Modification of two distinct COOH-terminal domains is required for murine p53 activation by bacterial Hsp70.

The Journal of Biological Chemistry
S HansenT R Hupp

Abstract

Activation of the latent DNA binding function of human p53 protein by the bacterial Hsp70, DnaK, represents a unique reaction in which a heat shock protein can interact with a native protein to affect its function. We have localized a likely DnaK interaction site on native human p53 tetramers to a motif flanking the COOH-terminal casein kinase II and protein kinase C phosphorylation sites. Murine p53 is less efficiently activated by DnaK, which has permitted a search for factors that might cooperate in p53 activation by DnaK. We show that optimal activation by DnaK may be dependent upon the phosphorylation state of murine p53, in particular, modification of p53 at the cdc2 phosphorylation site by point mutation decreases the extent of activation by DnaK. Additionally, the monoclonal antibody PAb241, binding in the vicinity of the cdc2 phosphorylation site, is able to activate the specific DNA binding function of p53. This has led us to propose a second regulatory motif flanking the tetramerization domain of p53 that cooperates with factors binding at the negative regulatory domain in the extreme COOH terminus.

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Citations

Aug 5, 1998·Pharmacology & Therapeutics·M Scheffner
Sep 25, 2009·European Journal of Cancer : Official Journal for European Organization for Research and Treatment of Cancer (EORTC) [and] European Association for Cancer Research (EACR)·Yosef Buganim, Varda Rotter
Nov 4, 2000·The Biochemical Journal·T R HuppK L Ball
Jun 10, 1998·The Journal of Investigative Dermatology·K NakazawaH Nakazawa
Apr 3, 1999·The Journal of Biological Chemistry·C DelphinJ Baudier
Feb 19, 2002·Oncogene·Mana MiyakodaMasami Watanabe
May 26, 1999·The Journal of Pathology·C Prives, P A Hall
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May 31, 2003·Oncogene·Marcus Achison, Ted R Hupp
Nov 18, 2000·The Journal of Biological Chemistry·J P BlaydesT R Hupp
Jul 8, 2000·Journal of Molecular Biology·M G LucianiT R Hupp

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