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Basis for the checkpoint signal specificity that regulates Chk1 and Cds1 protein kinases

Academic Article
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Overview

related to degree

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

authors

  • Brondello, J. M.
  • Boddy, Michael
  • Baber-Furnari, Beth Anne
  • Russell, Paul

publication date

  • June 1999

journal

  • Molecular and Cellular Biology  Journal

abstract

  • Six checkpoint Rad proteins (Rad1, Rad3, Rad9, Rad17, Rad26, and Hus1) are needed to regulate checkpoint protein kinases Chk1 and Cds1 in fission yeast. Chk1 is required to prevent mitosis when DNA is damaged by ionizing radiation (IR), whereas either kinase is sufficient to prevent mitosis when DNA replication is inhibited by hydroxyurea (HU). Checkpoint Rad proteins are required for IR-induced phosphorylation of Chk1 and HU-induced activation of Cds1. IR activates Cds1 only during the DNA synthesis (S) phase, whereas HU induces Chk1 phosphorylation only in cds1 mutants. Here, we investigate the basis of the checkpoint signal specificity of Chk1 phosphorylation and Cds1 activation. We show that IR fails to induce Chk1 phosphorylation in HU-arrested cells. Release from the HU arrest following IR causes substantial Chk1 phosphorylation. These and other data indicate that Cds1 prevents Chk1 phosphorylation in HU-arrested cells, which suggests that Cds1 actively suppresses a repair process that leads to Chk1 phosphorylation. Cds1 becomes more highly concentrated in the nucleus only during the S phase of the cell cycle. This finding correlates with S-phase specificity of IR-induced activation of Cds1. However, constitutive nuclear localization of Cds1 does not enhance IR-induced activation of Cds1. This result suggests that Cds1 activation requires DNA structures or protein activities that are present only during S phase. These findings help to explain how Chk1 and Cds1 respond to different checkpoint signals.

subject areas

  • Cell Cycle
  • Cell Nucleus
  • Checkpoint Kinase 2
  • DNA Repair
  • Enzyme Inhibitors
  • GTP-Binding Proteins
  • Hydroxyurea
  • Immunoblotting
  • Phosphorylation
  • Protein Kinases
  • Protein Serine-Threonine Kinases
  • Recombinant Fusion Proteins
  • S Phase
  • Schizosaccharomyces
  • Time Factors
  • ras Proteins
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Identity

PubMed Central ID

  • PMC104386

International Standard Serial Number (ISSN)

  • 0270-7306

PubMed ID

  • 10330167
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Additional Document Info

start page

  • 4262

end page

  • 4269

volume

  • 19

issue

  • 6

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