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

Iosefson, Ohad; Azem, Abdussalam

doi:10.1016/j.febslet.2010.02.019

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Volume 584, Issue 6 , Pages 1080-1084, 19 March 2010

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

Edited by Varda Rotter

Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel

Received 18 November 2009; received in revised form 3 February 2010; accepted 4 February 2010. published online 11 February 2010.

Abstract

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)

Abbreviations: mtHsp70, 70-kDa mitochondrial heat-shock protein, PAGE, polyacrylamide gel electrophoresis, ssDNA, salmon sperm DNA, FL-p53, full-length p53, NLS, nuclear localization signal