Insights into association of the NuRD complex with FOG-1 from the crystal structure of an RbAp48·FOG-1 complex.
J Biol Chem
; 286(2): 1196-203, 2011 Jan 14.
Article
en En
| MEDLINE
| ID: mdl-21047798
ABSTRACT
Chromatin-modifying complexes such as the NuRD complex are recruited to particular genomic sites by gene-specific nuclear factors. Overall, however, little is known about the molecular basis for these interactions. Here, we present the 1.9 Å resolution crystal structure of the NuRD subunit RbAp48 bound to the 15 N-terminal amino acids of the GATA-1 cofactor FOG-1. The FOG-1 peptide contacts a negatively charged binding pocket on top of the RbAp48 ß-propeller that is distinct from the binding surface used by RpAp48 to contact histone H4. We further show that RbAp48 interacts with the NuRD subunit MTA-1 via a surface that is distinct from its FOG-binding pocket, providing a first glimpse into the way in which NuRD assembly facilitates interactions with cofactors. Our RbAp48·FOG-1 structure provides insight into the molecular determinants of FOG-1-dependent association with the NuRD complex and into the links between transcription regulation and nucleosome remodeling.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Represoras
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Factores de Transcripción
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Transcripción Genética
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Proteínas Nucleares
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Complejo Desacetilasa y Remodelación del Nucleosoma Mi-2
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Proteína 4 de Unión a Retinoblastoma
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Histona Desacetilasas
Tipo de estudio:
Risk_factors_studies
Idioma:
En
Año:
2011
Tipo del documento:
Article