ArticleEpigenetics & chromatin2025
ZAD mediates chromatin binding and insulator activity of Drosophila Pita and can be replaced with the human ZFP276 ZAD-like domain.
Article in Epigenetics & chromatin, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Cooperation between architectural C2H2 proteins in CP190 recruitment to Drosophila regulatory elements.Epigenetics & chromatin · 2025Article
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Abstract
backgroundThe zinc finger-associated domain (ZAD), found in numerous Drosophila architectural proteins, such as Pita, enables homodimerization. Despite its prevalence in insects, only one human protein, ZFP276, possesses a ZAD-like domain. To date, the role of Pita has been studied in the formation of the boundaries of regulatory domains in the Bithorax complex, and the functional significance of its ZAD remains unclear.
resultsUsing CRISPR/Cas9-mediated pita replacement with an attP site, we generated flies expressing modified Pita variants. Null pita mutants die in the late stages of embryogenesis. Flies expressing Pita lacking ZAD, Pita
conclusionsZAD is critical for the insulator activity of Pita and its ability to efficiently bind to specific genomic regions. The human ZFP276 ZAD-like domain may function similarly to the ZAD of Pita, raising the question of why ZADs spread in insects but not in mammals.
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