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

    54 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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