The N-Terminal Part of IDrosophila/I CP190 Is a Platform for Interaction with Multiple Architectural Proteins

• Published in: International journal of molecular sciences Vol. 24; no. 21
• Main Authors: Golovnin, Anton, Melnikova, Larisa, Babosha, Valentin, Pokholkova, Galina V, Slovohotov, Ivan, Umnova, Anastasia, Maksimenko, Oksana, Zhimulev, Igor F, Georgiev, Pavel
• Format: Journal Article
• Language: English
• Published: MDPI AG 01.11.2023
• Subjects: Chromatin; DNA binding proteins; Drosophila; Genetic engineering; Genetic transcription; Protein binding
• ISSN: 1422-0067; 1422-0067
• DOI: 10.3390/ijms242115917

CP190 is a co-factor in many Drosophila architectural proteins, being involved in the formation of active promoters and insulators. CP190 contains the N-terminal BTB/POZ (Broad-Complex, Tramtrack and Bric a brac/POxvirus and Zinc finger) domain and adjacent conserved regions involved in protein interactions. Here, we examined the functional roles of these domains of CP190 in vivo. The best-characterized architectural proteins with insulator functions, Pita, Su(Hw), and dCTCF, interacted predominantly with the BTB domain of CP190. Due to the difficulty of mutating the BTB domain, we obtained a transgenic line expressing a chimeric CP190 with the BTB domain of the human protein Kaiso. Another group of architectural proteins, M1BP, Opbp, and ZIPIC, interacted with one or both of the highly conserved regions in the N-terminal part of CP190. Transgenic lines of D. melanogaster expressing CP190 mutants with a deletion of each of these domains were obtained. The results showed that these mutant proteins only partially compensated for the functions of CP190, weakly binding to selective chromatin sites. Further analysis confirmed the essential role of these domains in recruitment to regulatory regions associated with architectural proteins. We also found that the N-terminal of CP190 was sufficient for recruiting Z4 and Chromator proteins and successfully achieving chromatin opening. Taken together, our results and the results of previous studies showed that the N-terminal region of CP190 is a platform for simultaneous interaction with various DNA-binding architectural proteins and transcription complexes.