Substrate specificity determinants of the checkpoint protein kinase Chk1

James R.A. Hutchins; Mike Hughes; Paul R. Clarke

doi:10.1016/S0014-5793(99)01763-9

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 journal › Article › peer-review

56 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 language	English
Pages (from-to)	91-95
Number of pages	5
Journal	FEBS Letters
Volume	466
Issue number	1
DOIs	https://doi.org/10.1016/S0014-5793(99)01763-9
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

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10.1016/S0014-5793(99)01763-9

Cite this

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AU - Hughes, Mike

AU - Clarke, Paul R.

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AB - 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.

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Substrate specificity determinants of the checkpoint protein kinase Chk1

Abstract

Keywords

ASJC Scopus subject areas

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