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Titolo:
Adenovirus early region 1A protein binds to mammalian SUG1-a regulatory component of the proteasome
Autore:
Grand, RJA; Turnell, AS; Mason, GGF; Wang, WL; Milner, AE; Mymryk, JS; Rookes, SM; Rivett, AJ; Gallimore, PH;
Indirizzi:
Univglandingham, CRC, Inst Canc Studies, Birmingham B15 2TA, W Midlands, En Univ Birmingham Birmingham W Midlands England B15 2TA 2TA, W Midlands, En JohnsAHopkins Univ, Sch Med, Howard Hughes Med Inst, Baltimore, MD 21205 US Johns Hopkins Univ Baltimore MD USA 21205 ed Inst, Baltimore, MD 21205 US Johns Hopkins Univ, Sch Med, Dept Mol Biol & Genet, Baltimore, MD 21205 USA Johns Hopkins Univ Baltimore MD USA 21205 Genet, Baltimore, MD 21205 USA Univ Bristol, Dept Biochem, Bristol BS8 1TD, Avon, England Univ Bristol Bristol Avon England BS8 1TD Bristol BS8 1TD, Avon, England Univ Western Ontario, Dept Oncol, London, ON N6A 4L6, Canada Univ Western Ontario London ON Canada N6A 4L6 London, ON N6A 4L6, Canada
Titolo Testata:
ONCOGENE
fascicolo: 2, volume: 18, anno: 1999,
pagine: 449 - 458
SICI:
0950-9232(19990114)18:2<449:AER1PB>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
WILD-TYPE P53; E1A PROTEIN; TRANSCRIPTIONAL MEDIATOR; TUMOR-SUPPRESSOR; EPITHELIAL-CELLS; 26-S PROTEASOME; DNA-SYNTHESIS; ACTIVATION; APOPTOSIS; SUBUNIT;
Keywords:
adenovirus; adenovirus 12; E1A; SUG1; proteasome; Trip 1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Grand, RJA Univglandingham, CRC, Inst Canc Studies, Birmingham B15 2TA, W Midlands, En Univ Birmingham Birmingham W Midlands England B15 2TA ands, En
Citazione:
R.J.A. Grand et al., "Adenovirus early region 1A protein binds to mammalian SUG1-a regulatory component of the proteasome", ONCOGENE, 18(2), 1999, pp. 449-458

Abstract

Adenovirus early region 1A (Ad E1A) is a multifunctional protein which is essential for adenovirus-mediated transformation and oncogenesis, Whilst E1A is generally considered to exert its influence on recipient cells throughregulation of transcription it also increases the le, el of cellular p53 by increasing the protein half-life. With this in, view, we have investigated the relationship of Ad E1A to the proteasome, which is normally responsible for degradation of p53, Here we have shown that both Ad5 and Ad12 EIA 12S and 13S proteins can be co-immunoprecipitated with proteasomes and that the larger Ad12 E1A protein binds strongly to at least three components of the 26S but not 20S proteasome, One of these interacting species has been identified as mammalian SUG1, a proteasome regulatory component which also plays a role in the cell as a mediator of transcription, In vitro assays havedemonstrated a direct interaction between Ad12 E1A 13S protein and mouse SUG1, Following infection of human cells with Ad5 wt and Ad5 mutants with lesions in the E1A gene it has been shown that human SUG1 can be co-immunoprecipitated with full-length E1A and with E1A carrying a deletion in conserved region 1 which is the region considered to be responsible for increased expression of p53, We have concluded therefore that Ad E1A binds strongly toSUG1 but that this interaction is not responsible for inhibition of proteasome activity, This is consistent with the observation that purified Ad12 E1A inhibits the activity of the purified 20S but not 26S proteasomes, We have also demonstrated that SUG1 can be co-immunoprecipitated with SV40 T andtherefore,ve suggest that this may represent a common interaction of transforming proteins of DNA tumour viruses.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 09:55:50