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The N-Terminal Part of Drosophila CP190 Is a Platform for Interaction with Multiple Architectural Proteins
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 inte...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10648081/ https://www.ncbi.nlm.nih.gov/pubmed/37958900 http://dx.doi.org/10.3390/ijms242115917 |
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author | Golovnin, Anton Melnikova, Larisa Babosha, Valentin Pokholkova, Galina V. Slovohotov, Ivan Umnova, Anastasia Maksimenko, Oksana Zhimulev, Igor F. Georgiev, Pavel |
author_facet | Golovnin, Anton Melnikova, Larisa Babosha, Valentin Pokholkova, Galina V. Slovohotov, Ivan Umnova, Anastasia Maksimenko, Oksana Zhimulev, Igor F. Georgiev, Pavel |
author_sort | Golovnin, Anton |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-10648081 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-106480812023-11-02 The N-Terminal Part of Drosophila CP190 Is a Platform for Interaction with Multiple Architectural Proteins Golovnin, Anton Melnikova, Larisa Babosha, Valentin Pokholkova, Galina V. Slovohotov, Ivan Umnova, Anastasia Maksimenko, Oksana Zhimulev, Igor F. Georgiev, Pavel Int J Mol Sci Article 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. MDPI 2023-11-02 /pmc/articles/PMC10648081/ /pubmed/37958900 http://dx.doi.org/10.3390/ijms242115917 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Golovnin, Anton Melnikova, Larisa Babosha, Valentin Pokholkova, Galina V. Slovohotov, Ivan Umnova, Anastasia Maksimenko, Oksana Zhimulev, Igor F. Georgiev, Pavel The N-Terminal Part of Drosophila CP190 Is a Platform for Interaction with Multiple Architectural Proteins |
title | The N-Terminal Part of Drosophila CP190 Is a Platform for Interaction with Multiple Architectural Proteins |
title_full | The N-Terminal Part of Drosophila CP190 Is a Platform for Interaction with Multiple Architectural Proteins |
title_fullStr | The N-Terminal Part of Drosophila CP190 Is a Platform for Interaction with Multiple Architectural Proteins |
title_full_unstemmed | The N-Terminal Part of Drosophila CP190 Is a Platform for Interaction with Multiple Architectural Proteins |
title_short | The N-Terminal Part of Drosophila CP190 Is a Platform for Interaction with Multiple Architectural Proteins |
title_sort | n-terminal part of drosophila cp190 is a platform for interaction with multiple architectural proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10648081/ https://www.ncbi.nlm.nih.gov/pubmed/37958900 http://dx.doi.org/10.3390/ijms242115917 |
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