Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 289, Issue 32, Pages 21844-21855Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M114.558940
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Funding
- National Institutes of Health [OD010949-10]
- European Commission through 4DCell-Fate project (EC FP7) [CP 277899]
- MRC [G1001696] Funding Source: UKRI
- Cancer Research UK [11431] Funding Source: researchfish
- Medical Research Council [G1001696] Funding Source: researchfish
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The nucleosome remodeling and deacetylase (NuRD) complex is a widely conserved transcriptional co-regulator that harbors both nucleosome remodeling and histone deacetylase activities. It plays a critical role in the early stages of ES cell differentiation and the reprogramming of somatic to induced pluripotent stem cells. Abnormalities in several NuRD proteins are associated with cancer and aging. We have investigated the architecture of NuRDby determining the structure of a subcomplex comprising RbAp48 and MTA1. Surprisingly, RbAp48 recognizes MTA1 using the same site that it uses to bind histone H4, showing that assembly into NuRD modulates RbAp46/48 interactions with histones. Taken together with other results, our data show that the MTA proteins act as scaffolds for NuRD complex assembly. We further show that the RbAp48-MTA1 interaction is essential for the in vivo integration of RbAp46/48 into the NuRD complex.
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