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Titolo:
Histone deacetylases specifically down-regulate p53-dependent gene activation
Autore:
Juan, LJ; Shia, WJ; Chen, MH; Yang, WM; Seto, E; Lin, YS; Wu, CW;
Indirizzi:
Natl Hlth Res Inst, Taipei 115, Taiwan Natl Hlth Res Inst Taipei Taiwan 115 l Hlth Res Inst, Taipei 115, Taiwan Acad Sinica, Inst Biomed Sci, Taipei 11529, Taiwan Acad Sinica Taipei Taiwan 11529 a, Inst Biomed Sci, Taipei 11529, Taiwan Univ S Florida, H Lee Moffitt Canc Ctr & Res Inst, Mol Oncol Program, Tampa, FL 33612 USA Univ S Florida Tampa FL USA 33612 Mol Oncol Program, Tampa, FL 33612 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 27, volume: 275, anno: 2000,
pagine: 20436 - 20443
SICI:
0021-9258(20000707)275:27<20436:HDSDPG>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
WILD-TYPE P53; TRANSCRIPTIONAL REPRESSION; IN-VIVO; DNA METHYLATION; ACETYLATION; CBP; ACETYLTRANSFERASES; EXPRESSION; CHROMATIN; FAMILY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Wu, CW Natl Hlth Res Inst, 128 Yen Chiu Yuan Rd,Sec 2, Taipei 115, Taiwan Natl Hlth Res Inst 128 Yen Chiu Yuan Rd,Sec 2 Taipei Taiwan 115 an
Citazione:
L.J. Juan et al., "Histone deacetylases specifically down-regulate p53-dependent gene activation", J BIOL CHEM, 275(27), 2000, pp. 20436-20443

Abstract

p53, the most commonly mutated gene in cancer cells, directs cell cycle arrest or induces programmed cell death (apoptosis) in response to stress. Ithas been demonstrated that p53 activity is up-regulated in part by posttranslational acetylation. In agreement with these observations, here we show that mammalian histone deacetylase (HDAC)-1, -2, and -3 are all capable of downregulating p53 function. Down-regulation of p53 activity by HDACs is HDAC dosage-dependent, requires the deacetylase activity of HDACs, and depends on the region of p53 that is acetylated by p300/CREB-binding protein (CBP). These results suggest that interactions of p53 and HDACs likely result in p53 deacetylation, thereby reducing its transcriptional activity. In support of this idea, GST pull-down and immunoprecipitation assays show that p53 interacts with HDAC1 both in vitro and in vivo. Furthermore, a pre-acetylated p53 peptide was significantly deacetylated by immunoprecipitated wild type HDAC1 but not deacetylase mutant. Also, coexpression of HDAC1 greatly reduced the in vivo acetylation level of p53. Finally, we report that the activation potential of p53 on the BAX promoter, a natural p53-responsive system, is reduced in the presence of HDACs. Taken together; our findings indicate that deacetylation of p53 by histone deacetylases is likely to be part of the mechanisms that control the physiological activity of p53.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 22:25:31