Reconstitution of the mitochondrial Hsp70 (mortalin)-p53 interaction using purified proteins - Identification of additional interacting regions

Previous studies have shown that the mammalian mitochondrial 70 kDa heat-shock protein ( mortalin) can also be detected in the cytosol. Cytosolic mortalin binds p53 and by doing so, prevents translocation of the tumor suppressor into the nucleus. In this study, we developed a novel binding assay, using purified proteins, for tracking the interaction between p53 and mortalin. Our results reveal that: (i) P53 binds to the peptide-binding site of mortalin which enhances the ability of the former to bind DNA. (ii) An additional previously unknown binding site for mortalin exists within the C-terminal domain of p53. Structured summary: MINT-7557591: p53 (uniprotkb: P04637) binds (MI: 0407) to DnaK ( uniprotkb: P0A6Y8) by affinity chromatography technology ( MI: 0004) MINT-7557644: mortalin (uniprotkb: P38646) binds (MI: 0407) to p53 (uniprotkb: P04637) by pull down ( MI: 0096) MINT-7557580, MINT-7557611: p53 ( uniprotkb: P04637) binds ( MI: 0407) to mortalin ( uniprotkb: P38646) by affinity chromatography technology ( MI: 0004) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.