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Originally published In Press as doi:10.1074/jbc.M105144200 on October 24, 2001

J. Biol. Chem., Vol. 277, Issue 1, 630-638, January 4, 2002
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A Plant Phytotoxin, Solanapyrone A, Is an Inhibitor of DNA Polymerase beta  and lambda *

Yoshiyuki MizushinaDagger §, Shinji Kamisuki||, Nobuyuki Kasai||, Noriko Shimazaki||, Masaharu Takemura**, Hitomi AsaharaDagger Dagger , Stuart LinnDagger Dagger , Shonen Yoshida**, Akio Matsukage§§, Osamu Koiwai||, Fumio Sugawara||, Hiromi YoshidaDagger §, and Kengo Sakaguchi||

From the Dagger  Laboratory of Food & Nutritional Sciences, Department of Nutritional Science, § High Technology Research Center, Kobe-Gakuin University, Nishi-ku, Kobe, Hyogo 651-2180, Japan, the || Department of Applied Biological Science, Science University of Tokyo, Noda, Chiba 278-8510, Japan, the ** Laboratory of Cancer Cell Biology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Aichi 466-8550, Japan, the Dagger Dagger  Division of Biochemistry and Molecular Biology, Barker Hall, University of California, Berkeley, California 94720-3202, and the §§ Department of Chemical and Biological Sciences, Japan Women's University, Bunkyo-ku, Tokyo 112-8681, Japan

Solanapyrone A, a phytotoxin and enzyme inhibitor isolated from a fungus (SUT 01B1-2) selectively inhibits the activities of mammalian DNA polymerase beta  and lambda  (pol beta  and lambda ) in vitro. The IC50 values of the compound were 30 µM for pol beta  and 37 µM for pol lambda . Because pol beta  and lambda  are in a family and their three-dimensional structures are thought to be highly similar to each other, we used pol beta  to analyze the biochemical relationship with solanapyrone A. On pol beta , solanapyrone A antagonistically competed with both the DNA template and the nucleotide substrate. BIAcore analysis demonstrated that solanapyrone A bound selectively to the N-terminal 8-kDa domain of pol beta . This domain is known to bind single-stranded DNA, provide 5'-phosphate recognition of gapped DNA, and cleave the sugar-phosphate bond 3' to an intact apurinic/apyrimidinic (AP) site (i.e. AP lyase activity) including 5'-deoxyribose phosphate lyase activity. Solanapyrone A inhibited the single-stranded DNA-binding activity but did not influence the activities of the 5'-phosphate recognition in gapped DNA structures and the AP lyase. Based on these results, the inhibitory mechanism of solanapyrone A is discussed.

* This work was supported in part by the Fujisawa Foundation (to Y. M.), the Uehara Memorial Foundation (to F. S.), and Grants-in-Aid 12780442 (to Y. M.) and 12660103 (to F. S.) from the Ministry of Education, Science, Sports, and Culture of Japan.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.

Recipient of the Research Award for Young Scientists from the Inoue Foundation for Science. To whom correspondence should be addressed. Tel.: 81-78-974-1551, Ext. 3232; Fax: 81-78-974-5689; E-mail: mizushin@nutr.kobegakuin.ac.jp.

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


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