Substrate specificity determinants of the checkpoint protein kinase Chk1

James R.A. Hutchins, Mike Hughes, Paul R. Clarke (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

53 Citations (Scopus)

Abstract

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 Φ-X-β-X-X-(S/T)*, where * indicates the phosphorylated residue, Φ is a hydrophobic residue (M>I>L>V), β 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. ũ 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)91-95
Number of pages5
JournalFEBS Letters
Volume466
Issue number1
DOIs
Publication statusPublished - 21 Jan 2000

Keywords

  • Cdc25
  • Cell cycle checkpoint
  • Chk1
  • Protein kinase specificity

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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