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Originally published In Press as doi:10.1074/jbc.M111573200 on May 15, 2002

J. Biol. Chem., Vol. 277, Issue 31, 28099-28108, August 2, 2002
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The DNA Polymerase Domain of polepsilon Is Required for Rapid, Efficient, and Highly Accurate Chromosomal DNA Replication, Telomere Length Maintenance, and Normal Cell Senescence in Saccharomyces cerevisiae*

Tomoko OhyaDagger , Yasuo KawasakiDagger , Shin-Ichiro HiragaDagger , Sakie Kanbara, Kou Nakajo, Naomi Nakashima§, Akiko Suzuki, and Akio Sugino

From the Department of Biochemistry and Molecular Biology, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamada-oka, Suita, Osaka 565-0871, Japan

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 temperatures. 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 Pol2p is required for rapid, efficient, and highly accurate chromosomal DNA replication in yeast.

* This work was supported in part by grant-in-aid for Scientific Research on Priority Area (A), grant-in-aid for Scientific Research (A) from the Ministry of Education, Science, Sports, and Culture of Japan, and Human Frontier Science Program Research Grants RG039/2000-M (to A. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger These authors contributed equally to this work.

§ Present address: Nippon Medical School, Kawasaki, Kanagawa, Japan.

To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamada-oka, Suita, Osaka 565-0871, Japan. Tel.: 81-6-6879-8331; Fax: 81-6-6877-3584; E-mail: asugino@biken.osaka-u.ac.jp.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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