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Titolo:
DETERMINATION OF FUNCTIONAL DOMAINS IN THE C-SUBUNIT OF THE CCAAT-BINDING FACTOR (CBF) NECESSARY FOR FORMATION OF A CBF-DNA COMPLEX - CBF-BINTERACTS SIMULTANEOUSLY WITH BOTH THE CBF-A AND CBF-C SUBUNITS TO FORM A HETEROTRIMERIC CBF MOLECULE
Autore:
KIM IS; SINHA S; DECROMBRUGGHE B; MAITY SN;
Indirizzi:
UNIV TEXAS,MD ANDERSON CANC CTR,DEPT MOLEC GENET,1515 HOLCOMBE BLVD HOUSTON TX 77030 UNIV TEXAS,MD ANDERSON CANC CTR,DEPT MOLEC GENET HOUSTON TX 77030
Titolo Testata:
Molecular and cellular biology
fascicolo: 8, volume: 16, anno: 1996,
pagine: 4003 - 4013
SICI:
0270-7306(1996)16:8<4003:DOFDIT>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTION FACTOR; NF-Y; SEQUENCE IDENTITY; HISTONE OCTAMER; PROTEIN; YEAST; HAP2;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
I.S. Kim et al., "DETERMINATION OF FUNCTIONAL DOMAINS IN THE C-SUBUNIT OF THE CCAAT-BINDING FACTOR (CBF) NECESSARY FOR FORMATION OF A CBF-DNA COMPLEX - CBF-BINTERACTS SIMULTANEOUSLY WITH BOTH THE CBF-A AND CBF-C SUBUNITS TO FORM A HETEROTRIMERIC CBF MOLECULE", Molecular and cellular biology, 16(8), 1996, pp. 4003-4013

Abstract

The mammalian CCAAT-binding factor (CBF; also called NF-Y and CP1) isa heterotrimeric protein consisting of three subunits, CBF-A, CBF-B, and CBF-C, all of which are required for DNA binding and all of which are present in the CBF-DNA complex. In this study using cross-linking and immunoprecipitation methods, we first established that CBF-B interacts simultaneously with both subunits of the CBF-A-CBFG heterodimer to form a heterotrimeric CBF molecule. We then performed a mutational analysis of CBF-C to define functional interactions with the other two CBF subunits and with DNA using several in vitro assays and an in vivoyeast two-hybrid system. Our experiments established that the evolutionarily conserved segment of CBF-C, which shows similarities with the histone-fold motif of histone H2A, was necessary for formation of the CBF-DNA complex. The domain of CBF-C which interacts with CBF-A included a large portion of this segment, one that corresponds to the segment of the histone-fold moth in H2A used for interaction with H2B. Two classes of interactions involved in formation of the CBF-A-CBF-C heterodimer were detected; one class, provided by residues in the middle of the interaction domain, was needed for formation of the CBF-A-CBF-C heterodimer. The other, provided by sequences flanking those of the first class was needed for stabilization of the heterodimer. Two separate domains were identified in the conserved segment of CBF-C for interaction with CBF-B; these were located on each side of the CBF-A interaction domain. Since our previous experiments identified a single CBF-B interaction domain in the histone-fold motif of CBF-A, we propose that atridentate interaction domain in the CBF-A-CBF-C heterodimer interacts with the 21-amino-acid-long subunit interaction domain of CBF-B. Together with our previous mutational analysis of CBF-A (S. Sinha, L-S. Rim, K.-Y. Sohn, B. de Crombrugghe, and S. N. Maity, Mol. Cell. Biol. 16:328-337, 1996), this study demonstrates that the histone fold-motifsof CBF-A and CBF-C interact with each other to form the CBF-A-CBF-C heterodimer and generate a hybrid surface which then interacts with CBF-B to form the heterotrimeric CBF molecule.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 09:49:13