Identification of two serine residues important for p53 DNA binding and protein stability

FEBS Letters

Liu, Xuan¹  Wei, Gang¹  Liu, Guoxia¹ 

[1] Department of Biochemistry, University of California, Riverside, CA 92521, USA

关键词: p53;    DNA binding;    Stability;    Ser-116;    Ser-127;   

DOI  :  10.1016/S0014-5793(03)00369-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown