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Chromatin Binding of Gcn5 in Drosophila is Largely Mediated by CP190 [RNA-seq]

ABSTRACT: 80% of the genomic binding sites of the histone acetyltransferase Gcn5 are colocalizing with CP190 binding. Depletion of CP190 reduces the number of Gcn5 binding sites and binding strength to chromatin. Binding dependency was further supported by Gcn5 mediated co-precipitation of CP190

ORGANISM(S): Drosophila melanogaster

PROVIDER: GSE83406 | GEO | 2016/12/05

SECONDARY ACCESSION(S): PRJNA325818

REPOSITORIES: GEO

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Chromatin Binding of Gcn5 in Drosophila is Largely Mediated by CP190 [ChIP-seq]

Project description:80% of the genomic binding sites of the histone acetyltransferase Gcn5 are colocalizing with CP190 binding. Depletion of CP190 reduces the number of Gcn5 binding sites and binding strength to chromatin. Binding dependency was further supported by Gcn5 mediated co-precipitation of CP190

2016-12-05 | GSE83408 | GEO

Chromatin Binding of Gcn5 in Drosophila is Largely Mediated by CP190

Project description:Chromatin Binding of Gcn5 in Drosophila is Largely Mediated by CP190

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Chromatin binding of Gcn5 in Drosophila is largely mediated by CP190.

Project description:Centrosomal 190 kDa protein (CP190) is a promoter binding factor, mediates long-range interactions in the context of enhancer-promoter contacts and in chromosomal domain formation. All Drosophila insulator proteins bind CP190 suggesting a crucial role in insulator function. CP190 has major effects on chromatin, such as depletion of nucleosomes, high nucleosomal turnover and prevention of heterochromatin expansion. Here, we searched for enzymes, which might be involved in CP190 mediated chromatin changes. Eighty percent of the genomic binding sites of the histone acetyltransferase Gcn5 are colocalizing with CP190 binding. Depletion of CP190 reduces Gcn5 binding to chromatin. Binding dependency was further supported by Gcn5 mediated co-precipitation of CP190. Gcn5 is known to activate transcription by histone acetylation. We used the dCas9 system to target CP190 or Gcn5 to a Polycomb repressed and H3K27me3 marked gene locus. Both, CP190 as well as Gcn5, activate this locus, thus supporting the model that CP190 recruits Gcn5 and thereby activates chromatin.

| S-EPMC5389606 | biostudies-literature

Identification of genome-wide binding sites of Plasmodium falciparum GCN5-acetyltransferase

Project description:Identification of genome-wide binding sites of Plasmodium falciparum GCN5-acetyltransferase

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GCN5 modulates salicylic acid homeostasis by regulating H3K14ac levels at the 5ʹ and 3ʹ ends of its target genes

Project description:The modification of histones by acetyl groups has a key role in the regulation of chromatin structure and transcription. The Arabidopsis thaliana histone acetyltransferase GCN5 regulates histone modifications as part of the Spt-Ada-Gcn5 Acetyltransferase (SAGA) transcriptional coactivator complex. GCN5 was previously shown to acetylate lysine 14 of histone 3 (H3K14ac) in the promoter regions of its target genes; however, its binding did not systematically correlate with gene activation and the mechanism by which GCN5 controls transcription thus remained unclear. To gain insight into GCN5 function, we fine-mapped its genome-wide binding sites and explored the effect of GCN5 loss-of-function on the expression of its target genes, finding that GCN5 has a dual role in the regulation of H3K14ac levels in their 5ʹ and 3ʹ ends. We found that the gcn5 mutation leads to a genome-wide reduction of H3K14ac in the 5ʹ end of some of the GCN5 targets, a phenomenon associated to their down-regulated in the gcn5 mutant. By contrast, an increase of H3K14ac in the 3ʹ end was observed in GCN5 targets that are up-regulated in the gcn5 mutant, indicating that this protein plays a dual role in the control of H3K14ac levels and in the regulation of transcription. Furthermore, changes in H3K14ac levels in the gcn5 mutant correlated with changes in H3K9ac in a genome-wide fashion at both 5ʹ and 3ʹ ends, providing evidence for a molecular link between the deposition of these two histone modifications. Finally, we show that GCN5 participates in responses to biotic stress by repressing salicylic acid (SA) accumulation and SA-mediated immunity, highlighting the role of this protein in the regulation of the crosstalk between diverse developmental and stress-responsive physiological programs.

