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Conserved properties between functionally distinct MutS homologs in yeast

P Pochart1, D Woltering, N M Hollingsworth

  • 1Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York at Stony Brook, Stony Brook, New York 11794-5215, USA. nancyhol@mcbsgi.bio.sunysb.edu

The Journal of Biological Chemistry
|December 31, 1997
PubMed

Insights

In yeast, five MutS homologs perform distinct DNA repair roles. MSH4 and MSH5 form specific protein pairs for meiotic crossovers, separate from mismatch repair proteins.

Area of Science:

  • Molecular Biology
  • Genetics
  • Yeast Research

Background:

  • The yeast Saccharomyces cerevisiae possesses five nuclear MutS homologs.
  • These homologs are involved in distinct cellular processes: DNA mismatch repair and meiotic crossover formation.

Purpose of the Study:

  • To investigate the hetero-oligomeric interactions of MutS homologs in yeast.
  • To determine the functional specificity of MutS homologs in DNA repair and meiotic recombination.

Main Methods:

  • Coimmunoprecipitation assays to detect protein interactions.
  • Two-hybrid experiments to confirm protein complex formation.
  • Site-directed mutagenesis to assess protein domain function.

Main Results:

  • MSH4 and MSH5 proteins form a stable hetero-oligomeric complex.
  • Mutations in key Msh5p domains disrupt function but not Msh4p interaction.
  • No hetero-oligomers form between mismatch repair proteins (Msh2p, Msh6p) and MSH4/MSH5.

Conclusions:

  • Distinct hetero-oligomer formation provides functional specificity for MutS homologs.
  • MSH4-MSH5 complex is crucial for meiotic crossover facilitation.
  • NTP binding is a downstream event in MSH4-MSH5 complex function.

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