期刊
DNA REPAIR
卷 12, 期 11, 页码 947-953出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.dnarep.2013.08.013
关键词
XPC; Nucleotide excision repair; Base excision repair; Lesion recognition; DNA binding; High-throughput assay
资金
- NIH [R01 ES016561, P01 CA092584, P30 ES00267, P30 CA068485]
- American Cancer Society [119569-PF-11-271-01-DMC]
- [T32 ES07028]
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. (C) 2013 Elsevier B.V. All rights reserved.
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