Loss of H2A.Z Is Not Sufficient to Determine Transcriptional Activity of Snf2-Related CBP Activator Protein or p400 Complexes

Bowman, Tamara A.; Wong, May Q.; Cox, Linda K.; Baldassare, Joseph J.; Chrivia, John C.

doi:10.1155/2011/715642

Cited by 9 publications

(11 citation statements)

References 32 publications

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“…However, loss of H2A.Z binding was not sufficient to stimulate p21 expression in MDA-MB231 cells. This observation correlates with previous studies showing that a 50% reduction H2A.Z association was not sufficient to induce changes in gene regulation [31].…”

Section: Discussionsupporting

confidence: 92%

Activation of p21 by HDAC Inhibitors Requires Acetylation of H2A.Z

et al. 2013

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Differential positioning of the histone variant H2A.Z in a p53 dependent manner was shown to regulate p21 transcription. Whether H2A.Z is involved in p21 activity in the absence of p53 is not known. The p21 gene is repressed in estrogen receptor (ER) negative cell lines that are p53−/− and hormone independent for their growth. Here we demonstrate that class I and II pan Histone deacetylase inhibitors (HDACi) induce p21 transcription and reduce cell proliferation of MDA-MB231, an ERα-negative mammary tumor cell line, in a H2A.Z dependent manner. H2A.Z is associated with the transcription start site (TSS) of the repressed p21 gene. Depleting H2A.Z did not lead to transcription of p21 but annihilated the stimulating effect of HDACi on this gene. Acetylation of H2A.Z but not of H3K9 at the p21 promoter correlated with p21 activation. We further show that HDACi treatment reduced the presence of the p400 chromatin remodeler at the p21 TSS. We propose a model in which association of p400 negatively affects p21 transcription by interfering with acetylation of H2A.Z.

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Section: Discussionsupporting

confidence: 92%

Activation of p21 by HDAC Inhibitors Requires Acetylation of H2A.Z

et al. 2013

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“…However, h2a.z;pie1 double mutants exhibit early developmental arrest not seen in either of the single mutant lines, indicating that H2A.Z may be deposited in the absence of the PIE1 complex, potentially by the Arabidopsis homolog of INO80 [76], which can deposit H2A.Z in yeast [51]. The PIE1 complex might also have H2A.Z-indpendent roles, as has been hypothesized for the PIE1/SWR1 orthologs in animals [49], [50]. Indeed, a recent study showed that H2A.Z deposition by p400 and SRCAP, the human orthologs of SWR1, could not account for all the regulatory roles of these complexes [50].…”

Section: Discussionmentioning

confidence: 88%

“…There is now considerable evidence that the PIE1 complex deposits H2A.Z into chromatin in Arabidopsis, though whether it has H2A.Z-independent functions, as has been shown for other eukaryotic SWR1 homologs, remains unclear [29], [49], [50]. Other Arabidopsis chromatin remodelers are probably also able to deposit H2A.Z, as does the yeast INO80 complex [51], because H2A.Z is incorporated into nucleosomes at low levels in pie1 and swr1 mutants [29], [34], [52].…”

Section: Introductionmentioning

confidence: 99%

Deposition of Histone Variant H2A.Z within Gene Bodies Regulates Responsive Genes

Coleman‐Derr¹,

2012

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The regulation of eukaryotic chromatin relies on interactions between many epigenetic factors, including histone modifications, DNA methylation, and the incorporation of histone variants. H2A.Z, one of the most conserved but enigmatic histone variants that is enriched at the transcriptional start sites of genes, has been implicated in a variety of chromosomal processes. Recently, we reported a genome-wide anticorrelation between H2A.Z and DNA methylation, an epigenetic hallmark of heterochromatin that has also been found in the bodies of active genes in plants and animals. Here, we investigate the basis of this anticorrelation using a novel h2a.z loss-of-function line in Arabidopsis thaliana. Through genome-wide bisulfite sequencing, we demonstrate that loss of H2A.Z in Arabidopsis has only a minor effect on the level or profile of DNA methylation in genes, and we propose that the global anticorrelation between DNA methylation and H2A.Z is primarily caused by the exclusion of H2A.Z from methylated DNA. RNA sequencing and genomic mapping of H2A.Z show that H2A.Z enrichment across gene bodies, rather than at the TSS, is correlated with lower transcription levels and higher measures of gene responsiveness. Loss of H2A.Z causes misregulation of many genes that are disproportionately associated with response to environmental and developmental stimuli. We propose that H2A.Z deposition in gene bodies promotes variability in levels and patterns of gene expression, and that a major function of genic DNA methylation is to exclude H2A.Z from constitutively expressed genes.

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“…Alternatively, scaffolding activities might partially explain some roles of chromatin remodelers, as suggested for SRCAP (Bowman et al, 2011). So far, our knowledge of the mechanisms of H2A.V incorporation has been anecdotal (Joyce et al, 2011;Kusch et al, 2014;Lu et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Splice variants of the SWR1-type nucleosome remodeling factor Domino have distinct functions during Drosophila melanogaster oogenesis

Börner

Becker

2016

Development

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SWR1-type nucleosome remodeling factors replace histone H2A by variants to endow chromatin locally with specialized functionality. In Drosophila melanogaster a single H2A variant, H2A.V, combines functions of mammalian H2A.Z and H2A.X in transcription regulation and the DNA damage response. A major role in H2A.V incorporation for the only SWR1-like enzyme in flies, Domino, is assumed but not well documented in vivo. It is also unclear whether the two alternatively spliced isoforms, DOM-A and DOM-B, have redundant or specialized functions. Loss of both DOM isoforms compromises oogenesis, causing female sterility. We systematically explored roles of the two DOM isoforms during oogenesis using a cell type-specific knockdown approach. Despite their ubiquitous expression, DOM-A and DOM-B have non-redundant functions in germline and soma for egg formation. We show that chromatin incorporation of H2A.V in germline and somatic cells depends on DOM-B, whereas global incorporation in endoreplicating germline nurse cells appears to be independent of DOM. By contrast, DOM-A promotes the removal of H2A.V from stage 5 nurse cells. Remarkably, therefore, the two DOM isoforms have distinct functions in cell type-specific development and H2A.V exchange.

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Loss of H2A.Z Is Not Sufficient to Determine Transcriptional Activity of Snf2-Related CBP Activator Protein or p400 Complexes

Cited by 9 publications

References 32 publications

Activation of p21 by HDAC Inhibitors Requires Acetylation of H2A.Z

Activation of p21 by HDAC Inhibitors Requires Acetylation of H2A.Z

Deposition of Histone Variant H2A.Z within Gene Bodies Regulates Responsive Genes

Splice variants of the SWR1-type nucleosome remodeling factor Domino have distinct functions during Drosophila melanogaster oogenesis

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