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.
Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Ohad
O
Iosefson
Abdussalam
A
Azem
D001665:Binding Sites; D004247:DNA / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D008928:Mitochondria / Q000737:chemistry / Q000378:metabolism; D009711:Nucleotides / Q000494:pharmacology; D011485:Protein Binding / Q000187:drug effects; D054730:Protein Interaction Domains and Motifs / Q000187:drug effects; D025941:Protein Interaction Mapping / Q000379:methods; D055503:Protein Multimerization / Q000187:drug effects; D011506:Proteins / Q000302:isolation & purification / Q000378:metabolism; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*
D018840:HSP70 Heat-Shock Proteins; D009711:Nucleotides; D011506:Proteins; D016159:Tumor Suppressor Protein p53; C080352:mortalin; D004247:DNA