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Polymerization of BTB transcription factors regulates chromatin occupancy

ABSTRACT: Polymerization of BTB transcription factors regulates chromatin occupancy

PROVIDER: PRJNA1055064 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27295900_1.fastq.gz	Fastqsanger.gz
	SRR27295900_2.fastq.gz	Fastqsanger.gz
	SRR27295901_1.fastq.gz	Fastqsanger.gz
	SRR27295901_2.fastq.gz	Fastqsanger.gz
	SRR27295902_1.fastq.gz	Fastqsanger.gz

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

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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.

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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.

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