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Substrate specificity determinants of the checkpoint protein kinase Chk1
Author(s) -
Hutchins James R.A.,
Hughes Mike,
Clarke Paul R.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01763-9
Subject(s) - chek1 , substrate (aquarium) , substrate specificity , kinase , chemistry , protein kinase a , microbiology and biotechnology , biochemistry , biology , enzyme , cell cycle checkpoint , cell cycle , ecology , gene
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.