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Originally published In Press as doi:10.1074/jbc.M011177200 on February 2, 2001

J. Biol. Chem., Vol. 276, Issue 18, 15434-15440, May 4, 2001
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Damaged DNA-binding Protein DDB Stimulates the Excision of Cyclobutane Pyrimidine Dimers in Vitro in Concert with XPA and Replication Protein A*

Mitsuo WakasugiDagger §, Mayuko ShimizuDagger , Hiroshi Morioka, Stuart Linn||, Osamu NikaidoDagger , and Tsukasa MatsunagaDagger **

From the Dagger  Faculty of Pharmaceutical Sciences, Kanazawa University, Kanazawa 920-0934, Japan,  Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan, and || Division of Biochemistry and Molecular Biology, University of California, Berkeley, California 94720-3202

Human cells contain a protein that binds to UV-irradiated DNA with high affinity. This protein, damaged DNA-binding protein (DDB), is a heterodimer of two polypeptides, p127 and p48. Recent in vivo studies suggested that DDB is involved in global genome repair of cyclobutane pyrimidine dimers (CPDs), but the mechanism remains unclear. Here, we show that in vitro DDB directly stimulates the excision of CPDs but not (6-4)photoproducts. The excision activity of cell-free extracts from Chinese hamster AA8 cell line that lacks DDB activity was increased 3-4-fold by recombinant DDB heterodimer but not p127 subunit alone. Moreover, the addition of XPA or XPA + replication protein A (RPA), which themselves enhanced excision, also enhanced the excision in the presence of DDB. DDB was found to elevate the binding of XPA to damaged DNA and to make a complex with damaged DNA and XPA or XPA + RPA as judged by both electrophoretic mobility shift assays and DNase I protection assays. These results suggest that DDB assists in the recognition of CPDs by core NER factors, possibly through the efficient recruitment of XPA or XPA·RPA, and thus stimulates the excision reaction of CPDs.

* This work was supported by grants from Ministry of Education, Science, 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.

§ Supported by Research Fellowships of the Japan Society for the Promotion of Science for Young Scientists.

** To whom correspondence should be addressed: Faculty of Pharmaceutical Sciences, Kanazawa University, 13-1 Takara-machi, Kanazawa 920-0934, Japan. Tel.: 81-76-234-4487; Fax: 81-76-234-4427; E-mail: matsukas@kenroku.kanazawa-u.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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