Purification of a human SRCAP complex that remodels chromatin by incorporating the histone variant H2A.Z into nucleosomes.
Biochemistry
; 45(17): 5671-7, 2006 May 02.
Article
en En
| MEDLINE
| ID: mdl-16634648
The Snf-2-related CREB-binding protein activator protein (SRCAP) serves as a coactivator for a number of transcription factors known to interact with CBP. Swr1, the closest Saccharomyces cerevisiae ortholog of SRCAP, is a component of the chromatin remodeling complex SWR-C, which catalyzes exchange of the histone variant H2A.Z into nucleosomes. In this report, we use a combination of conventional chromatography and anti-SRCAP immunoaffinity chromatography to purify a native human SRCAP complex with a polypeptide composition similar to that of SWR-C, and we show for the first time that this SRCAP-containing complex supports ATP-dependent exchange of histone dimers containing H2B and H2A.Z into mononucleosomes reconstituted with recombinant H2A, H2B, H3, and H4. Our findings, together with previous evidence implicating H2A.Z in transcriptional regulation, suggest that SRCAP's coactivator function may depend on its ability to promote incorporation of H2A.Z into chromatin.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Cromatina
/
Histonas
/
Nucleosomas
/
Adenosina Trifosfatasas
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Proteínas de Saccharomyces cerevisiae
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Complejos Multiproteicos
Idioma:
En
Revista:
Biochemistry
Año:
2006
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Estados Unidos