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Papers In Press, published online ahead of print May 15, 2002
J. Biol. Chem, 10.1074/jbc.M111573200
Submitted on December 5, 2001
Revised on May 14, 2002
Accepted on May 15, 2002
Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871
Corresponding Author: asugino{at}biken.osaka-u.ac.jp
Saccharomyces cerevisiae POL2 encodes the catalytic subunit of DNA polymerase epsilon. This study investigates the cellular functions performed by the polymerase domain of Pol2p and its role in DNA metabolism. The pol2-16 mutation has a deletion in the catalytic domain of DNA polymerase epsilon that eliminates its polymerase and exonuclease activities. It is a viable mutant, which displays temperature sensitivity for growth and a defect in elongation step of chromosomal DNA replication even at permissive temperature. This mutation is synthetic lethal in combination with temperature-sensitive mutants or the 3’ to 5’ exonuclease deficient mutant of DNA polymerase delta in a haploid cell. These results suggest that the catalytic activity of DNA polymerase epsilon participates in the same pathway as DNA polymerase delta, and this is consistent with the observation that DNA polymerases delta and epsilon colocalize in some punctate foci on yeast chromatids during S phase. The pol2-16 mutant senesces more rapidly than wild type strain and also has shorter telomeres. These results indicate that the DNA polymerase domain of Polepsilon is required for rapid, efficient, and highly accurate chromosomal DNA replication in yeast.
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