Drosophila melanogaster
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA236229 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR1141010.fastq.gz | Fastqsanger.gz | |||
| SRR1141008.fastq.gz | Fastqsanger.gz | |||
| SRR1141009.fastq.gz | Fastqsanger.gz |
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Project description:Insulators are multiprotein–DNA complexes that regulate nuclear architecture. The Drosophila CP190 protein is a common cofactor of two main insulator complexes formed by the DNA-binding proteins Su(Hw) and dCTCF. Here, we have identified two new DNA-binding proteins, Pita and ZIPIC, that interact with CP190. In vitro, CP190 interacts with Pita through the BTB domain and with ZIPIC through the centrosomal targeting domain. The artificial binding sites for Pita or ZIPIC partially block enhancers and protect gene expression from PRE-mediated silencing in transgenic lines. Pita binds adjacent to dCTCF in the well-studied Mcp insulator and is required for its activity, which indicates that two insulator proteins can cooperate in organizing a functional insulator. Pita and ZIPIC preferentially bind to the promoter regions and extensively colocalize with dCTCF and BEAF. These results suggest that insulator proteins can fulfill multiple functions in chromosome architecture and gene expression.
2014-10-01 | GSE54337 | GEO
Project description:Genome-wide distribution of proteins Pita, ZIPIC, Zw5 in Drosophila embryos
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Project description:Genome-wide binding profiles of Drosophila melanogaster insulator proteins in Kc and Mbn2 cells
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Project description:This SuperSeries is composed of the following subset Series: GSE15660: Gene Expression analysis of Kc and Mbn2 cell lines from Drosophila melanogaster. GSE15661: Genome-wide binding profiles of Drosophila melanogaster insulator proteins in Kc and Mbn2 cells (Set1) GSE15662: Genome-wide binding profiles of Drosophila melanogaster insulator proteins in Kc and Mbn2 cells (Set2) GSE15663: Genome-wide binding profiles of Drosophila melanogaster insulator proteins in Kc and Mbn2 cells (Set3) Refer to individual Series
2010-05-19 | E-GEOD-15664 | biostudies-arrayexpress
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.
2020-11-30 | GSE160007 | GEO
Project description:Analysis of genome-wide binding of the insulator factors CTCF and CP190
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Project description:Drosophila Pita belongs to large group of architectural proteins that have C-terminal cluster of C2H2-type zinc-finger domains and N-terminal zinc finger-associated domain (ZAD) that can homodimerize. Despite widespread distribution of ZADs in insects, only one human protein, Zinc-finger protein 276 (ZFP276), has a ZAD-like domain. The functional role of Pita has been studied so far only in the formation of the boundaries of regulatory domains in Bithorax complex. Here we tested the role of ZAD in the functional activity of the Pita protein. Using CRISPR/Cas9, we replaced the promoter region of the pita gene with attP, allowing expression of modified protein variants. Pita null mutants die at a late embryonic stage, whereas flies expressing a Pita mutant lacking ZAD, PitaΔZ, show reduced viability. ChIP-seq studies showed that PitaΔZ effectively binds to promoters of housekeeping genes and insulators in cooperation with other known architectural C2H2 proteins and CP190. However, ZAD is required for the binding of Pita to a subset of chromatin regions and its function as an insulator protein. The ZAD-like domain from human ZFP276 can almost completely compensate for the ZAD functions in the Pita protein. The results directly demonstrate that ZAD is required for insulator activity of Pita and its ability to efficiently bind to specific genomic regions. The ZAD-like domain of human ZFP276 may function similarly to the ZAD of Pita, raising the question of why ZADs have not spread to mammalian C2H2 proteins as they have to most insects.
2025-12-09 | GSE300416 | GEO
Project description:Ibf1 and Ibf2 are DNA-binding proteins required for insulator function in Drosophila [ChIP-seq]
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Project description:Distribution of Drosophila insulator proteins during interphase and mitosis
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Project description:According to recent models, as yet poorly studied architectural proteins appear to be required for local regulation of enhancer–promoter interactions, as well as for global chromosome organization. Transcription factors ZIPIC, Pita, and Zw5 belong to the class of chromatin insulator proteins and preferentially bind to promoters near the TSS. They are structurally similar in containing the N-terminal zinc finger-associated domain (ZAD) and different numbers of C2H2-type zinc fingers at the C-terminus. We have shown that the ZAD domains of ZIPIC, Pita, and Zw5 usually form homodimers. In Drosophila transgenic lines, these proteins can support long-distance interaction between GAL4 activator and the reporter gene promoter. However, no functional interaction between binding sites for different proteins has been revealed, suggesting that such interactions are highly specific. ZIPIC facilitates long-distance stimulation of reporter gene by GAL4 activator in yeast. Thus, ZAD-containing zinc-finger proteins probably belong to the class of architectural proteins.
2016-05-06 | GSE76997 | GEO