ChIP-Seq in Saccaromyces cerevisiae via Sin3-(3xHA)
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ABSTRACT:
ORGANISM(S): Saccharomyces cerevisiae
PROVIDER: GSE211772 | GEO | 2025/08/22
REPOSITORIES: GEO
Similar Datasets
Project description:As part of a larger study identifying novel HDAC complex inhibitors, WT cells were treated with DMSO, 20 μM TSA or 50 μM E6R to investigate changes in gene expression levels. Also, cultures of rpd3Δ and sin3Δ mutant strains treated with DMSO were investigated.
2025-08-22 | GSE211775 | GEO
Project description:As part of a larger study identifying novel HDAC complex inhibitors, cells were treated with 0.8% DMSO, 1 μM TSA, or 25 μM E6R to investigate changes in gene expression levels.
2025-08-22 | GSE211773 | GEO
Project description:The Sin3/HDAC complex is highly conserved from yeast to humans. Sin3 provides the scaffolding needed to coordinate DNA binding proteins with various chromatin modifying enzymes, most often histone deacetylases, to establish chromatin environments important both for correct gene regulation and genome stability (reviewed in [1]). Three Sin3 homologs are present. Here we explore Pst3, the most ancient of the Sin3 molecules, in Schizosaccharomyces pombe. In contrast to Pst1 [2] and Pst2 [3], Pst3 occupies the entire nuclear space, including the nucleolus. The deletion of pst3+ causes general genome instability including chomosome mis-segregation, gross sporulation defects, rampant anneuploidy, and distended nucleoli. Genome-wide expression analysis indicated a role in both gene repression and gene activation. Interestingly, highly expressed genes encoding ribosomal and nucleolar proteins were positively regulated by Pst3. Genome wide binding analysis for Pst3-GFP indicated that Pst3 is bound both to intergenic and coding regions, and could be correlated with expression data. Proteins previously identified as part of the Clr6/Pst2 complex co-immunopercipitated with Pst3-TAP. Additionally, Snf59, the kinase Ssp1, and the Dead-Box helicase Dbp10 were identified as Pst3 interaction partners. Taken together this data suggests that Pst3 has a direct role in the structure and function of the nucleolus. Keywords: Expression profiling Expression profiling experiments were performed and quantified according to (Xue et al., 2004).
2010-05-16 | E-GEOD-7133 | biostudies-arrayexpress
Project description:The Sin3/HDAC complex is highly conserved from yeast to humans. Sin3 provides the scaffolding needed to coordinate DNA binding proteins with various chromatin modifying enzymes, most often histone deacetylases, to establish chromatin environments important both for correct gene regulation and genome stability (reviewed in [1]). Three Sin3 homologs are present. Here we explore Pst3, the most ancient of the Sin3 molecules, in Schizosaccharomyces pombe. In contrast to Pst1 [2] and Pst2 [3], Pst3 occupies the entire nuclear space, including the nucleolus. The deletion of pst3+ causes general genome instability including chomosome mis-segregation, gross sporulation defects, rampant anneuploidy, and distended nucleoli. Genome-wide expression analysis indicated a role in both gene repression and gene activation. Interestingly, highly expressed genes encoding ribosomal and nucleolar proteins were positively regulated by Pst3. Genome wide binding analysis for Pst3-GFP indicated that Pst3 is bound both to intergenic and coding regions, and could be correlated with expression data. Proteins previously identified as part of the Clr6/Pst2 complex co-immunopercipitated with Pst3-TAP. Additionally, Snf59, the kinase Ssp1, and the Dead-Box helicase Dbp10 were identified as Pst3 interaction partners. Taken together this data suggests that Pst3 has a direct role in the structure and function of the nucleolus. Keywords: Expression profiling
2008-11-14 | GSE7133 | GEO
Project description:SIN3 associates with RPD3 and other accessory proteins to form the SIN3 histone modifying complex. A single Sin3A gene encodes multiple SIN3 isoforms, of which SIN3 187 and SIN3 220 are predominant. Previous studies from our laboratory and others have indicated that SIN3 isoforms play non-redundant roles during fly development, however, the genes regulated by SIN3 isoforms are not known. We mapped the genome-wide binding sites of SIN3 isoforms in Drosophila. We established stable S2 cell lines that express either HA-tagged SIN3 187 or SIN3 220. The binding profiles revealed that the majority of the binding sites of SIN3 isoforms are overlapping. Our data revealed that SIN3 isoforms localize to euchromatic regions of the genome and enrichment of SIN3 isoforms are generally concentrated around the transcription start sites of genes. In addition, the extent of SIN3 binding confirmed previous findings indicating that SIN3 is a global transcriptional regulator.
