The DNA polymerase domain of pole is required for rapid, efficient, and highly accurate chromosomal DNA replication, telomere length maintenance, and normal cell senescence in Saccharomyces cerevisiae

T Ohya, Y Kawasaki, SI Hiraga, S Kanbara, K Nakajo, N Nakashima, A Suzuki, A Sugino

Research output: Contribution to journalArticle

67 Citations (Scopus)

Abstract

Saccharomyces cerevisiae POL2 encodes the catalytic subunit of DNA polymerase ε. 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 ε 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 δ in a haploid cell. These results suggest that the catalytic activity of DNA polymerase ε participates in the same pathway as DNA polymerase δ, and this is consistent with the observation that DNA polymerases δ and ε colocalize in some punctate foci on yeast chromatids during S phase. Thepol2-16 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.
Original languageEnglish
Pages (from-to)28099-28108
Number of pages11
JournalJournal of Biological Chemistry
Volume277
Issue number31
Early online date15 May 2002
DOIs
Publication statusPublished - 2 Aug 2002

Fingerprint

Telomere Homeostasis
Cell Aging
DNA-Directed DNA Polymerase
DNA Replication
Yeast
Saccharomyces cerevisiae
Poles
Catalytic DNA
DNA
Exonucleases
Temperature
Catalytic Domain
Yeasts
Phosphodiesterase I
Chromatids
Haploidy
Telomere
S Phase
Metabolism
Elongation

Cite this

The DNA polymerase domain of pole is required for rapid, efficient, and highly accurate chromosomal DNA replication, telomere length maintenance, and normal cell senescence in Saccharomyces cerevisiae. / Ohya, T; Kawasaki, Y; Hiraga, SI; Kanbara, S; Nakajo, K; Nakashima, N; Suzuki, A; Sugino, A.

In: Journal of Biological Chemistry, Vol. 277, No. 31, 02.08.2002, p. 28099-28108.

Research output: Contribution to journalArticle

@article{870284a680e54828a272614ecec3bc91,
title = "The DNA polymerase domain of pole is required for rapid, efficient, and highly accurate chromosomal DNA replication, telomere length maintenance, and normal cell senescence in Saccharomyces cerevisiae",
abstract = "Saccharomyces cerevisiae POL2 encodes the catalytic subunit of DNA polymerase ε. 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 ε 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 δ in a haploid cell. These results suggest that the catalytic activity of DNA polymerase ε participates in the same pathway as DNA polymerase δ, and this is consistent with the observation that DNA polymerases δ and ε colocalize in some punctate foci on yeast chromatids during S phase. Thepol2-16 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.",
author = "T Ohya and Y Kawasaki and SI Hiraga and S Kanbara and K Nakajo and N Nakashima and A Suzuki and A Sugino",
note = "Acknowledgments—We thank Drs. L. Hartwell, R. Rothstein, C. Wittenberg, and J. L. Campbell for strains and plasmid DNA.",
year = "2002",
month = "8",
day = "2",
doi = "10.1074/jbc.M111573200",
language = "English",
volume = "277",
pages = "28099--28108",
journal = "The Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC",
number = "31",

}

TY - JOUR

T1 - The DNA polymerase domain of pole is required for rapid, efficient, and highly accurate chromosomal DNA replication, telomere length maintenance, and normal cell senescence in Saccharomyces cerevisiae

AU - Ohya, T

AU - Kawasaki, Y

AU - Hiraga, SI

AU - Kanbara, S

AU - Nakajo, K

AU - Nakashima, N

AU - Suzuki, A

AU - Sugino, A

N1 - Acknowledgments—We thank Drs. L. Hartwell, R. Rothstein, C. Wittenberg, and J. L. Campbell for strains and plasmid DNA.

PY - 2002/8/2

Y1 - 2002/8/2

N2 - Saccharomyces cerevisiae POL2 encodes the catalytic subunit of DNA polymerase ε. 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 ε 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 δ in a haploid cell. These results suggest that the catalytic activity of DNA polymerase ε participates in the same pathway as DNA polymerase δ, and this is consistent with the observation that DNA polymerases δ and ε colocalize in some punctate foci on yeast chromatids during S phase. Thepol2-16 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.

AB - Saccharomyces cerevisiae POL2 encodes the catalytic subunit of DNA polymerase ε. 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 ε 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 δ in a haploid cell. These results suggest that the catalytic activity of DNA polymerase ε participates in the same pathway as DNA polymerase δ, and this is consistent with the observation that DNA polymerases δ and ε colocalize in some punctate foci on yeast chromatids during S phase. Thepol2-16 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.

U2 - 10.1074/jbc.M111573200

DO - 10.1074/jbc.M111573200

M3 - Article

VL - 277

SP - 28099

EP - 28108

JO - The Journal of Biological Chemistry

JF - The Journal of Biological Chemistry

SN - 0021-9258

IS - 31

ER -