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Damage tolerance protein Mus81 associates with the FHA1 domain of checkpoint kinase Cds1

M N Boddy1, A Lopez-Girona, P Shanahan

  • 1Departments of Molecular Biology and Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

Molecular and Cellular Biology
|November 14, 2000
PubMed

Insights

The fission yeast kinase Cds1 interacts with Mus81, an endonuclease. Mus81 is crucial for DNA damage tolerance and cell survival, particularly during replication stress.

Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • Cds1 (cell division cycle 1) is a serine/threonine kinase regulating the S-M checkpoint in Schizosaccharomyces pombe.
  • Cds1 is vital for survival under replicational stress, but its precise mechanisms remain unclear.

Purpose of the Study:

  • To elucidate the functional mechanisms of Cds1 in DNA damage tolerance.
  • To identify Cds1 interacting partners involved in replication fork stability.

Main Methods:

  • Protein interaction studies using the forkhead-associated-1 (FHA1) domain of Cds1.
  • Phenotypic analysis of mus81 inactivation mutants.
  • Genetic epistasis studies.

Main Results:

  • Cds1's FHA1 domain directly interacts with Mus81, an endonuclease.
  • Mus81 is essential for survival during deoxynucleotide triphosphate starvation, UV radiation, and DNA polymerase impairment.
  • Mus81 is critical in the absence of the Bloom's syndrome Rqh1 helicase and for meiosis.
  • Mus81 inactivation leads to a checkpoint-dependent delay in mitosis.

Conclusions:

  • Mus81 functions with recombination enzymes to ensure proper replication of damaged DNA.
  • Mus81 likely recruits Cds1 to aberrant DNA structures, where Cds1 modulates damage tolerance pathways.

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