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  • Title: Three phosphorylation sites in elongation factor 2.
    Author: Ovchinnikov LP, Motuz LP, Natapov PG, Averbuch LJ, Wettenhall RE, Szyszka R, Kramer G, Hardesty B.
    Journal: FEBS Lett; 1990 Nov 26; 275(1-2):209-12. PubMed ID: 2261989.
    Abstract:
    Elongation factor 2 (EF-2) of rabbit reticulocytes was phosphorylated in vitro by incubation with partially purified EF-2 kinase and [gamma-32P]ATP. After exhaustive tryptic hydrolysis 4 phosphopeptides were revealed by two-dimensional peptide mapping. The phosphopeptides were isolated by high performance liquid chromatography and sequenced. A comparison of the primary structure of the phosphopeptides with that of EF-2 showed that all 4 phosphopeptides originated from one region of EF-2 located near the N-terminus that contains 3 threonine residues: Thr-53, Thr-56, Thr-58. A direct estimation of localization of radioactive phosphate in the phosphopeptides demonstrated that all the enumerated threonine residues in EF-2 can be phosphorylated in vitro.
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