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Titolo:
THE EPSTEIN-BARR-VIRUS NUCLEAR-PROTEIN-2 ACIDIC DOMAIN FORMS A COMPLEX WITH A NOVEL CELLULAR COACTIVATOR THAT CAN INTERACT WITH TFIIE
Autore:
TONG X; DRAPKIN R; YALAMANCHILI R; MOSIALOS G; KIEFF E;
Indirizzi:
12 S THORN BLDG,75 FRANCIS ST BOSTON MA 02115 HARVARD UNIV,DEPT MED BOSTON MA 02115 HARVARD UNIV,DEPT MICROBIOL & MOLEC GENET BOSTON MA 02115 UNIV MED & DENT NEW JERSEY,ROBERT WOOD JOHNSON MED SCH,HOWARD HUGHES MED INST,DEPT BIOCHEM PISCATAWAY NJ 08854
Titolo Testata:
Molecular and cellular biology
fascicolo: 9, volume: 15, anno: 1995,
pagine: 4735 - 4744
SICI:
0270-7306(1995)15:9<4735:TENADF>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA POLYMERASE-II; LATENT MEMBRANE-PROTEIN; TRANSCRIPTION FACTOR-IIE; HUMAN LYMPHOCYTES-B; ATP-CITRATE-LYASE; BURKITTS-LYMPHOMA; EXPRESSION; GENE; ANTIGEN-2; EBNA-2;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
65
Recensione:
Indirizzi per estratti:
Citazione:
X. Tong et al., "THE EPSTEIN-BARR-VIRUS NUCLEAR-PROTEIN-2 ACIDIC DOMAIN FORMS A COMPLEX WITH A NOVEL CELLULAR COACTIVATOR THAT CAN INTERACT WITH TFIIE", Molecular and cellular biology, 15(9), 1995, pp. 4735-4744

Abstract

Epstein-Barr virus nuclear antigen 2 (EBNA 2) activates transcriptionof specific genes and is essential for B-lymphocyte transformation, EBNA 2 has an acidic activation domain which interacts with general transcription factors TFIIB, TFIIH, and TAF40. We now show that EBNA 2 isspecifically bound to a novel nuclear protein, p100, and that p100 can coactivate gene expression mediated by the EBNA 2 acidic domain. TheEBNA 2 acidic domain was used to affinity purify p100. cDNA clones encoding the p100 open reading frame were identified on the basis of peptide sequences of the purified protein. Antibody against p100 coimmunoprecipitated p100 and EBNA 2 from Epstein-Barr virus-transformed lymphocyte extracts, indicating that EBNA 2 and p100 are complexed in vivo.p100 overexpression in cells specifically augmented EBNA 2 acidic domain-mediated activation. The coactivating effect is probably mediated by p100 interaction with TFIIE. Bacterially expressed p100 specifically adsorbs TFIIE from nuclear extracts, and in vitro-translated p56 or p34 TFIIE subunit can independently bind to p100, p100 also appears tobe essential for normal cell growth, since cell viability was reducedby antisense p100 RNA and restored by sense p100 RNA expression.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/10/20 alle ore 01:02:34