3 PHOSPHORYLATION SITES IN ELONGATION FACTOR-II

被引：49

作者：

OVCHINNIKOV, LP

MOTUZ, LP

NATAPOV, PG

AVERBUCH, LJ

WETTENHALL, REH

SZYSZKA, R

KRAMER, G

HARDESTY, B

机构：

[1] UNIV TEXAS,CLAYTON FDN BIOCHEM INST,AUSTIN,TX 78712

[2] UNIV TEXAS,DEPT CHEM,AUSTIN,TX 78712

[3] ACAD SCI USSR,INST PROT RES,PUSHCHINO 142292,USSR

[4] UNIV MELBOURNE,RUSSELL GRIMWADE SCH BIOCHEM,PARKVILLE,VIC 3052,AUSTRALIA

[5] MARIE CURIE SKLODOWSKA UNIV,DEPT MOLEC BIOL,PL-20033 LUBLIN,POLAND

来源：

FEBS LETTERS | 1990年 / 275卷 / 1-2期

关键词：

EF-2; kinase; Elongation factor 2; Phosphorylation; Tryptic phosphopeptide;

D O I：

10.1016/0014-5793(90)81473-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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. © 1990.

引用

页码：209 / 212

页数：4

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