Structure of p53 binding to the BAX response element reveals DNA unwinding and compression to accommodate base-pair insertion.

ABSTRACT: The p53 core domain binds to response elements (REs) that contain two continuous half-sites as a cooperative tetramer, but how p53 recognizes discontinuous REs is not well understood. Here we describe the crystal structure of the p53 core domain bound to a naturally occurring RE located at the promoter of the Bcl-2-associated X protein (BAX) gene, which contains a one base-pair insertion between the two half-sites. Surprisingly, p53 forms a tetramer on the BAX-RE that is nearly identical to what has been reported on other REs with a 0-bp spacer. Each p53 dimer of the tetramer binds in register to a half-site and maintains the same protein-DNA interactions as previously observed, and the two dimers retain all the protein-protein contacts without undergoing rotation or translation. To accomm

SUBMITTER: Chen Y 

PROVIDER: S-EPMC3783167 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature