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Insights into association of the NuRD complex with FOG-1 from the crystal structure of an RbAp48·FOG-1 complex

DOI: 10.1074/jbc.M110.195842 DOI Help
PMID: 21047798 PMID Help

Authors: Sara Lejon (University of Cambridge) , Sock Yue Thong (University of Sydney) , Andal Murthy (University of Cambridge) , Saad Alqarni (University of Sydney) , Nathalie V. Murzina (University of Cambridge) , Gerd A. Blobel (Children's Hospital of Philadelphia) , Ernest D. Laue (University of Cambridge) , Joel P. Mackay (University of Sydney)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Biological Chemistry , VOL 286 (2) , PAGES 1196-1203

State: Published (Approved)
Published: November 2010

Open Access Open Access

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 β-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.

Journal Keywords: Animals; Binding; Cells; Cultured; Conserved; Crystallography; X-Ray; Histone; Histones; Mi-2; Microfilament; Nuclear; Protein; Tertiary; Recombinant; Repressor; Retinoblastoma-Binding; Spodoptera; Transcription; Transcription; Genetic

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: I03-Macromolecular Crystallography

Added On: 11/01/2011 08:58


Discipline Tags:

Biochemistry Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)