Structural highlights
Publication Abstract from PubMedChromatin 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-Angstrom 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 beta-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 Metastasis Associated-1 (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 structure provides insight into the molecular determinants of FOG-1 dependent association with the NuRD complex and into the links between transcriptional regulation and nucleosome remodelling. Insights into the association of the nucleosome remodelling and deacetylase (NURD) complex with friend of gata-1 (FOG-1) from the crystal structure of a retinoblastoma associated protein-48 (RBAP48) fog-1 complex.,Lejon S, Thong SY, Murthy A, Alqarni S, Murzina NV, Blobel GA, Laue ED, Mackay JP J Biol Chem. 2010 Nov 2. PMID:21047798[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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