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CCR4 (show CCR4 Proteins) and CAF1, the two deadenylases in the CCR4 (show CCR4 Proteins)-NOT complex, can remove 3' terminal non-A residues in an exonucleolytic manner.
CAF1-p180 (show RRBP1 Proteins) and CAF1-p75 (show HNRNPM Proteins) subunits mediate assembly of two different forms of chromatin.
CAF-1 promotes Notch (show NOTCH1 Proteins) signaling through epigenetic control of target gene expression during Drosophila development.
these studies suggest that p55 is not crucial for PRC2-mediated gene silencing in vivo, and the vital function of p55 is probably not dependent on its interaction with histone H4.
Chromatin-modifying complex component Nurf55/p55 associates with histones H3 and H4 and polycomb (show CBX2 Proteins) repressive complex 2 subunit Su(z)12 through partially overlapping binding sites.
analysis of Caf1 mutant tissue suggests that Caf1 plays important roles in cell survival and segment identity, and loss of Caf1 is associated with a reduction in the Polycomb (show CBX2 Proteins) Repressive Complex 2 (PRC2)-specific histone methylation mark H3K27me3
spreading of heterochromatin is compromised in flies that have reduced CAF-1 p180 (show RRBP1 Proteins). Furthermore, reduced CAF-1 p180 (show RRBP1 Proteins) causes a defect in the dynamics of heterochromatic markers in early Drosophila embryos.
sliding model in which the position-specific tethering of NURF forces a translocating ISWI ATPase to pump a DNA distortion over the histone octamer, thereby changing the translational position of the nucleosome.
Data show that removal of p55 deregulated the expression of E2F targets that are normally repressed by dE2F2/RBF-1 and -2 complexes in a cell cycle-independent manner but had no effect on the expression of targets normally coupled with cell proliferation.
The nucleosome-binding subunits Su(z)12 and Nurf55 anchor the E(z) enzyme on chromatin substrates, an essential process in maintaining HOX (show MSH2 Proteins) gene silencing during development.
The MTA1 (show MTA1 Proteins) subunit of the nucleosome remodeling and deacetylase complex can recruit two copies of RBBP4/RBBP7 (show RBBP7 Proteins).
RbAp48 is likely to act as a potent antiretroviral defense.
The crystal structure reveals an extensive interface between MTA1 (show MTA1 Proteins) and RBBP4.
RBBP4 interacts with ep300 (show EP300 Proteins) protein to form a complex that drives the expression of methylguanine-DNA-methyltransferase (show MGMT Proteins) , RAD51 (show RAD51 Proteins), and other selected DNA repair genes through histone acetylation.
RbAp48 was identified as critical in the proliferation of hypopharyngeal carcinoma in both in vitro and in vivo experiments.
RBBP4 functions as a novel regulatory factor to increase the efficiency of importin alpha/beta-mediated nuclear import
Our RBBP4-PHF6 (show PHF6 Proteins) complex structure provides insights into the molecular basis of PHF6 (show PHF6 Proteins)-NuRD complex interaction and implicates a role for PHF6 (show PHF6 Proteins) in chromatin structure modulation and gene regulation.
Our results reveal that the protein structure does not affect ligand binding, and the top three TCM candidates Bittersweet alkaloid II, Eicosandioic acid, and Perivine might resolve the instability of the RbAp48-FOG1 (show ZFPM1 Proteins) complex
RbAp48 recognizes MTA1 (show MTA1 Proteins) using the same site that it uses to bind histone H4, showing that assembly into NuRD modulates RbAp46 (show RBBP7 Proteins)/48 interactions with histones.
The most significant change was an age-related decline in RbAp48, a histone-binding protein that modifies histone acetylation.
RBBP4 is a regulator of histone deacetylation during oocyte maturation and deacetylation is required for bipolar spindle assembly through Aurora kinase C (show AURKC Proteins)
Studies indicate that estrogen deficiency initiates tissue-specific apoptosis in the exocrine gland cells through RbAp48 overexpression.
Estrogen deficiency initiates p53 (show TP53 Proteins)-mediated apoptosis in the exocrine glands through Rbbp4 overexpression.
Results report that transgenic expression of RbAp48 resulted in the development of autoimmune exocrinopathy resembling Sjogren's syndrome.
This gene encodes a ubiquitously expressed nuclear protein which belongs to a highly conserved subfamily of WD-repeat proteins. It is present in protein complexes involved in histone acetylation and chromatin assembly. It is part of the Mi-2 complex which has been implicated in chromatin remodeling and transcriptional repression associated with histone deacetylation. This encoded protein is also part of co-repressor complexes, which is an integral component of transcriptional silencing. It is found among several cellular proteins that bind directly to retinoblastoma protein to regulate cell proliferation. This protein also seems to be involved in transcriptional repression of E2F-responsive genes. Three transcript variants encoding different isoforms have been found for this gene.
histone-binding protein RBBP4
, nucleosome-remodeling factor subunit RBAP48
, retinoblastoma-binding protein 4
, histone-binding protein RBBP4-A
, retinoblastoma A associated protein
, retinoblastoma-binding protein 4-A
, retinoblastoma-binding protein p48-A
, chromatin assembly Factor-1
, chromatin assembly factor 1
, chromatin assembly factor 1 subunit
, chromatin associated factor-1 subunit
, nucleosome remodeling factor
, nucleosome remodeling factor - 55kD
, retinoblastoma binding protein 4
, CAF-1 subunit C
, CAF-I 48 kDa subunit
, CAF-I p48
, MSI1 protein homolog
, chromatin assembly factor 1 subunit C
, chromatin assembly factor I p48 subunit
, chromatin assembly factor/CAF-1 p48 subunit
, retinoblastoma-binding protein p48
, CAF-1 p48 subunit
, chCAF-1 p48
, chromatin assembly factor 1 p48 subunit