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Mol Cell Biol, June 1998, p. 3182-3190, Vol. 18, No. 6
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
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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
Otrin,1
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.
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