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cAMP‐dependent activation of protein synthesis correlates with dephosphorylation of elongation factor 2
Author(s) -
Sitikov A.S.,
Simonenko P.N.,
Shestakova E.A.,
Ryazanov A.G.,
Ovchinnikov L.P.
Publication year - 1988
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(88)80025-5
Subject(s) - dephosphorylation , elongation , elongation factor , chemistry , phosphorylation , microbiology and biotechnology , biochemistry , biology , phosphatase , materials science , gene , ribosome , rna , metallurgy , ultimate tensile strength
The addition of 5 mM cAMP to a cell‐free translation system from rabbit reticulocytes increases the rate of protein synthesis 3–5‐fold. Lower concentrations of cAMP (0.005, 0.05 and 0.5 mM) have no effect on translation in this system. cAMP at all the concentrations tested stimulates the phosphorylation of the same pattern of polypeptides, while 5 mM cAMP additionally stimulates dephosphorylation of the 95 kDa polypeptide identified as elongation factor 2 (EF‐2). Testing of the preparations of EF‐2 with a different content of the phosphorylated form in poly(U)‐directed poly(Phe) synthesis reveals that the EF‐2 activity correlates with the fraction of non‐phosphorylated EF‐2. Thus cAMP‐dependent activation of protein synthesis seems to be due to dephosphorylation of EF‐2.