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Mol Cell Biol, June 1998, p. 3182-3190, Vol. 18, No. 6
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Relationship of the Xeroderma Pigmentosum Group E DNA Repair Defect to the Chromatin and DNA Binding Proteins UV-DDB and Replication Protein A

Vesna Rapic' Otrin,1 Isao Kuraoka,2 Tiziana Nardo,3 Mary McLenigan,1 A. P. M. Eker,4 Miria Stefanini,3 Arthur S. Levine,1,* and Richard D. Wood2

Section on DNA Replication, Repair, and Mutagenesis, National Institute of Child Health and Human Development, Bethesda, Maryland 20892-27251; Imperial Cancer Research Fund, Clare Hall Laboratories, South Mimms, Hertfordshire EN6 3LD, United Kingdom2; Istituto di Genetica Biochimica ed Evolutionisticia, CNR, 27100 Pavia, Italy3; and Department of Cell Biology and Genetics, Erasmus University, 3000 DR Rotterdam, The Netherlands4

Received 23 October 1997/Returned for modification 15 December 1997/Accepted 19 March 1998

Cells from complementation groups A through G of the heritable sun-sensitive disorder xeroderma pigmentosum (XP) show defects in nucleotide excision repair of damaged DNA. Proteins representing groups A, B, C, D, F, and G are subunits of the core recognition and incision machinery of repair. XP group E (XP-E) is the mildest form of the disorder, and cells generally show about 50% of the normal repair level. We investigated two protein factors previously implicated in the XP-E defect, UV-damaged DNA binding protein (UV-DDB) and replication protein A (RPA). Three newly identified XP-E cell lines (XP23PV, XP25PV, and a line formerly classified as an XP variant) were defective in UV-DDB binding activity but had levels of RPA in the normal range. The XP-E cell extracts did not display a significant nucleotide excision repair defect in vitro, with either UV-irradiated DNA or a uniquely placed cisplatin lesion used as a substrate. Purified UV-DDB protein did not stimulate repair of naked DNA by DDB- XP-E cell extracts, but microinjection of the protein into DDB- XP-E cells could partially correct the repair defect. RPA stimulated repair in normal, XP-E, or complemented extracts from other XP groups, and so the effect of RPA was not specific for XP-E cell extracts. These data strengthen the connection between XP-E and UV-DDB. Coupled with previous results, the findings suggest that UV-DDB has a role in the repair of DNA in chromatin.

* Corresponding author. Mailing address: Section on DNA Replication, Repair, and Mutagenesis, National Institute of Child Health and Human Development, NIH, Building 6, Rm. 1A15, Bethesda, MD 20892-2725. Phone: (301) 496-2133. Fax: (301) 402-0105. E-mail: LevineA{at}EXCHANGE.NIH.GOV.

Mol Cell Biol, June 1998, p. 3182-3190, Vol. 18, No. 6
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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