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Identification of two serine residues important for p53 DNA binding and protein stability
Gang Wei1, Guoxia Liu, Xuan Liu
1Department of Biochemistry, University of California, Riverside, CA 92521, USA.
FEBS Letters
|May 20, 2003
Abstract:
The p53 core DNA binding domain has been implied in Mdm2-mediated protein degradation. Here we show that the substitution of the serine residues 116 and 127 with alanine residues (S116/127A) has no effect on p53 DNA binding and protein stability. However, the substitution of the serine residues with the aspartic acid (S116/127D) abolished p53 DNA binding and led to protein stabilization. Importantly, we have shown that S116/127D exhibits a structural mutant conformation that results in a loss of p53-dependent transcription and Mdm2-mediated protein degradation.