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Titolo:
Co-operative DNA binding by GAGA transcription factor requires the conserved BTB/POZ domain and reorganizes promoter topology
Autore:
Katsani, KR; Hajibagheri, MAN; Verrijzer, CP;
Indirizzi:
Imperial Canc Res Fund, London WC2A 3PX, England Imperial Canc Res Fund London England WC2A 3PX London WC2A 3PX, England
Titolo Testata:
EMBO JOURNAL
fascicolo: 3, volume: 18, anno: 1999,
pagine: 698 - 708
SICI:
0261-4189(19990201)18:3<698:CDBBGT>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACUTE PROMYELOCYTIC LEUKEMIA; RNA-POLYMERASE-II; PROTEIN INTERACTION MOTIF; ALPHA FUSION PROTEINS; HEAT-SHOCK PROMOTER; DROSOPHILA-MELANOGASTER; NUCLEOSOME DISRUPTION; CHROMATIN STRUCTURE; REPRESSING DOMAIN; GENE-EXPRESSION;
Keywords:
BTB; POZ domain; chromatin; DNA bending; GAGA; transcription;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Verrijzer, CP Imperial Canc Res Fund, 44 Lincolns Inn Fields, London WC2A 3PX, England Imperial Canc Res Fund 44 Lincolns Inn Fields London England WC2A 3PX
Citazione:
K.R. Katsani et al., "Co-operative DNA binding by GAGA transcription factor requires the conserved BTB/POZ domain and reorganizes promoter topology", EMBO J, 18(3), 1999, pp. 698-708

Abstract

The POZ domain is a conserved protein-protein interaction motif present ina variety of transcription factors involved in development, chromatin remodelling and human cancers, Here, we study the role of the POZ domain of theGAGA transcription factor in promoter recognition. Natural target promoters for GAGA typically contain multiple GAGA-binding elements. Our results show that the POZ domain mediates strong cooperative binding to multiple sites but inhibits binding to single sites. Protein cross-linking and gel filtration chromatography experiments established that the POZ domain is required for GAGA oligomerization into higher order complexes. Thus, GAGA oligomerization increases binding specificity by selecting only promoters with multiple sites. Electron microscopy revealed that GAGA binds to multiple sites as a large oligomer and induces bending of the promoter DNA. Our results indicate a novel mode of DNA binding by GAGA, in which a large GAGA complex binds multiple GAGA elements that are spread out over a region of a few hundred base pairs. We suggest a model in which the promoter DNA is wrapped around a GAGA multimer in a conformation that may exclude normal nucleosome formation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 11:06:42