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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...
Previously we have found that elongation factor 2 (EF-2) from mammalian cells can be phosphorylated by a special Ca 2+ /calmodulin-dependent protein kinase (EF-2 kinase). Phosphorylation results in complete inactivation of EF-2 in the poly(U)-directed cell-free translation system. However, the partial function of EF-2 affected by phosphorylation remained unknown. Here we show that phosphorylated...
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