ArticleNucleic acids research2021
Structural basis of diversity and homodimerization specificity of zinc-finger-associated domains in Drosophila.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Shared binding sites for the chromosomal architectural protein Su(Hw) mediate physical interactions betweenbioRxiv : the preprint server for biology · 2026Article
- Decoding the molecular logic of rapidly evolving ZAD zinc finger proteins inScience advances · 2026Article
- Beyond DNA binding: single C2H2 zinc fingers with adjacent β-strands mediate dimerization in Drosophila transcription factors.Nucleic acids research · 2026Article
- Cooperation between architectural C2H2 proteins in CP190 recruitment to Drosophila regulatory elements.Epigenetics & chromatin · 2025Article
- ZAD mediates chromatin binding and insulator activity of Drosophila Pita and can be replaced with the human ZFP276 ZAD-like domain.Epigenetics & chromatin · 2025Article
- Ecdysone signaling-induced dumpless1 expression controls nurse cell dumping in Drosophila oogenesis.Nature communications · 2025Article
- The homie insulator has sub-elements with different insulating and long-range pairing properties.Genetics · 2025Article
- Drosophila architectural proteins M1BP and Opbp cooperatively form the active promoter of a ribosomal protein gene.Epigenetics & chromatin · 2025Article
- ThebioRxiv : the preprint server for biology · 2025Article
- Drosophila Protein Z4 Possesses ZAD Dimerization Domain.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections · 2024Article
- Chromosome structure ineLife · 2024Article
- New Drosophila promoter-associated architectural protein Mzfp1 interacts with CP190 and is required for housekeeping gene expression and insulator activity.Nucleic acids research · 2024Article
- The N-terminal dimerization domains of human and Drosophila CTCF have similar functionality.Epigenetics & chromatin · 2024Article
- Study of the Association of Ouib and Nom with Heterochromatin in Drosophila melanogaster.Doklady. Biochemistry and biophysics · 2023Article
- Article
- Mechanisms of Interaction between Enhancers and Promoters in ThreeInternational journal of molecular sciences · 2023Review
- Safeguarding Drosophila female germ cell identity depends on an H3K9me3 mini domain guided by a ZAD zinc finger protein.PLoS genetics · 2022Article
- TheeLife · 2022Article
- Dimerization Activity of a Disordered N-Terminal Domain fromInternational journal of molecular sciences · 2022Article
- Structures and biological functions of zinc finger proteins and their roles in hepatocellular carcinoma.Biomarker research · 2022Review
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8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In arthropods, zinc finger-associated domains (ZADs) are found at the N-termini of many DNA-binding proteins with tandem arrays of Cys2-His2 zinc fingers (ZAD-C2H2 proteins). ZAD-C2H2 proteins undergo fast evolutionary lineage-specific expansion and functional diversification. Here, we show that all ZADs from Drosophila melanogaster form homodimers, but only certain ZADs with high homology can also heterodimerize. CG2712, for example, is unable to heterodimerize with its paralog, the previously characterized insulator protein Zw5, with which it shares 46% homology. We obtained a crystal structure of CG2712 protein's ZAD domain that, in spite of a low sequence homology, has similar spatial organization with the only known ZAD structure (from Grauzone protein). Steric clashes prevented the formation of heterodimers between Grauzone and CG2712 ZADs. Using detailed structural analysis, site-directed mutagenesis, and molecular dynamics simulations, we demonstrated that rapid evolutionary acquisition of interaction specificity was mediated by the more energy-favorable formation of homodimers in comparison to heterodimers, and that this specificity was achieved by multiple amino acid substitutions resulting in the formation or breaking of stabilizing interactions. We speculate that specific homodimerization of ZAD-C2H2 proteins is important for their architectural role in genome organization.
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