Characterization of an Hsp90-Independent Interaction between Co-Chaperone p23 and Transcription Factor p53.

ABSTRACT: Cancer-suppressing transcription factor p53 is regulated by a wide variety of cellular factors, including many chaperones. The DNA-binding domain (DBD) of p53 is known to interact with the chaperone Hsp90, but the role of other members of the chaperone network, including co-chaperones such as p23, is unknown. Using a combination of nuclear magnetic resonance (NMR) titration, isothermal titration calorimetry, fluorescence anisotropy, and native agarose gel electrophoresis, we have identified a direct interaction between the p53 DBD and Hsp90 co-chaperone p23 that occurs in the absence of Hsp90. The affinity is relatively weak and largely determined by electrostatic interactions between the acidic C-terminal disordered tail of p23 and the two DNA-binding regions of the p53 DBD. We show by NM

SUBMITTER: Wu H 

PROVIDER: S-EPMC5811392 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature