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Corresponding author: Eric Alani, Department of Molecular Biology and Genetics, Cornell University, 459 Biotechnology Bldg., Ithaca, NY 14853-2703., eea3{at}cornell.edu (E-mail)
Communicating editor: F. WINSTON
mutation is synthetically lethal with pol3-01, a mutation in the Pol
proofreading exonuclease. Six conditional alleles of msh2 were identified as those that conferred viability in pol3-01 strains at 26° but not at 35°. DNA sequencing revealed that mutations in several of the msh2ts alleles are located in regions with previously unidentified functions. The conditional inviability of two mutants, msh2-L560S pol3-01 and msh2-L910P pol3-01, was suppressed by overexpression of EXO1 and MSH6, respectively. Partial suppression was also observed for the temperature-sensitive mutator phenotype exhibited by msh2-L560S and msh2-L910P strains in the lys2-Bgl reversion assay. High-copy plasmids bearing mutations in the conserved EXO1 nuclease domain were unable to suppress msh2-L560S pol3-01 conditional lethality. These results, in combination with a genetic analysis of msh6 pol3-01 and msh3 pol3-01 strains, suggest that the activity of the Msh2p-Msh6p heterodimer is important for viability in the presence of the pol3-01 mutation and that Exo1p plays a catalytic role in Msh2p-mediated mismatch repair.
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