Identification and Characterization of Saccharomyces cerevisiae EXO1, a Gene Encoding an Exonuclease that Interacts with MSH2

A two-hybrid screen was used to identify Saccharomyces cerevisiae genes encoding proteins that interact with MSH2. One gene was found to encode a homologue of Schizosaccharomyces pombe EXO1, a double-stranded DNA-specific 5′-3′exonuclease. S. cerevisiae EXO1 interacted with both S. cerevisiae and hu...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1997-07, Vol.94 (14), p.7487-7492
Main Authors: Tishkoff, Daniel X., Boerger, Adrienne L., Bertrand, Pascale, Filosi, Nicole, Gaida, Gretchen M., Kane, Michael F., Kolodner, Richard D.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antibodies
Biological Sciences
DNA
DNA Repair Enzymes
DNA-Binding Proteins - genetics
Exodeoxyribonucleases - genetics
Exonucleases - genetics
Fungal Proteins
Genes
Genes, Fungal
Genetic mutation
Genetics
Genomics
Human genetics
Humans
Molecular Sequence Data
MutS Homolog 2 Protein
Open reading frames
Phenotypes
Plasmids
Polymerase chain reaction
Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae Proteins
Schizosaccharomyces pombe
Schizosaccharomyces pombe Proteins
Sequence Homology, Amino Acid
Yeast
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Summary:A two-hybrid screen was used to identify Saccharomyces cerevisiae genes encoding proteins that interact with MSH2. One gene was found to encode a homologue of Schizosaccharomyces pombe EXO1, a double-stranded DNA-specific 5′-3′exonuclease. S. cerevisiae EXO1 interacted with both S. cerevisiae and human MSH2 in two-hybrid and coimmunoprecipitation experiments. exo1 mutants showed a mutator phenotype, and epistasis analysis was consistent with EXO1 functioning in the MSH2-dependent mismatch repair pathway. exo1 mutations were lethal in combination with rad27 mutations, and overexpression of EXO1 suppressed both the temperature sensitive and mutator phenotypes of rad27 mutants.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.94.14.7487