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Originally published In Press as doi:10.1074/jbc.M111026200 on May 9, 2002

J. Biol. Chem., Vol. 277, Issue 29, 26632-26641, July 19, 2002
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Coupling of DNA Helicase and Endonuclease Activities of Yeast Dna2 Facilitates Okazaki Fragment Processing*

Sung-Ho BaeDagger , Dong Wook Kim, Jiyoung Kim, Jeong-Hoon Kim, Do-Hyung Kim, Hee-Dai Kim§, Ho-Young Kang, and Yeon-Soo Seo

From the National Creative Research Initiative Center for Cell Cycle Control, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, 300 Chunchun-Dong, Changan-Ku, Suwon, Kyunggi-Do, 440-746, Dagger  Department of Pharmacology, Dong-A University College of Medicine, 3-ga, Tongdaesin-Dong, Seo-Gu, Busan, 602-103, and § Department of Biotechnology and Bioinformatics, Chungbuk Provincial University of Science and Technology, 40 Gumgu-ri, Okchon, Chungbuk, 373-807, Korea

Saccharomyces cerevisiae Dna2 possesses both helicase and endonuclease activities. Its endonuclease activity is essential and well suited to remove RNA-DNA primers of Okazaki fragments. In contrast, its helicase activity, although required for optimal growth, is not essential when the rate of cell growth is reduced. These findings suggest that DNA unwinding activity of Dna2 plays an auxiliary role in Okazaki fragment processing. To address this issue, we examined whether the Dna2 helicase activity influenced its intrinsic endonuclease activity using two mutant proteins, Dna2D657A and Dna2K1080E, which contain only helicase or endonuclease activity, respectively. Experiments performed with a mixture of Dna2D657A and Dna2K1080E enzymes revealed that cleavage of a single-stranded DNA by endonuclease activity of Dna2 occurs while the enzyme translocates along the substrate. In addition, DNA unwinding activity efficiently removed the secondary structure formed in the flap structure, which was further aided by replication protein A. Our results suggest that the Dna2 unwinding activity plays a role in facilitating the removal of the flap DNA by its intrinsic endonuclease activity.

* This work was supported by a grant from the Creative Research Initiatives Program of the Korean Ministry of Science and Technology (to Y.-S. 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.

To whom correspondence should be addressed. Tel.: 82-31-299-6440; Fax: 82-31-299-6435; E-mail: ysseo@med.skku.ac.kr.

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