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Serine-345 is required for Rad3-dependent phosphorylation and function of checkpoint kinase Chk1 in fission yeast

Academic Article
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Overview

related to degree

  • Baber-Furnari, Beth Anne, Ph.D. in Biology, Scripps Research 1994 - 1999

authors

  • Lopez-Girona, A.
  • Tanaka, K.
  • Chen, X. B.
  • Baber-Furnari, Beth Anne
  • McGowan, C. H.
  • Russell, Paul

publication date

  • September 2001

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Genome integrity is monitored by a checkpoint that delays mitosis in response to DNA damage. This checkpoint is enforced by Chk1, a protein kinase that inhibits the mitotic inducer Cdc25. In fission yeast, Chk1 is regulated by a group of proteins that includes Rad3, a protein kinase related to human ATM and ATR. These kinases phosphorylate serine or threonine followed by glutamine (SQ/TQ). Fission yeast and human Chk1 proteins share two conserved SQ motifs at serine-345 and serine-367. Serine-345 of human Chk1 is phosphorylated in response to DNA damage. Here we report that Rad3 and ATM phosphorylate serine-345 of fission yeast Chk1. Mutation of serine-345 (chk1-S345A) abrogates Rad3-dependent phosphorylation of Chk1 in vivo. The chk1-S345A cells are sensitive to DNA damage and are checkpoint defective. In contrast, mutations of serine-367 and other SQ/TQ sites do not substantially impair the checkpoint or cause damage sensitivity. These findings attest to the importance of serine-345 phosphorylation for Chk1 function and strengthen evidence that transduction of the DNA damage checkpoint signal requires direct phosphorylation of Chk1 by Rad3.

subject areas

  • Adenosine Triphosphatases
  • Amino Acid Sequence
  • Amino Acid Substitution
  • Animals
  • Cell Cycle
  • Conserved Sequence
  • DNA Helicases
  • Humans
  • Mice
  • Molecular Sequence Data
  • Mutagenesis
  • Mutagenesis, Site-Directed
  • Phosphorylation
  • Point Mutation
  • Protein Kinases
  • Ranidae
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Serine
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Identity

PubMed Central ID

  • PMC58722

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.191557598

PubMed ID

  • 11553781
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Additional Document Info

start page

  • 11289

end page

  • 11294

volume

  • 98

issue

  • 20

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