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Originally published In Press as doi:10.1074/jbc.M006795200 on December 20, 2000

J. Biol. Chem., Vol. 276, Issue 12, 8778-8784, March 23, 2001
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Analysis of the Binding of p53 to DNAs Containing Mismatched and Bulged Bases*

Natalya Degtyareva, Deepa Subramanian, and Jack D. GriffithDagger

From the Lineberger Comprehensive Cancer Center and the Department of Microbiology and Immunology, University of North Carolina, Chapel Hill, North Carolina 27599-7295

The tumor suppressor protein p53 modulates cellular response to DNA damage by a variety of mechanisms that may include direct recognition of some forms of primary DNA damage. Linear 49-base pair duplex DNAs were constructed containing all possible single-base mismatches as well as a 3-cytosine bulge. Filter binding and gel retardation assays revealed that the affinity of p53 for a number of these lesions was equal to or greater than that of the human mismatch repair complex, hMSH2-hMSH6, under the same binding conditions. However, other mismatches including G/T, which is bound strongly by hMSH2-hMSH6, were poorly recognized by p53. The general order of affinity of p53 was greatest for a 3-cytosine bulge followed by A/G and C/C mismatches, then C/T and G/T mismatches, and finally all the other mismatches.

* This work was supported in part by National Institutes of Health Grants CA70343 and GM31819.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.

Dagger To whom correspondence should be addressed. Tel.: 919-966-2151; Fax: 919-966-3015; E-mail: jdg@med.unc.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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