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Abstract Background DNA polymerase ε (Pol ε) is essential for S-phase replication, DNA damage repair and checkpoint control in yeast. A <it>pol2-Y831A </it>mutation leading to a tyrosine to alanine change in the Pol ε active site does not cause growth defects and confers a mutator phenotype that is normally subtle but strong in a mismatch repair-deficient strain. Here we investigate the mechanism responsible for the mutator effect. Results Purified four-subunit Y831A Pol ε turns over more deoxynucleoside triphosphates to deoxynucleoside monophosphates than does wild-type Pol ε, suggesting altered coordination between the polymerase and exonuclease active sites. The <it>pol2-Y831A </it>mutation suppresses the mutator effect of the <it>pol2-4 </it>mutation in the exonuclease active site that abolishes proofreading by Pol ε, as measured in haploid strain with the <it>pol2-Y831A,4 </it>double mutation. Analysis of mutation rates in diploid strains reveals that the <it>pol2-Y831A </it>allele is recessive to <it>pol2-4</it>. In addition, the mutation rates of strains with the <it>pol2-4 </it>mutation in combination with active site mutator mutations in Pol δ and Pol α suggest that Pol ε may proofread certain errors made by Pol α and Pol δ during replication <it>in vivo</it>. Conclusions Our data suggest that Y831A replacement in Pol ε reduces replication fidelity and its participation in chromosomal replication, but without eliminating an additional function that is essential for viability. This suggests that other polymerases can substitute for certain functions of polymerase ε.</p

bmc biology

Evidence for interplay among yeast replicative DNA polymerases alpha, delta and epsilon from studies of exonuclease and polymerase active site mutations.