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Nucleic Acids Research Advance Access first published online on December 4, 2008
This version published online on December 8, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn964
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Genome Integrity, Repair and Replication

Physical and functional interaction between DDB and XPA in nucleotide excision repair

Mitsuo Wakasugi1, Hiromi Kasashima1, Yuko Fukase1, Mayumi Imura1, Rika Imai1, Saki Yamada1, James E. Cleaver2 and Tsukasa Matsunaga1,*

1Laboratory of Human Molecular Genetics, Institute of Medical, Pharmaceutical and Health Sciences, Kanazawa University, Kanazawa 920-1192, Japan and 2Auerback Melanoma Laboratory, Helen Diller Family Comprehensive Cancer Center, University of California San Francisco, San Francisco, CA 94143-0808, USA

*To whom correspondence should be addressed. Tel: +81 76 234 4487; Fax: +81 76 234 4427; Email: matsukas{at}kenroku.kanazawa-u.ac.jp

Received August 30, 2008. Revised November 9, 2008. Accepted November 12, 2008.

Damaged DNA-binding protein (DDB), consisting of DDB1 and DDB2 subunits recognizes a wide spectrum of DNA lesions. DDB is dispensable for in vitro nucleotide excision repair (NER) reaction, but stimulates this reaction especially for cyclobutane pyrimidine dimer (CPD). Here we show that DDB directly interacts with XPA, one of core NER factors, mainly through DDB2 subunit and the amino-acid residues between 185 and 226 in XPA are important for the interaction. Interestingly, the point mutation causing the substitution from Arg-207 to Gly, which was previously identified in a XP-A revertant cell-line XP129, diminished the interaction with DDB in vitro and in vivo. In a defined system containing R207G mutant XPA and other core NER factors, DDB failed to stimulate the excision of CPD, although the mutant XPA was competent for the basal NER reaction. Moreover, in vivo experiments revealed that the mutant XPA is recruited to damaged DNA sites with much less efficiency compared with wild-type XPA and fails to support the enhancement of CPD repair by ectopic expression of DDB2 in SV40-transformed human cells. These results suggest that the physical interaction between DDB and XPA plays an important role in the DDB-mediated NER reaction.


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