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Nucleic Acids Research 2005 33(9):2993-3001; doi:10.1093/nar/gki610
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Published online 24 May 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

Human XPC-hHR23B interacts with XPA-RPA in the recognition of triplex-directed psoralen DNA interstrand crosslinks

Brian S. Thoma, Mitsuo Wakasugi1, Jesper Christensen2, Madhava C. Reddy and Karen M. Vasquez*

Department of Carcinogenesis, The University of Texas M. D. Anderson Cancer Center, Science Park—Research Division Smithville, TX 78957, USA 1Faculty of Pharmaceutical Sciences, Kanazawa University Takara-machi, Kanazawa 920-0934, Japan 2Biotech Research and Innovation Centre Fruebjergvej 3, 2100 Copenhagen, Denmark

*To whom correspondence should be addressed. Tel: +512 237 9324; Fax: +512 237 2475; Email: kvasquez{at}sprd1.mdacc.tmc.edu

Received February 4, 2005. Revised May 3, 2005. Accepted May 3, 2005.

DNA interstrand crosslinks (ICLs) represent a severe form of damage that blocks DNA metabolic processes and can lead to cell death or carcinogenesis. The repair of DNA ICLs in mammals is not well characterized. We have reported previously that a key protein complex of nucleotide excision repair (NER), XPA-RPA, recognizes DNA ICLs. We now report the use of triplex technology to direct a site-specific psoralen ICL to a target DNA substrate to determine whether the human global genome NER damage recognition complex, XPC-hHR23B, recognizes this lesion. Our results demonstrate that XPC-hHR23B recognizes psoralen ICLs, which have a structure fundamentally different from other lesions that XPC-hHR23B is known to bind, with high affinity and specificity. XPC-hHR23B and XPA-RPA protein complexes were also observed to bind psoralen ICLs simultaneously, demonstrating not only that psoralen ICLs are recognized by XPC-hHR23B alone, but also that XPA-RPA may interact cooperatively with XPC-hHR23B on damaged DNA, forming a multimeric complex. Since XPC-hHR23B and XPA-RPA participate in the recognition and verification of DNA damage, these results support the hypothesis that interplay between components of the global genome repair sub-pathway of NER is critical for the recognition of psoralen DNA ICLs in the mammalian genome.


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