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The role of Su(Hw) in recruiting the architectural protein Pita to chromatin

ABSTRACT: The architectural C2H2 proteins Pita and Su(Hw) significantly contribute to the formation of active promoters and insulators in Drosophila. At the majority of regulatory elements, these proteins bind and function independently of each other. We have shown that Pita and Su(Hw) can be present in the same complex in embryonic extract, yet they do not interact directly with each other. We identified 49 genomic sites where Pita binding is completely dependent on Su(Hw). These sites lack the co-localization with CP190, which typically binds to both Pita and Su(Hw). Such sites are also characterized by a strong, consensus-like motif for the Su(Hw) protein and, conversely, a relatively degenerate motif for Pita. The obtained results suggest a novel mechanism for recruiting the architectural protein Pita to regulatory elements through complex formation with Su(Hw), which determines chromatin binding.

ORGANISM(S): Drosophila melanogaster

PROVIDER: GSE312693 | GEO | 2026/09/01

REPOSITORIES: GEO

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The role of Su(Hw) in recruiting the architectural protein Pita to chromatin

Project description:The role of Su(Hw) in recruiting the architectural protein Pita to chromatin

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Cooperation between architectural C2H2 proteins in CP190 recruitment to Drosophila regulatory elements [RNA-Seq]

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Project description:The architectural protein Pita is critical for Drosophila embryogenesis and predominantly binds to gene promoters and insulators. In particular, Pita is involved in the organization of boundaries between regulatory domains, controlled by the expression of three hox genes in the Bithorax complex (BX-C). The best-characterized partner for Pita is the BTB/POZ-domain containing protein CP190. Here, we precisely mapped two unstructured regions of Pita that interact with the BTB domain of CP190. The deletion of the CP190-interacting regions did not significantly affect the binding of the mutant Pita protein to most chromatin sites. The expression of the mutant protein completely complemented the null pita mutation. However, the mutant Pita protein does not support the ability of multimerized Pita sites to prevent cross-talk between the iab-6 and iab-7 regulatory domains that activate the expression of Abdominal-B (Abd-B), one of the genes in the BX-C. The recruitment of the Pita region and the interaction with CP190 and the polytene chromosomes of larvae induces the formation of a new interband, which is a consequence of the formation of open chromatin in this region. These results suggested that the interaction with CP190 is required for the primary Pita activities, but other architectural proteins may also recruit CP190 in flies expressing only the mutant Pita protein.

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Su(Hw) interacts with Combgap to establish long-range chromatin contacts

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