbit reticulocytes or rat liver with [γ‐ 32 P]ATP and Ca 2+ results in incorporation of 32 P predominantly into a single polypeptide of M r ∼ 100 000. This polypeptide is identified as elongation factor 2 (EF‐2). Phosphorylation of EF‐2 is strictly Ca 2+ ‐dependent and can be inhibited by the calmodulin antagonist trifluoperazine. It is suggested that the Ca 2+ /calmodulin‐dependent phosphorylation of EF‐2 is involved in regulation of protein biosynthesis.