Analysis of the binding of p53 to DNAs containing mismatched and bulged bases

作者：Degtyareva N; Subramanian D; Griffith JD^*

来源：Journal of Biological Chemistry, 2001, 276(12): 8778-8784.

DOI：10.1074/jbc.M006795200

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 primacy DNA damage. Linear 49-base pair duplex DNAs were constructed containing all possible single-base mismatches as well as a S-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.

• 出版日期2001-3-23