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PMID: 7523888 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Xeroderma pigmentosum group E binding factor recognizes a broad spectrum of DNA damage.

Mutation research ·Vol. 310 ·No. 1 ·1994-10-01 ·Pages 89-102

Payne A, Chu G

Abstract

Xeroderma pigmentosum complementation group E binding factor (XPE-BF) is a damaged DNA binding protein that is deficient in a subset of patients from complementation group E of xeroderma pigmentosum. The protein recognizes various forms of DNA damage including some cyclobutane pyrimidine dimers, 6-4 photoproducts, cis-diamminedichloroplatinum(II) adducts, and single-stranded DNA. We now show that it also recognizes damage induced by nitrogen mustard; N-methyl-N'-nitro-N-nitrosoguanidine, and depurination, but has no detectable affinity for DNA adducts generated by trans-diamminedichloroplatinum(II), 4-nitroquinoline-N-oxide, 8-methoxypsoralen, or enzymatically methylated cytosine and adenine. The failure to recognize 4-nitroquinoline-N-oxide and 8-methoxypsoralen adducts is consistent with previous reports that XPE cells carry out wild-type levels of repair synthesis after DNA damage by those drugs. These results demonstrate that XPE-BF is a versatile damage recognition protein, but suggest that other proteins must contribute to the recognition of DNA lesions for the human excision repair pathway.

MeSH Terms
4-Nitroquinoline-1-oxide/metabolism,toxicity Cisplatin/metabolism,toxicity DNA/drug effects,metabolism,radiation effects DNA Damage DNA Repair DNA-Binding Proteins/metabolism Genetic Complementation Test HeLa Cells Humans Mechlorethamine/metabolism,toxicity Methoxsalen/metabolism,toxicity Methylnitronitrosoguanidine/metabolism,toxicity Mutagens/metabolism,toxicity Ultraviolet Rays Xeroderma Pigmentosum/genetics,metabolism
Chemicals
DDB1 protein, human DNA-Binding Proteins Mutagens Methylnitronitrosoguanidine transplatin Mechlorethamine 4-Nitroquinoline-1-oxide DNA Cisplatin Methoxsalen
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Payne A
Department of Medicine, Stanford University School of Medicine, CA 94305.
Chu G
Article Info
Journal
Mutation research
Abbr.
Mutat Res
ISSN
0027-5107
Published
1994-10-01
Pages
89-102
Language
English
Region
Netherlands
NLM ID
0400763
Subset
IM
Grants
NCI NIH HHS · CA-44949 · United States
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