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M111026200v1
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Papers In Press, published online ahead of print May 9, 2002
J. Biol. Chem, 10.1074/jbc.M111026200
Submitted on November 16, 2001
Revised on April 1, 2002
Accepted on May 9, 2002

Coupling of DNA helicase and endonuclease activities of yeast Dna2 facilitates Okazaki fragment processing

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

Molecular and Cellular Biology, Sungkyunkwan University School of Medicine, Suwon, Kyunggi 440-746

Corresponding Author: ysseo{at}med.skku.ac.kr

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. In order 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 play a role to facilitate the removal of the flap DNA by its intrinsic endonuclease activity.


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