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Three phosphorylation sites in elongation factor 2
Author(s) -
Ovchinnikov Lev P.,
Motuz Lyudmila P.,
Natapov Pavel G.,
Averbuch Lidiya J.,
Wettenhall Richard E.H.,
Szyszka Ryszard,
Kramer Gisela,
Hardesty Boyd
Publication year - 1990
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(90)81473-2
Subject(s) - threonine , phosphorylation , chemistry , peptide , in vitro , elongation factor , phosphate , hydrolysis , biochemistry , kinase , elongation , protein kinase a , chromatography , serine , rna , ribosome , materials science , ultimate tensile strength , metallurgy , gene
Elongation factor 2 (EF‐2) of rabbit reticulocytes was phosphorylated in vitro by incubation with partially purified EF‐2 kinase and (γ 32 P)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.