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 language | English |
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Pages (from-to) | 91-95 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 466 |
Issue number | 1 |
DOIs | |
Publication status | Published - 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