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Polymerization of BTB transcription factors regulates chromatin occupancy [ChIP-Seq]

ABSTRACT: Polymerization of BTB transcription factors regulates chromatin occupancy [ChIP-Seq]

PROVIDER: PRJNA1055065 | ENA |

REPOSITORIES: ENA

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Polymerization of BTB transcription factors regulates chromatin occupancy

Project description:Polymerization of BTB transcription factors regulates chromatin occupancy

| PRJNA1055064 | ENA

Polymerization of BTB transcription factors regulates chromatin occupancy [RNA-Seq]

Project description:Polymerization of BTB transcription factors regulates chromatin occupancy [RNA-Seq]

| PRJNA1054993 | ENA

Polymerization of BTB transcription factors regulates chromatin occupancy [ChIP-Seq]

Project description:The broad-complex, tramtrack and bric-à-brac (BTB) family of transcription factors (TFs) serve as important regulators of hematopoietic development. The BTB domains of these TFs mediate co-repressor recruitment and dimerization, but their propensity to self-assemble into higher-order structures has not been established. Here, we survey 189 human BTB proteins and identify 18 BTB TFs that form punctate nuclear foci. We demonstrate that these foci-forming BTB TFs polymerize into filaments and present the cryo-EM structures of ZBTB5BTB and ZBTB9BTB filaments. Finally, we find that polymerization in BTB TFs enhances chromatin occupancy within regions containing homotypic clusters of TF binding sites. This increased chromatin occupancy in turn leads to the repression of target genes. Taken together, our results reveal a novel mechanism to regulate BTB TFs, and suggest an underappreciated role for polymerization in regulating TF function.

2024-07-11 | GSE251687 | GEO

Polymerization of BTB transcription factors regulates chromatin occupancy [RNA-Seq]

2024-07-11 | GSE251638 | GEO

Polymerization of BTB transcription factors regulates chromatin occupancy

Project description:This SuperSeries is composed of the SubSeries listed below.

2024-07-11 | GSE251688 | GEO

Small molecule-induced polymerization triggers degradation of BCL6

Project description:Most small-molecule protein degraders act as interface stabilizers ‘molecular glues’ between E3 ubiquitin ligases and target proteins to induce ternary complex formation and ubiquitin-dependent target protein degradation. Here we report polymerization as a novel mechanism for small molecule-induced degradation. Using functional screens in combination with molecular and biochemical assays, we found that BI-3802, which binds to the BTB domain of the oncogenic transcription factor BCL6, induces polymerization of BCL6 into regular helical structures in vitro and foci in vivo. Polymerization precedes degradation by the SIAH1 E3 ubiquitin ligase. Hereby, a VxP amino acid motif on BCL6, distal from the drug-binding BTB domain, is required for SIAH1 binding, ubiquitination and BI-3802-induced degradation. Our findings propose that small molecule-induced polymerization is not only a new modality for targeted protein degradation, but also provides synthetic biology with a tool for tunable protein polymerization and opens new avenues for future drug design.

2020-11-20 | PXD016185 | Pride

Chd1 co-occupancy with early transcription elongation factors

Project description:We report the genome-wide Chd1 co-occupancy with early transcription elongation factors

2014-10-23 | GSE56061 | GEO

Chd1 co-occupancy with early transcription elongation factors

Project description:We report the genome-wide Chd1 co-occupancy with early transcription elongation factors ChIP-seq for Chd1 and elongating RNA polymerase II

2014-10-23 | E-GEOD-56061 | biostudies-arrayexpress

Alterations in Mycobacterium tuberculosis transcriptome at the site of infection in BTB tuberculosis

Project description:In-vivo transcriptome analysis was performed to understand the Mtb adaptation strategies to survive in the host and establish infection in BTB. Gene expression profiling of Mtb within abscesses or necrotic specimens obtained from patients with BTB TB compared to exponentially growing in-vitro Mtb culture using whole genome microarray was studied.

2022-01-25 | GSE165232 | GEO

SAM domain polymerization links subnuclear clustering of PRC1 to silencing

Project description:Polycomb group (PcG) proteins mediate heritable but reversible silencing of developmental regulator genes by modifying their chromatin configuration. Accumulating evidence documents a role for PcG proteins in regulating higher order chromatin structures likely by their clustering, however, underlying mechanisms and its impact on transcriptional regulation remain obscure. In this study, we found that subnuclear clustering of PRC1 at canonical PcG target genes depended on head-to-tail polymerization property of SAM domain of Phc2 and likely Phc1. We show that Phc2-SAM polymerization limits the dynamic nature of PRC1, thereby promotes stable association of PRC1 with PcG target genes and contributes to their robust silencing. Our findings suggest a novel model by which SAM polymerization of Phc2 modulates the structural organization of PcG complexes to enable robust yet reversible PcG-mediated repression during development.

2013-06-01 | GSE37530 | GEO

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