ArticleDoklady. Biochemistry and biophysics2021
The BEAF-32 Protein Directly Interacts with Z4/putzig and Chriz/Chromator Proteins in Drosophila melanogaster.
Article in Doklady. Biochemistry and biophysics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Cooperation between architectural C2H2 proteins in CP190 recruitment to Drosophila regulatory elements.Epigenetics & chromatin · 2025Article
- 3D chromatin structures precede genome activation in Drosophila embryogenesis.Cell genomics · 2025Article
- Characterization of core promoter activation by the Drosophila insulator-binding protein BEAF.Scientific reports · 2025Article
- Insulator BEAF32 regulates expression of tissue-specific genes and piRNA source loci in Drosophila ovaries.Epigenetics & chromatin · 2025Article
- Drosophila Protein Z4 Possesses ZAD Dimerization Domain.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections · 2024Article
- Proximity labeling reveals a new in vivo network of interactors for the histone demethylase KDM5.Epigenetics & chromatin · 2023Article
- Mechanisms of Interaction between Enhancers and Promoters in ThreeInternational journal of molecular sciences · 2023Review
- Mechanisms of enhancer-promoter communication and chromosomal architecture in mammals andFrontiers in genetics · 2022Review
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Authors and funding
5 authors.
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Abstract
In Drosophila, the BEAF-32, Z4/putzig, and Chriz/Chromator proteins colocalize in the interbands of polytene chromosomes. It was assumed that these proteins can form a complex that affects the structure of chromatin. However, the mechanism of the formation of such a complex has not been studied. We have proved for the first time that the BEAF-32, Z4/putzig, and Chriz/Chromator proteins interact directly with each other and localized the protein domains that provide multiple protein-protein interactions. Based on the data obtained, we developed a model of the mechanism of the formation the BEAF/Z4/Chriz complex and its recruitment to chromatin.
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