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Originally published In Press as doi:10.1074/jbc.M000960200 on April 20, 2000

J. Biol. Chem., Vol. 275, Issue 28, 21422-21428, July 14, 2000
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Human Damage-specific DNA-binding Protein p48
CHARACTERIZATION OF XPE MUTATIONS AND REGULATION FOLLOWING UV IRRADIATION*

Anne F. NicholsDagger , Toshiki ItohDagger , Jay A. GrahamDagger , Wei LiuDagger , Masaru Yamaizumi§, and Stuart LinnDagger

From the Dagger  Division of Biochemistry and Molecular Biology, University of California, Berkeley, California 94720-3202 and the § Department of Cell Genetics, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kumamoto 862-0976, Japan

Damage-specific DNA binding (DDB) activity purifies from HeLa cells as a heterodimer (p127 and p48) and is absent from cells of a subset (Ddb-) of xeroderma pigmentosum Group E (XPE) patients. Each subunit was overexpressed in insect cells and purified. Both must be present for the damaged DNA band shift characteristic of the HeLa heterodimer. However, overexpressed p48 peptides containing the mutations found in three Ddb- XPE strains are inactive, and wild type p48 restores DDB activity to extracts from a fourth XPE Ddb- strain, GM01389, in which compound heterozygous mutations in DDB2 (p48) lead to a L350P change from one allele and a Asn-349 deletion from the other. Although these results indicate that these mutations are each responsible for the loss of DDB activity, they do not affect nuclear localization of p48. In normal fibroblasts, a 4-fold increase in p48 mRNA amount was observed 38 h after UV irradiation, preceding a similar elevation in p48 protein and DDB activity at 48 h, implying that p48 limits DDB activity in vivo. Because DNA repair is virtually complete before 48 h, a role for DDB other than DNA repair is suggested.

* This work was supported by National Institutes of Health Grant P30ES08196, by DOE Contract FG03-92ER61458, and by grants (09670887 and 11770468) 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.

To whom correspondence should be addressed: Division of Biochemistry and Molecular Biology, 401 Barker Hall, University of California, Berkeley, 94720-3202. Tel.: 510-642-7583; Fax: 510-643-9290; E-mail: slinn@socrates.berkeley.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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