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Interaction of heat-shock protein 70 with p53 translated in vitro: evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation.

1992; Springer Nature; Volume: 11; Issue: 10 Linguagem: Inglês

10.1002/j.1460-2075.1992.tb05434.x

1460-2075

Pierre Hainaut, J Milner,

Nuclear Structure and Function

Research Article1 October 1992free access Interaction of heat-shock protein 70 with p53 translated in vitro: evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation. P. Hainaut P. Hainaut Department of Pathology, University of Cambridge, UK. Search for more papers by this author J. Milner J. Milner Department of Pathology, University of Cambridge, UK. Search for more papers by this author P. Hainaut P. Hainaut Department of Pathology, University of Cambridge, UK. Search for more papers by this author J. Milner J. Milner Department of Pathology, University of Cambridge, UK. Search for more papers by this author Author Information P. Hainaut1 and J. Milner1 1Department of Pathology, University of Cambridge, UK. The EMBO Journal (1992)11:3513-3520https://doi.org/10.1002/j.1460-2075.1992.tb05434.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info In intact cells, hsp70 proteins selectively complex with mutant p53. We report here that rabbit reticulocyte lysate contains hsp70 which selectively complexes with the mutant p53 translated in vitro. Hsp70 complexes with dimers and possibly monomers of p53 in a manner that requires the terminal 28 amino acids of p53. Using murine p53Val135, which is temperature-sensitive for phenotype, we demonstrate that p53-hsp70 complexes can occur after post-translational switching from wild-type to mutant p53 phenotype. Moreover, the temperature-induced switch of full-length p53Val135 from wild-type to mutant phenotype is ATP-independent, whereas the switch from mutant to wild-type form requires ATP hydrolysis and involves hsp70. These results imply that hsp70 is involved in the regulation of p53 conformation. Previous ArticleNext Article Volume 11Issue 101 October 1992In this issue RelatedDetailsLoading ...