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>RBBP4 / RBAP48 Protein & cDNA Clone
RBBP4 / RBAP48 Protein & cDNA Clone
RBAP48 / RBBP4 Related Areas
RBAP48 / RBBP4 Alternative Names
RBBP4, RBAP48, NURF55, CAF-1 subunit C, CAF-I 48 kDa subunit, CAF-I p48, RBBP-4 [Homo sapiens]
Rbbp4, RP23-391E6.3, mRbAp48, CAF-1 p48 subunit, CAF-1 subunit C, CAF-I 48 kDa subunit, CAF-I p48, RBBP-4 [Mus musculus]
RBAP48 / RBBP4 Background
Histone-binding protein RBBP4, also known as Retinoblastoma-binding protein 4, Retinoblastoma-binding protein p48, Chromatin assembly factor 1 subunit C, Chromatin assembly factor I p48 subunit, Nucleosome-remodeling factor subunit RBAP48 and RBBP4, is a nucleus protein which belongs to the WD repeat RBAP46/RBAP48/MSI1 family. RBBP4 is a core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. RBBP4 is a component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling and the NURF (nucleosome remodeling factor) complex.
RBAP48 / RBBP4 Roles in Age-related Memory Loss
Lows amounts of a brain protein called RbAp48 protein may be responsible for the memory loss that normally occurs in older individuals, a U.S. study said Wednesday. One common myth is that age-related memory loss is an early indication of Alzheimer's disease. But researchers at the Columbia University Medical Center in New York City have found a specific protein, RbAp48, that they believe is responsible for age-related memory problems. What's more, by replenishing RbAp48 in the brains of mice, the researchers were able to undo existing age-related memory damage. Learn more...
Structural Basis for RBAP48 Binding to FOG-1
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. 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 has been analysed. 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. 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. The 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.