Coordinated Conformational Processing of the Tumor Suppressor Protein p53 by the Hsp70 and Hsp90 Chaperone Machineries (Molecular Cell)

p53 activity is tightly regulated by opposing effects of Hsp70 and Hsp90 on its conformation. Hsp70-Hsp40 unfolds p53, whereas Hsp90 and Hop fold it into native conformation upon ATP hydrolysis. These findings establish a concept of how DNA binding of transcription factors can be tightly regulated by Hsp70 and Hsp90.