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Modulation of p53 protein conformation and DNA-binding activity by intracellular chelation of zinc

✍ Scribed by Gerald W. Verhaegh; Marie-Odile Parat; Marie-Jeanne Richard; Pierre Hainaut

Publisher: John Wiley and Sons
Year: 1998
Tongue: English
Weight: 295 KB
Volume: 21
Category: Article
ISSN: 0899-1987
DOI: 10.1002/(sici)1098-2744(199803)21:3<205::aid-mc8>3.0.co;2-k

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✦ Synopsis

The transcription factor p53 controls the proliferation and survival of cells exposed to DNA damage. The specific DNA-binding domain of p53 (residues 102-292) has a complex tertiary structure that is stabilized by zinc. In this study, we showed that exposure of cultured cells to the membrane-permeable chelator N,N,N´, N´-tetrakis(2-pyridylmethyl)ethylenediamine induced wild-type p53 to accumulate in an immunologically "mutant" form (PAb240+, PAb1620-) with decreased DNA-binding activity. Removal of N,N,N´,N´-tetrakis(2pyridylmethyl)ethylenediamine from culture medium allowed p53 to refold into the immunologically wild-type form, followed by a transient increase in DNA binding, expression of the cyclin-dependent kinase inhibitor p21 WAF1 , and cell-cycle delay in the G 1 phase. Thus, modulation of intracellular zinc induced conformational changes in p53 that activated wild-type function, suggesting that metalloregulation may play a role in controlling p53.

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