Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Golovnin, Anton, Melnikova, Larisa, Babosha, Valentin, Pokholkova, Galina V., Slovohotov, Ivan, Umnova, Anastasia, Maksimenko, Oksana, Zhimulev, Igor F., Georgiev, Pavel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
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
_version_ 1785135256067637248
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
work_keys_str_mv AT golovninanton thenterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT melnikovalarisa thenterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT baboshavalentin thenterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT pokholkovagalinav thenterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT slovohotovivan thenterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT umnovaanastasia thenterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT maksimenkooksana thenterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT zhimulevigorf thenterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT georgievpavel thenterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT golovninanton nterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT melnikovalarisa nterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT baboshavalentin nterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT pokholkovagalinav nterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT slovohotovivan nterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT umnovaanastasia nterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT maksimenkooksana nterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT zhimulevigorf nterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins
AT georgievpavel nterminalpartofdrosophilacp190isaplatformforinteractionwithmultiplearchitecturalproteins