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Originally published In Press as doi:10.1074/jbc.M105382200 on November 8, 2001

J. Biol. Chem., Vol. 277, Issue 2, 1255-1260, January 11, 2002
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MutS Preferentially Recognizes Cisplatin- over Oxaliplatin-modified DNA*

Zoran Z. ZdraveskiDagger §, Jill A. MelloDagger §, Christine K. FarinelliDagger §, John M. EssigmannDagger §||, and Martin G. Marinus**Dagger Dagger

From the Dagger  Department of Chemistry and § Division of Bioengineering and Environmental Health, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 and the ** Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01605

Loss of mismatch repair leads to tumor resistance by desensitizing cells to specific DNA-damaging agents, including the anticancer drug cisplatin. Cisplatin analogs with a diamminocyclohexane (DACH) carrier ligand, such as oxaliplatin and Pt(DACH)Cl2, do not elicit resistance in mismatch repair-deficient cells and therefore present promising therapeutic agents. This study compared the interactions of the purified Escherichia coli mismatch repair protein MutS with DNA modified to contain cisplatin and DACH adducts. MutS recognized the cisplatin-modified DNA with 2-fold higher affinity in comparison to the DACH-modified DNA. ADP stimulated the binding of MutS to cisplatin-modified DNA, whereas it had no effect on the MutS interaction with DNA modified by DACH or EN adducts. In parallel cytotoxicity experiments, methylation-deficient E. coli dam mutants were 2-fold more sensitive to cisplatin than DACH compounds. A panel of recombination-deficient mutants showed striking sensitivity to both compounds, indicating that both types of adducts are strong replication blocks. The differential affinity of MutS for DNA modified with the different platinum analogs could provide the molecular basis for the distinctive cellular responses to cisplatin and oxaliplatin.

* This work was supported by National Institutes of Health Grant CA86061 (to J. M. E.) and a Howard Hughes Medical Institute Research Resources Program for Medical Schools award to the University of Massachusetts Medical School.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Each laboratory contributed equally to this work.

|| To whom correspondence may be addressed. Tel.: 617-253-6224; Fax: 617-253-5445; E-mail: jessig@mit.edu.

Dagger Dagger To whom correspondence may be addressed. Tel.: 508-856-3330; Fax: 508-856-3036; E-mail: martin.marinus@umassmed.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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