FEBS Letters | |
Three phosphorylation sites in elongation factor 2 | |
Natapov, Pavel G.4  Motuz, Lyudmila P.4  Averbuch, Lidiya J.4  Hardesty, Boyd2  Kramer, Gisela2  Szyszka, Ryszard1  Ovchinnikov, Lev P.4  Wettenhall, Richard E.H.3  | |
[1] Department of Molecular Biology, University of Maria Curie Sklodowska, 20-033 Lublin, Poland;Clayton Foundation Biochemical Institute, and Department of Chemistry, The University of Texas at Austin, Austin, TX 78712, USA;The Russell Grimvade School of Biochemistry, The University of Melbourne, Parkville, Victoria 3052, Australia;Institute of Protein Research, Academy of Sciences of the USSR, 142292 Pushchino, Moscow Region, USSR | |
关键词: Elongation factor 2; Phosphorylation; EF-2 kinase; Tryptic phosphopeptide; EF-1; EF-2; elongation factor 1; elongation factor 2; DEAE-cellulose; diethylaminoethyl cellulose; TPCK; L-1-tosyl-amino-2-phenylethyl chloromethyl ketone; SDS; sodium dodecyl sulfate; Hepes; 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid; DTT; dithiothreitol; TCA; trichloroacetic acid; RP-HPLC; reversed-phase high performance liquid chromatography; TFA; trifluoroacetic acid; EDTA; ethylenediaminetetraacetic acid; PTH; 2-phenyl-5-thio-hydantoin; MES; 2-(N-morpholino) ethanesulfonic acid; ATZ; 2-anilino-5-thiazolinone; | |
DOI : 10.1016/0014-5793(90)81473-2 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Elongation factor 2 (EF-2) of rabbit reticulocytes was phosphorylated in vitro by incubation with partially purified EF-2 kinase and (γ32P)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.
【 授权许可】
Unknown
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