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The present study demonstrated that H2A.Z is overexpressed in ICC and expression of H2A.Z correlated with poor prognosis in patients with ICC. H2A.Z regulated cell proliferation in vitro and in vivo via H2A.Z/S-phase kinase-associated protein 2/p27 (show PAK2 Proteins)/p21 (show CDKN1A Proteins) signaling.
study identifies GAS41 as a histone acetylation reader that promotes histone H2A.Z deposition in non-small cell lung cancer.
Two possible modes of pioneering associated with combinations of H2A.Z and p300/CBP (show CREBBP Proteins) at nucleosome-occupied enhancers.
Results indicate that accumulation of H2A.Z within repressed genes can also be a consequence of the repression of gene transcription rather than an active mechanism required to establish the repression.
Findings suggest the oncogenic potential of H2A.Z.1 in liver tumorigenesis and that it plays established role in accelerating cell cycle transition and EMT (show ITK Proteins) during hepatocarcinogenesis.
Crystal structure results show that the flexible character of the H2A.Z L1 loop plays an essential role in forming the stable heterotypic H2A.Z/H2A nucleosome.
Monoubiquitination of histone H2B blocks eviction of histone variant H2A.Z from inducible enhancers.
Thus, PWWP2A is a novel H2A.Z-specific multivalent chromatin binder providing a surprising link between H2A.Z, chromosome segregation, and organ development.
SMYD3 (show SMYD3 Proteins)-mediated H2A.Z.1K101 dimethylation activates cyclin A1 (show CCNA1 Proteins) expression and contributes to driving the proliferation of breast cancer cells.
Results suggest that the N-terminal tail of H2A.Z makes distinctively different contributions to epigenetic events.
The data also suggest that H2A.Z restricts transcription, which is moderated by ANP32e (show ANP32E Proteins) at the promoter and gene bodies of expressed genes. Thus, ANP32e (show ANP32E Proteins), through inhibition of PP2A (show PPP2R2B Proteins), is required for nucleosomal inclusion of H2A.Z and the regulation of gene expression
In contrast to H2A-interacting proteins, the H2A.Z-interacting proteins are involved in transcriptional regulation. We found that the transcription factor Osr1 (show OSR1 Proteins) interacts with H2A.Z both in vitro and in vivo. It also mediates H2A.Z incorporation to a large number of target sites and regulates gene expression
This study reveals an antagonistic relationship between H2A.Z.1ub and BRD2 (show BRD2 Proteins) to regulate the transcriptional balance at bivalent genes to enable proper execution of developmental programs.
Embryonic stem cell BAF (show BANF1 Proteins) is required for normal H2A.Z localization in these cells, suggesting BAF (show BANF1 Proteins) either stabilizes H2A.Z containing nucleosomes or promotes subnucleosome to nucleosome conversion by facilitating H2A.Z deposition.
Study mapped H2A.Z genome-wide in embryonic stem cells and neural progenitors; H2A.Z is deposited at promoters and enhancers, and correlates strongly with H3K4 methylation. H2A.Z is present at poised promoters with bivalent chromatin and at active promoters with H3K4 methylation, but is absent from stably repressed promoters that are enriched for H3K27 trimethylation.
our work suggests that the divergent residues in the H2A.Z acidic patch comprise a unique domain that couples control of chromatin dynamics to the regulation of developmental gene expression patterns during lineage commitment.
Data propose that H2A.Z mediates such contrasting activities by acting as a general facilitator that generates access for a variety of complexes, both activating and repressive.
The variant histone H2A.Z and the winged helix transcription factor (show FOXC1 Proteins) Foxa2 (show FOXA2 Proteins) both act to regulate nucleosome depletion and gene activation, thus promoting embryonic stem cell differentiation, whereas DNA methylation (show HELLS Proteins) promotes nucleosome occupation and suppresses gene expression.
incorporation of the histone variant H2A.Z at the promoter regions of PPARgamma (show PPARG Proteins) target genes by p400 (show ITPR1 Proteins)/Brd8 (show BRD8 Proteins) is essential to allow fat cell differentiation
In mouse trophoblast stem cells, the amount of histone H2A.Z at promoters decreased during S phase, coinciding with homotypic (H2A.Z-H2A.Z) nucleosomes flanking the TSS (show RPL38 Proteins) becoming heterotypic (H2A.Z-H2A).
Depletion of H2A.Z by RNA interference perturbs Xenopus laevis development at gastrulation leading to embryos with malformed, shortened trunks.
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene encodes a replication-independent member of the histone H2A family that is distinct from other members of the family. Studies in mice have shown that this particular histone is required for embryonic development and indicate that lack of functional histone H2A leads to embryonic lethality.
, histone H2A.Z
, H2A histone family, member Z
, H2A histone family member V
, H2A histone family, member V
, histone H2A.V
, histone H2A.Z-like
, histone H2A.Zl2
, histone H2AF