2016-01-09 | GSE72171 | GEO
Project description:SIN3 associates with RPD3 and other accessory proteins to form the SIN3 histone modifying complex. A single Sin3A gene encodes multiple SIN3 isoforms, of which SIN3 187 and SIN3 220 are predominant. Previous studies from our laboratory and others have indicated that SIN3 isoforms play non-redundant roles during fly development, however, the genes regulated by SIN3 isoforms are not known. We mapped the genome-wide binding sites of SIN3 isoforms in Drosophila. We established stable S2 cell lines that express either HA-tagged SIN3 187 or SIN3 220. The binding profiles revealed that the majority of the binding sites of SIN3 isoforms are overlapping. Our data revealed that SIN3 isoforms localize to euchromatic regions of the genome and enrichment of SIN3 isoforms are generally concentrated around the transcription start sites of genes. In addition, the extent of SIN3 binding confirmed previous findings indicating that SIN3 is a global transcriptional regulator. Genome-wide binding analysis of SIN3 187 and SIN3 220 in Drosophila. Using chromatin prepared from cell lines expressing either of the isoforms, we performed chromatin immunoprecipitation on chromatin prepared from cells that expresses either of the isoforms using an antibody against HA (ChIP). We coupled our ChIP with high resolution deep sequencing (ChIP-seq) to identify genomic targets of SIN3 isoforms.
2016-01-09 | E-GEOD-72171 | biostudies-arrayexpress
Project description:SIN3 is a master transcriptional scaffold protein. SIN3 interacts with RPD3 and other accessory proteins to form a histone modifying complex. A single Sin3A gene encodes multiple isoforms of SIN3, of which SIN3 187 and SIN3 220 are the predominant isoforms. Previous studies demonstrated that SIN3 isoforms play non-redundant roles during fly development. In the current study, we sought to investigate the genes regulated by SIN3 187.
2016-01-09 | GSE72172 | GEO
Project description:The multi-subunit Sin3 co-repressor complex regulates gene transcription through deacetylation of nucleosomes. However, the full range of Sin3 activities and targets is not well understood. Here, we have investigated genome-wide binding of mouse Sin3 and RBP2 as well as histone modifications and nucleosome positioning as a function of myogenic differentiation. Remarkably, we find that Sin3 complexes spread immediately downstream of the transcription start site on repressed and transcribed genes during differentiation. We show that RBP2 is part of a Sin3 complex, and on a subset of E2F4 target genes, the coordinated activity of Sin3 and RBP2 leads to deacetylation, demethylation, and repositioning of nucleosomes. Our work provides evidence for coordinated binding of Sin3, chromatin modifications, and chromatin remodeling within discrete regulatory regions, suggesting a model in which spreading of Sin3 binding is ultimately linked to permanent gene silencing on a subset of E2F4 target genes.
2008-11-06 | GSE13247 | GEO
Project description:SIN3 is a master transcriptional scaffold protein. SIN3 interacts with RPD3 and other accessory proteins to form a histone modifying complex. A single Sin3A gene encodes multiple isoforms of SIN3, of which SIN3 187 and SIN3 220 are the predominant isoforms. Previous studies demonstrated that SIN3 isoforms play non-redundant roles during fly development. In the current study, we sought to investigate the genes regulated by SIN3 187. S2 cells and cells carrying a stable transgene of SIN3 187HA (SIN3 187HA cells) were treated with 0.07 µM CuSO4. CuSO4 treatment led to ectopic expression of SIN3 187HA. S2 cells were used as a control. Following induction, total mRNA was extracted. mRNA profiling of these samples were performed by deep sequencing using Illumina Hiseq2500. Three biological replicates were performed.
2016-01-09 | E-GEOD-72172 | biostudies-arrayexpress
Project description:The Sin3 histone deacetylase (HDAC) complex is a 1.2 MDa chromatin modifying complex that can repress transcription by binding to gene promoters and deacetylating histones. The Sin3/HDAC complex can affect cell cycle progression through multiple mechanisms and is among the targets of anticancer drugs, called HDAC inhibitors. We describe the identification of a new subunit of the Sin3 complex named family with sequence similarity 60 member A (FAM60A). We show that FAM60A/Sin3 complexes normally suppress the epithelial-to-mesenchymal transition (EMT) and cell migration. This occurs through transcriptional repression of genes that encode components of the TGF-beta signaling pathway. This work reveals that FAM60A and the Sin3 complex are upstream repressors of TGF-beta signaling, EMT and cell migration and extends the known biological roles of the Sin3 complex. This experiment investigates the role of FAM60A in gene expression by comparing A549 lung cancer cells treated with or without siRNA against FAM60A. The Sin3 histone deacetylase (HDAC) complex is a 1.2 MDa chromatin modifying complex that can repress transcription by binding to gene promoters and deacetylating histones. SDS3 is a core component of the Sin3 complex. The Sin3/HDAC complex can affect cell cycle progression through multiple mechanisms and is among the targets of anticancer drugs, called HDAC inhibitors. We describe the identification of a new subunit of the Sin3 complex named family with sequence similarity 60 member A (FAM60A). We show that FAM60A/Sin3 complexes normally suppress the epithelial-to-mesenchymal transition (EMT) and cell migration. This occurs through transcriptional repression of genes that encode components of the TGF-beta signaling pathway. This work reveals that FAM60A and the Sin3 complex are upstream repressors of TGF-beta signaling, EMT and cell migration and extends the known biological roles of the Sin3 complex. As a base line to better understand the relationship between FAM60A and the Sin3 complex, this experiment investigates the gene expression changes which occur in A549 lung cancer cells when the Sin3 complex is perturbed by knockdown of a core component via siRNA against SDS3. FAM60A siRNA knockdowns were compared to a non-targeting control in triplicate, for a total of 6 samples. SDS3 siRNA knockdowns were compared to a non-targeting control in triplicate, for a total of 6 samples.
2012-09-15 | E-GEOD-39733 | biostudies-arrayexpress