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Titolo:
FUNCTIONAL INTERACTION OF ADENOVIRUS-E1A WITH HOLO-TFIID
Autore:
BOYER TG; BERK AJ;
Indirizzi:
UNIV CALIF LOS ANGELES,INST MOLEC BIOL,DEPT MICROBIOL & MOLEC GENET LOS ANGELES CA 90024 UNIV CALIF LOS ANGELES,INST MOLEC BIOL,DEPT MICROBIOL & MOLEC GENET LOS ANGELES CA 90024
Titolo Testata:
Genes & development
fascicolo: 9, volume: 7, anno: 1993,
pagine: 1810 - 1823
SICI:
0890-9369(1993)7:9<1810:FIOAWH>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA POLYMERASE-II; EUKARYOTIC TRANSCRIPTIONAL ACTIVATORS; BOX-BINDING-PROTEIN; DOMAIN BINDS; E1A PROTEIN; GENE; IDENTIFICATION; PROMOTER; GAL4; DNA;
Keywords:
TRANSCRIPTION; TRANSCRIPTION FACTORS; TRANSCRIPTIONAL ACTIVATION; RNA POLYMERASE-II; TAFS; ACTIVATION DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
T.G. Boyer e A.J. Berk, "FUNCTIONAL INTERACTION OF ADENOVIRUS-E1A WITH HOLO-TFIID", Genes & development, 7(9), 1993, pp. 1810-1823

Abstract

The activation domains of several regulatory transcription factors have been shown to bind directly in vitro to the TATA box-binding protein (TBP). Yet TBP must also interact with multiple associated polypeptides, called TAFs, for these same activators to stimulate transcription. These findings raise the question of how TBP can interact with so many proteins, both activators and TAFs, simultaneously. Here, we show that the activation domain of the adenovirus large E1A protein can bindspecifically and stably to isolated holo-TFIID, the multisubunit protein complex consisting of TBP plus TAFs. Consequently, the surface of TBP that interacts with E1A must be exposed in the holo-TFIID complex. To assess the functional significance of this interaction, we established an in vitro transcription system responsive to the E1A activationdomain. The addition of excess E1A to this system inhibits (squelches) both E1A-dependent and E1A-independent transcription by sequesteringa target factor required for E1A activation. From among the componentactivities that collectively reconstitute E1A-responsive transcription in this system, holo-TFIID alone is singularly capable of reversing the inhibition of transcription mediated by excess E1A, indicating that holo-TFIID is the direct functional target of the E1A activation domain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 21:51:34