Abstract:
:p300 acetylates and activates the tumor suppressor p53 after DNA damage. Here, we show that MDM2, a negative-feedback regulator of p53, inhibited p300-mediated p53 acetylation by complexing with these two proteins. First, we purified a p300-MDM2-p53 protein complex from HeLa nuclear extracts, which was inactive in p53 acetylation, but active in histone acetylation. Also, wild-type, but not N-terminally deleted, MDM2 inhibited p53 acetylation by p300 in vitro and in vivo. This inhibition was specific for p53, because MDM2 did not affect acetylation of histones or the C terminus of p73 by p300. Consequently, wild-type, but not the mutant, MDM2 repressed the p300-stimulated sequence-specific DNA-binding and transcriptional activities of p53. These results demonstrate that an additional mechanism of p53 inactivation by MDM2 is to inhibit p53 acetylation by p300.
journal_name
Proc Natl Acad Sci U S Aauthors
Kobet E,Zeng X,Zhu Y,Keller D,Lu Hdoi
10.1073/pnas.97.23.12547keywords:
subject
Has Abstractpub_date
2000-11-07 00:00:00pages
12547-52issue
23eissn
0027-8424issn
1091-6490pii
97/23/12547journal_volume
97pub_type
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