2020-04-28 | GSE137474 | GEO

Analysis of genome-wide binding of the insulator factors CTCF and CP190

Project description:We identified about 3000 CTCF sites in the genome. In addition to binding to CTCF sites we found CP190 to bind to transcriptional start sites of actively transcribed genes where it inversely correlates with nucleosome occupancy. Keywords: ChIP-chip CTCF and CP190 ChIP. 2 biological replicates per experiment. dye-swaps as indicated in sample description.

2010-05-05 | E-GEOD-12749 | biostudies-arrayexpress

Analysis of genome-wide binding of the insulator factors CTCF and CP190

2009-02-21 | GSE12749 | GEO

Genome wide expression profile of ada1 and gcn5 deletion strains in Saccharomycescerevisiae

Project description:Ada1, Spt-Ada-Gcn5 Acetyltransferase (SAGA) complex component, was isolated as boundary factor that separated silenced chromatin and euchromatin by previous screening, and Ada1 maintains SAGA complex integrity. SAGA complex is one of a histone modification complex that has multiple functions contributing to transcriptional activation. In Saccharomyces cerevisiae, silencing is occurred by Sir protein complex, which deacetylates histones and form high-order chromatin structure. Gcn5, SAGA complex component, has histone acetyltransferase activity, which is considered that antagonize to silencing by the screening. Ada1 and Gcn5 might have different functions in SAGA complex, we performed microarray analysis to find different functions of gene regulations by using ada1Δ and gcn5Δ strains. As the results, Ada1-regulated genes include more than halves of Gcn5-regelated genes, which occupied only a part of Ada1 regulated genes. These suggest that the differences of contribution to SAGA functions. When SAGA complex have a loss of Ada1, almost function was lost. On the other hand, Gcn5 play a role only as acetyltransferase in SAGA complex.

2016-12-01 | GSE73998 | GEO

PALB2 acetylation by KAT2A/B (GCN5/PCAF) in vitro

Project description:PArtner and Localizer of BRCA2 (PALB2) is essential to maintain genome stability in human cells. Upon DNA damage by double DNA strand breaks, PALB2 is required to repair DNA by homologous recombination. In undamaged conditions, PALB2 protects coding regions, by preventing DNA stress due to collisions between transcription and replication machineries. PALB2 associates with chromatin, which is essential to fulfill its function in genome stability maintenance, however molecular mechanisms regulating PALB2 chromatin association remain unknown. In our previous published study describing the KAT2A/B(GCN5/PCAF)-acetylome (Fournier et al., Nat.Comm. 2016, doi: 10.1038/ncomms13227) we have identified PALB2 as an acetylated protein target of the acetyltransferases KAT2A (GCN5) and KAT2B (PCAF) in vivo. KAT2A/B-acetylated sites of PALB2 were mapped within its DNA/Chromatin association domain. In this current study, we have conducted in vitro acetyltransferase (AT) assays, by mixing purified recombinant GST-tagged PALB2 full-length (FL) and PALB2 fragment P2.2 which associates with DNA/chromatin (from residues 295-610), with Flag-PCAF, Flag-GCN5 and Flag-GCN5 catalytic mutant (mut), followed by proteomics analysis to map PALB2 acetylated lysines by KAT2A(GCN5) and KAT2B(PCAF) in vitro. PALB2 FL and P2.2 alone, or PALB2 FL and P2.2 mixed with GCN5 catalytic mutant, were used as negative controls.

2023-03-10 | PXD014681 | Pride

M1BP cooperates with CP190 to activate transcription at TAD borders and promote chromatin insulator activity

Project description:Genome organization is driven by forces affecting transcriptional state, but the relationship between transcription and genome architecture remains unclear. Here, we identified the Drosophila transcription factor Motif 1 Binding Protein (M1BP) in physical association with the gypsy chromatin insulator core complex, including the universal insulator protein CP190. M1BP is required for enhancer-blocking and barrier activities of the gypsy insulator as well as its proper nuclear localization. Genome-wide, M1BP specifically colocalizes with CP190 at Motif 1-containing promoters, which are enriched at topologically associating domain (TAD) borders. M1BP facilitates CP190 chromatin binding at many shared sites and vice versa. Both factors promote Motif 1-dependent gene expression and transcription near TAD borders genome-wide. Finally, loss of M1BP reduces chromatin accessibility and increases both inter- and intra-TAD local genome compaction. Our results reveal physical and functional interaction between CP190 and M1BP to activate transcription at TAD borders and mediate chromatin insulator-dependent genome organization.

2021-06-07 | PXD026497 | Pride

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