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Titolo:
ADENOVIRUS E1A PROTEINS INTERACT WITH THE CELLULAR YY1 TRANSCRIPTION FACTOR
Autore:
LEWIS BA; TULLIS G; SETO E; HORIKOSHI N; WEINMANN R; SHENK T;
Indirizzi:
PRINCETON UNIV,HOWARD HUGHES MED INST,DEPT MOLEC BIOL PRINCETON NJ 08544 PRINCETON UNIV,HOWARD HUGHES MED INST,DEPT MOLEC BIOL PRINCETON NJ 08544
Titolo Testata:
Journal of virology
fascicolo: 3, volume: 69, anno: 1995,
pagine: 1628 - 1636
SICI:
0022-538X(1995)69:3<1628:AEPIWT>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
RETINOBLASTOMA GENE-PRODUCT; BINDING PROTEIN; DNA-SYNTHESIS; ACTIVATION; TRANSFORMATION; REPRESSION; SEQUENCE; ENHANCER; FAMILY; REGION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
54
Recensione:
Indirizzi per estratti:
Citazione:
B.A. Lewis et al., "ADENOVIRUS E1A PROTEINS INTERACT WITH THE CELLULAR YY1 TRANSCRIPTION FACTOR", Journal of virology, 69(3), 1995, pp. 1628-1636

Abstract

The adenovirus 12S and 13S E1A proteins have been shown to relieve repression mediated by the cellular transcription factor YY1. The 13S E1A protein not only relieves repression but also activates transcription through YY1 binding sites. In this study, using a variety of in vivoand in vitro assays, we demonstrate that both E1A proteins can bind to YY1, although the 13S E1A protein binds more efficiently than the 12S E1A protein. Two domains on the E1A proteins interact with YY1: an amino-terminal sequence (residues 15 to 35) that is present in both E1Aproteins and a domain that includes at least a portion of conserved region 3 (residues 140 to 188) that is present in the 13S but not the 12S E1A protein. Two domains on YY1 interact with EIA proteins: one is contained within residues 54 to 260, and the other is contained withinthe carboxy-terminal domain of YY1 (residues 332 to 414). Cotransfection of a plasmid expressing carboxy-terminal amino acids 332 to 414 ofYY1 fused to the GALA DNA-binding domain can inhibit expression from a reporter construct with GAIA DNA binding sites in its promoter, and inclusion of a third plasmid expressing ELA proteins can relieve the repression. Thus, we find a correlation between the ability of E1A to interact with the carboxy-terminal domain of YY1 and its ability to relieve repression caused by the carboxy-terminal domain of YY1. We propose that E1A proteins normally relieve YY1-mediated transcriptional repression by binding directly to the cellular transcription factor.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 08:25:29