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Title: Xeroderma pigmentosum complementation group C protein (XPC) serves as a general sensor of damaged DNA.

Authors: Shell, Steven M; Hawkins, Edward K; Tsai, Miaw-Sheue; Hlaing, Aye Su; Rizzo, Carmelo J; Chazin, Walter J

Published In DNA Repair (Amst), (2013 Nov)

Abstract: The Xeroderma pigmentosum complementation group C protein (XPC) serves as the primary initiating factor in the global genome nucleotide excision repair pathway (GG-NER). Recent reports suggest XPC also stimulates repair of oxidative lesions by base excision repair. However, whether XPC distinguishes among various types of DNA lesions remains unclear. Although the DNA binding properties of XPC have been studied by several groups, there is a lack of consensus over whether XPC discriminates between DNA damaged by lesions associated with NER activity versus those that are not. In this study we report a high-throughput fluorescence anisotropy assay used to measure the DNA binding affinity of XPC for a panel of DNA substrates containing a range of chemical lesions in a common sequence. Our results demonstrate that while XPC displays a preference for binding damaged DNA, the identity of the lesion has little effect on the binding affinity of XPC. Moreover, XPC was equally capable of binding to DNA substrates containing lesions not repaired by GG-NER. Our results suggest XPC may act as a general sensor of damaged DNA that is capable of recognizing DNA containing lesions not repaired by NER.

PubMed ID: 24051049 Exiting the NIEHS site

MeSH Terms: Animals; Base Sequence; Binding Sites/genetics; DNA Damage*; DNA Repair Enzymes/genetics; DNA Repair Enzymes/metabolism*; DNA Repair/physiology; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism*; DNA/chemistry*; DNA/metabolism; Fluorescence Polarization; High-Throughput Screening Assays; Humans; Sf9 Cells; Spodoptera/metabolism

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