Insights into Association of the NuRD Complex with FOG-1 from the Crystal Structure of an RbAp48·FOG-1 Complex
نویسندگان
چکیده
منابع مشابه
Insights into Association of the NuRD Complex with FOG-1 from the Crystal Structure of an RbAp48·FOG-1 Complex*
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 n...
متن کاملFOG-1 recruits the NuRD repressor complex to mediate transcriptional repression by GATA-1.
Transcription factor GATA-1 and its cofactor FOG-1 coordinate erythroid cell maturation by activating erythroid-specific genes and repressing genes associated with the undifferentiated state. Here we show that FOG-1 binds to the NuRD corepressor complex in vitro and in vivo. The interaction is mediated by a small conserved domain at the extreme N-terminus of FOG-1 that is necessary and sufficie...
متن کاملThe structure of the core NuRD repression complex provides insights into its interaction with chromatin
The NuRD complex is a multi-protein transcriptional corepressor that couples histone deacetylase and ATP-dependent chromatin remodelling activities. The complex regulates the higher-order structure of chromatin, and has important roles in the regulation of gene expression, DNA damage repair and cell differentiation. HDACs 1 and 2 are recruited by the MTA1 corepressor to form the catalytic core ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2011
ISSN: 0021-9258
DOI: 10.1074/jbc.m110.195842