Insights into association of the NuRD complex with FOG-1 from the crystal structure of an RbAp48·FOG-1 complex. Lejon, S., Thong, S., Murthy, A., AlQarni, S., Murzina, N., Blobel, G., Laue, E., & Mackay, J. Journal of Biological Chemistry, 286(2):1196-1203, 2011.
doi  abstract   bibtex   
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. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
@article{
 title = {Insights into association of the NuRD complex with FOG-1 from the crystal structure of an RbAp48·FOG-1 complex},
 type = {article},
 year = {2011},
 pages = {1196-1203},
 volume = {286},
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 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. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.},
 bibtype = {article},
 author = {Lejon, S. and Thong, S.Y. and Murthy, A. and AlQarni, S. and Murzina, N.V. and Blobel, G.A. and Laue, E.D. and Mackay, J.P.},
 doi = {10.1074/jbc.M110.195842},
 journal = {Journal of Biological Chemistry},
 number = {2}
}

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