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Evolutionary Conservation and Functional Role of the SWI/SNF Complex Protein BDH in Arabidopsis: Insights into Catalytic Subcomplex Stability and Biological Implications [RNA-Seq]

ABSTRACT: The SWI/SNF complexes play crucial roles in chromatin remodeling, with the protein BDH emerging as a key component in Arabidopsis. Through evolutionary analysis, we demonstrate the conservation of BDH function across mammals, yeast, and plants. Our study reveals that BDH is integral to the stability of the catalytic subcomplex within SWI/SNF assemblies. Furthermore, we elucidate the biological and molecular implications of BDH in Arabidopsis, highlighting its involvement in nucleosomal occupancy regulation. Mutational characterization and transcriptomic analyses underscore BDH's significance, shedding light on its multifaceted role in chromatin dynamics and gene regulation.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE268511 | GEO | 2024/10/10

REPOSITORIES: GEO

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Evolutionary Conservation and Functional Role of the SWI/SNF Complex Protein BDH in Arabidopsis: Insights into Catalytic Subcomplex Stability and Biological Implications [ChIP-Seq]

Project description:The SWI/SNF complexes play crucial roles in chromatin remodeling, with the protein BDH emerging as a key component in Arabidopsis. Through evolutionary analysis, we demonstrate the conservation of BDH function across mammals, yeast, and plants. Our study reveals that BDH is integral to the stability of the catalytic subcomplex within SWI/SNF assemblies. Furthermore, we elucidate the biological and molecular implications of BDH in Arabidopsis, highlighting its involvement in nucleosomal occupancy regulation. Mutational characterization and transcriptomic analyses underscore BDH's significance, shedding light on its multifaceted role in chromatin dynamics and gene regulation.

2024-10-10 | GSE268510 | GEO

Evolutionary Conservation and Functional Role of the SWI/SNF Complex Protein BDH in Arabidopsis: Insights into Catalytic Subcomplex Stability and Biological Implications [RNA-Seq]

Project description:Evolutionary Conservation and Functional Role of the SWI/SNF Complex Protein BDH in Arabidopsis: Insights into Catalytic Subcomplex Stability and Biological Implications [RNA-Seq]

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Evolutionary Conservation and Functional Role of the SWI/SNF Complex Protein BDH in Arabidopsis: Insights into Catalytic Subcomplex Stability and Biological Implications [ChIP-Seq]

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The mSWI/SNF ATPase module mediates subcomplex identity and non-catalytic targeting in SCCOHT [ATAC-seq]

Project description:Perturbations to mammalian SWI/SNF (mSWI/SNF) chromatin remodeling complexes have been widely implicated as driving events across cancers1. One such perturbation is the dual loss of the SMARCA4 and SMARCA2 ATPase subunits, which has recently been implicated in rare cancers such as small cell carcinoma of the ovary, hypercalcemic type (SCCOHT)2-5, SMARCA4-deficient thoracic sarcomas6 and dedifferentiated endometrial carcinomas7. The consequences of SMARCA4/2 dual loss on the biochemical composition of the complex, chromatin targeting and remodeling capabilities, and subcomplex identity (BAF vs. PBAF) in these cancers are unknown. Here, we leverage SCCOHT cell lines to identify an unexpected ATPase module of mSWI/SNF subunits. Using biochemical and genome-wide profiling assays, we found that the incorporation of the ATPase module is a critical step in the functional specification of BAF and PBAF subcomplexes. Furthermore, by utilizing ATPase mutant variants, we found that the ATPase module mediates two separate and concurrent mSWI/SNF targeting mechanisms, evenly split between catalytically-independent targeting to primed enhancers/promoters and catalytically-dependent targeting to de novo enhancers. Finally, by linking these distinct sites to separate tumor-suppressive gene expression programs across ovarian tissues , we clarify the mechanistic consequences of SMARCA4/2 loss dual loss in these rare tumors.

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The mSWI/SNF ATPase module mediates subcomplex identity and non-catalytic targeting in SCCOHT [ChIP-seq]

2019-03-11 | GSE117734 | GEO

The mSWI/SNF ATPase module mediates subcomplex identity and non-catalytic targeting in SCCOHT [RNA-seq]

2019-03-11 | GSE117311 | GEO

The ATPase module of mammalian SWI/SNF family complexes mediates subcomplex identity and catalytic activity-independent genomic targeting

Project description:The ATPase module of mammalian SWI/SNF family complexes mediates subcomplex identity and catalytic activity-independent genomic targeting

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BRAHMA-containing chromatin remodelling complex prevailing in Arabidopsis vegetative organs is a homolog of mammalian non-canonical SWI/SNF complexes and requires BRD subunits for assembly and stability

