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J. Biol. Chem., Vol. 281, Issue 30, 21422-21432, July 28, 2006

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GINS Is a DNA Polymerase Accessory Factor during Chromosomal DNA Replication in Budding Yeast^*

Takashi Seki, Masaki Akita, Yoichiro Kamimura^¶, Sachiko Muramatsu^¶, Hiroyuki Araki^¶, and Akio Sugino¹

From the Laboratories for Biomolecular Networks, Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamada-oka, Suita, Osaka 565-0871, the Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Aichi 464-8602, and the ^¶Division of Microbial Genetics, National Institute of Genetics, Mishima, Shizuoka 411-8540, Japan

GINS is a protein complex found in eukaryotic cells that is composed of Sld5p, Psf1p, Psf2p, and Psf3p. GINS polypeptides are highly conserved in eukaryotes, and the GINS complex is required for chromosomal DNA replication in yeasts and Xenopus egg. This study reports purification and biochemical characterization of GINS from Saccharomyces cerevisiae. The results presented here demonstrate that GINS forms a 1:1 complex with DNA polymerase (Pol ) holoenzyme and greatly stimulates its catalytic activity in vitro. In the presence of GINS, Pol is more processive and dissociates more readily from replicated DNA, while under identical conditions, proliferating cell nuclear antigen slightly stimulates Pol in vitro. These results strongly suggest that GINS is a Pol accessory protein during chromosomal DNA replication in budding yeast. Based on these results, we propose a model for molecular dynamics at eukaryotic chromosomal replication fork.

Received for publication, April 11, 2006 , and in revised form, May 17, 2006.

^* This work was supported by grants from the Ministry of Education, Science, Sports, Culture, and Technology of Japan (to H. A. and A. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement"in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental figures.

¹ To whom correspondence should be addressed: Laboratories for Biomolecular Networks, Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamada-oka, Suita, Osaka 565-0871, Japan. Tel.: 81-6-6879-4661; Fax: 81-6-6879-4663; E-mail: asugino{at}fbs.osaka-u.ac.jp.

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