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Titolo:
A DOMAIN NECESSARY FOR THE TRANSFORMING ACTIVITY OF SNON IS REQUIRED FOR SPECIFIC DNA-BINDING, TRANSCRIPTIONAL REPRESSION AND INTERACTION WITH TAF(II)110
Autore:
COHEN SB; NICOL R; STAVNEZER E;
Indirizzi:
CASE WESTERN RESERVE UNIV,DEPT BIOCHEM CLEVELAND OH 44106 CASE WESTERN RESERVE UNIV,DEPT BIOCHEM CLEVELAND OH 44106 UNIV CINCINNATI,COLL MED,DEPT MOL GENET BIOCHEM & MICROBIOL CINCINNATI OH 45267
Titolo Testata:
Oncogene
fascicolo: 19, volume: 17, anno: 1998,
pagine: 2505 - 2513
SICI:
0950-9232(1998)17:19<2505:ADNFTT>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
THYROID-HORMONE RECEPTOR; ADENOVIRUS E1A PROTEIN; FUNCTIONAL-ANALYSIS; CDNA CLONES; GENE; ACTIVATION; SKI; GAL4; OVEREXPRESSION; IDENTIFICATION;
Keywords:
ONCOGENE; REPRESSION; SNON; TRANSCRIPTION; TRANSFORMATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
S.B. Cohen et al., "A DOMAIN NECESSARY FOR THE TRANSFORMING ACTIVITY OF SNON IS REQUIRED FOR SPECIFIC DNA-BINDING, TRANSCRIPTIONAL REPRESSION AND INTERACTION WITH TAF(II)110", Oncogene, 17(19), 1998, pp. 2505-2513

Abstract

sno is a member of the ski oncogene family and shares ski's ability to transform avian fibroblasts and induce muscle differentiation. Ski and Sno are nuclear proteins that form homodimers and heterodimers, Skiactivates transcription of cellular and viral enhancers and we have identified a DNA binding site (GTCTAGAC) through which it represses transcription. In this work, we show that SnoN binds this site and represses transcription of reporters a with this binding site as an upstreamelement. Using fusions with the Gal4-DNA binding domain in a heterologous reporter assay, we identify a tripartite repression domain in SnoN, A 107 amino acid stretch of the SnoN repression domain, that contains two of the subdomains, is closely related to the minimal region of Ski required for transformation. The third subdomain is unique to SnoN, By analysing deletions involving each of the subdomains, we show that subdomains II and III are also required for DNA binding and cellulartransformation. We provide evidence for a quenching mechanism of transcriptional repression by which subdomain II binds to TAF(II)11O.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 10:27:46