Substrate specificity determinants of the checkpoint protein kinase Chk1

被引：56

作者：

Hutchins, JRA ^{[1
]}

Hughes, M ^{[1
]}

Clarke, PR ^{[1
]}

机构：

[1] Univ Dundee, Ninewells Hosp & Med Sch, Biomed Res Ctr, Dundee DD1 9SY, Scotland

来源：

FEBS LETTERS | 2000年 / 466卷 / 01期

基金：

英国医学研究理事会; 英国生物技术与生命科学研究理事会;

关键词：

Cdc25; Chk1; cell cycle checkpoint; protein kinase specificity;

D O I：

10.1016/S0014-5793(99)01763-9

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：

The Chk1 protein kinase plays a critical role in a DNA damage checkpoint pathway conserved between fission yeast and animals. We have developed a quantitative assay for Chk1 activity, using a peptide derived from a region of Xenopus Cdc25C containing Ser-287, a known target of Chk1, Variants of this peptide were used to determine the residues involved in substrate recognition by Chk1, revealing the phosphorylation motif Phi-X-beta-X-X-(S/T)*, where * indicates the phosphorylated residue, Phi is a hydrophobic residue (M > I > L > V), beta is a basic residue (R > K) and X is any amino acid. This motif suggests that Chk1 is a member of a group of stress-response protein kinases which phosphorylate target proteins with related specificities. (C) 2000 Federation of European Biochemical Societies.

引用

页码：91 / 95

页数：5

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