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• W2783756933 abstract "The 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 NMR titration, isothermal titration calorimetry, fluorescence anisotropy and native agarose gel electrophoresis, we have identified a direct interaction between the p53 DBD and the 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 p53 DBD. We show by NMR and native agarose gel electrophoresis that a p53-specific double-stranded DNA sequence competes successfully with p23 for binding to the p53 DBD. The Hsp90-independence of the interaction between p23 and p53 DBD, together with the p23-DNA comp..." @default.
• W2783756933 created "2018-01-26" @default.
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• W2783756933 date "2018-01-24" @default.
• W2783756933 modified "2023-10-03" @default.
• W2783756933 title "Characterization of an Hsp90-Independent Interaction between Co-Chaperone p23 and Transcription Factor p53" @default.
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• W2783756933 doi "https://doi.org/10.1021/acs.biochem.7b01076" @default.
• W2783756933 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5811392" @default.
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• W2783756933 hasPublicationYear "2018" @default.
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