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Molecular and Cellular Biology, April 2002, p. 2388-2397, Vol. 22, No. 7
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.7.2388-2397.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

hMutSß Is Required for the Recognition and Uncoupling of Psoralen Interstrand Cross-Links In Vitro

Nianxiang Zhang, Xiaoyan Lu, Xiaoshan Zhang, Carolyn A. Peterson, and Randy J. Legerski*

Department of Molecular Genetics, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030

Received 20 November 2001/ Returned for modification 20 December 2001/ Accepted 3 January 2002

The removal of interstrand cross-links (ICLs) from DNA in higher eucaryotes is not well understood. Here, we show that processing of psoralen ICLs in mammalian cell extracts is dependent upon the mismatch repair complex hMutSß but is not dependent upon the hMutS{alpha} complex or hMlh1. The processing of psoralen ICLs is also dependent upon the nucleotide excision repair proteins Ercc1 and Xpf but not upon other components of the excision stage of this pathway or upon Fanconi anemia proteins. Products formed during the in vitro reaction indicated that the ICL has been removed or uncoupled from the cross-linked substrate in the mammalian cell extracts. Finally, the hMutSß complex is shown to specifically bind to psoralen ICLs, and this binding is stimulated by the addition of PCNA. Thus, a novel pathway for processing ICLs has been identified in mammalian cells which involves components of the mismatch repair and nucleotide excision repair pathways.

* Corresponding author. Mailing address: Department of Molecular Genetics, The University of Texas M. D. Anderson Cancer Center, Houston, TX 77030. Phone: (713) 792-8941. Fax: (713) 794-4295. E-mail: rlegersk{at}mdanderson.org.

Molecular and Cellular Biology, April 2002, p. 2388-2397, Vol. 22, No. 7
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.7.2388-2397.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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