Project description:The SWI/SNF family of chromatin remodeling complexes is evolutionarily conserved and present in yeast, animals and plants. While the biological functions of plant SWI/SNF complexes have been studied in detail, their composition is still elusive. To clarify this picture we used protein extracts from Arabidopsis plants in vegetative phase of growth to perform a series of immunoprecipitation followed by mass spectrometry experiments, using GFP-tagged BRM ATPase as a bait. The analysis of MS data showed that the dominant form of SWI/SNF complex present in these extracts has a specific subunit composition including ARP4 and 7, SWI3C, SWP73B and BRIP2, as well as three bromodomain containing subunits, BRD1, 2 and 13. This subunit composition and the lack of the core SWI/SNF subunit BSH (SNF5/INI1) both strongly resemble the characteristics of the specific subclass of mammalian SWI/SNF complexes referred to as non-canonical BAFs, indicating that homologues of these complexes also exist in plants. We next found that depletion of the all three BRDs severely affected the assembly of this form of BRM-associated SWI/SNF complex. However, while BRD1 and BRD2 were found sufficient to allow complex formation, BRD13 was only required under BRD1/2 deficiency. The analyses of IP/MS results using BRM-GFP in different brd mutant backgrounds as well as BRD1-GFP indicate that SWI/SNF assemblies containing only one BRD isoform, BRD1 or BRD2, do exist. Furthermore, our data indicate that BRD1/2 may be necessary for the incorporation of BRIP2 subunit into the complex. Together, our results shed new light on the structural and functional diversification of SWI/SNF complexes in Arabidopsis.

2023-04-03 | PXD030928 | Pride

SWI/SNF is positively auto-regulated by an AT-hook in the catalytic subunit

Project description:The SWI/SNF ATP-dependent chromatin remodeler is a master regulator of the epigenome; controlling pluripotency, cell fate determination and differentiation. There is a sparsity of information on the autoregulation of SWI/SNF, the domains involved and their mode of action. We find a DNA or RNA binding module conserved from yeast to humans located in the C-terminus of the catalytic subunit of SWI/SNF called the AT-hook that positively regulates the chromatin remodeling activity of yeast and mouse SWI/SNF. The AT-hook in yeast SWI/SNF interacts with the SnAC and ATPase domains, which after binding to nucleosome switches to contacting the N-terminus of histone H3. Deletion of the AT-hooks in yeast SWI/SNF and mouse esBAF complexes reduces the remodeling activity of SWI/SNF without affecting complex integrity or its recruitment to nucleosomes. In addition, deletion of the AT-hook impairs the ATPase and nucleosome mobilizing activities of yeast SWI/SNF without disrupting the interactions of the ATPase domain with nucleosomal DNA. The AT-hook is also important in vivo for SWI/SNF-dependent response to amino acid starvation in yeast and for cell lineage priming in mouse embryonic stem cells. In summary, the AT-hook is shown to be an evolutionarily conserved autoregulatory domain of SWI/SNF that positively regulates SWI/SNF both in vitro and in vivo.

2023-06-15 | PXD040664 | Pride

Organization, genomic targeting and assembly of three distinct SWI/SNF chromatin remodeling complexes in Arabidopsis [ChIP-seq]

Project description:Switch defective/sucrose non-fermentable (SWI/SNF) complexes are evolutionarily conserved multi-subunit machines that play vital roles in chromatin architecture regulation for modulating gene expression via sliding or ejection of nucleosomes in eukaryotes. In plants, perturbations of SWI/SNF subunits often result in severe developmental disorders. However, the subunit composition, pathways of assembly, and genomic targeting of the plant SWI/SNF complexes remain undefined. Here, we reveal that Arabidopsis SWI/SNF complexes exist in three distinct final form assemblies: BRM-associated SWI/SNF complexes (BAS), SYD-associated SWI/SNF complexes (SAS) and MINU-associated SWI/SNF complexes (MAS). We show that BAS complexes are equivalent to human ncBAF, whereas SAS and MAS complexes evolve in multiple subunits unique to plants, suggesting a plant-specific functional evolution of SWI/SNF complexes. We further demonstrate overlapping and specific genomic targeting of the three plant SWI/SNF complexes on chromatin and reveal that SAS complexes are necessary for the correct genomic localization of the BAS complexes. Finally, by focusing on the SAS and BAS complexes, we establish a requirement for both the core module subunit and the ATPase in the assembly of the plant SWI/SNF complexes. Together, our work highlights the divergence of SWI/SNF chromatin remodelers during the eukaryote evolution and provides a comprehensive landscape for understanding the plant SWI/SNF complexes organization, assembly, genomic targeting, and function.

2023-04-24 | GSE218841 | GEO

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