Mechanisms of CP190 Interaction with Architectural Proteins in Drosophila Melanogaster

Most of the known Drosophila architectural proteins interact with an important cofactor, CP190, that contains three domains (BTB, M, and D) that are involved in protein–protein interactions. The highly conserved N-terminal CP190 BTB domain forms a stable homodimer that interacts with unstructured re...

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Autores principales:	Marat Sabirov, Anastasia Popovich, Konstantin Boyko, Alena Nikolaeva, Olga Kyrchanova, Oksana Maksimenko, Vladimir Popov, Pavel Georgiev, Artem Bonchuk
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	Pita Su(Hw) CTCF chromatin insulator transcription BTB domain Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/d5a6bdea5b2243b79c6cafb7e4885325
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spelling	oai:doaj.org-article:d5a6bdea5b2243b79c6cafb7e48853252021-11-25T17:56:17ZMechanisms of CP190 Interaction with Architectural Proteins in Drosophila Melanogaster10.3390/ijms2222124001422-00671661-6596https://doaj.org/article/d5a6bdea5b2243b79c6cafb7e48853252021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/22/12400https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Most of the known Drosophila architectural proteins interact with an important cofactor, CP190, that contains three domains (BTB, M, and D) that are involved in protein–protein interactions. The highly conserved N-terminal CP190 BTB domain forms a stable homodimer that interacts with unstructured regions in the three best-characterized architectural proteins: dCTCF, Su(Hw), and Pita. Here, we identified two new CP190 partners, CG4730 and CG31365, that interact with the BTB domain. The CP190 BTB resembles the previously characterized human BCL6 BTB domain, which uses its hydrophobic groove to specifically associate with unstructured regions of several transcriptional repressors. Using GST pull-down and yeast two-hybrid assays, we demonstrated that mutations in the hydrophobic groove strongly affect the affinity of CP190 BTB for the architectural proteins. In the yeast two-hybrid assay, we found that architectural proteins use various mechanisms to improve the efficiency of interaction with CP190. Pita and Su(Hw) have two unstructured regions that appear to simultaneously interact with hydrophobic grooves in the BTB dimer. In dCTCF and CG31365, two adjacent regions interact simultaneously with the hydrophobic groove of the BTB and the M domain of CP190. Finally, CG4730 interacts with the BTB, M, and D domains of CP190 simultaneously. These results suggest that architectural proteins use different mechanisms to increase the efficiency of interaction with CP190.Marat SabirovAnastasia PopovichKonstantin BoykoAlena NikolaevaOlga KyrchanovaOksana MaksimenkoVladimir PopovPavel GeorgievArtem BonchukMDPI AGarticlePitaSu(Hw)CTCFchromatin insulatortranscriptionBTB domainBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 12400, p 12400 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Pita Su(Hw) CTCF chromatin insulator transcription BTB domain Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	Pita Su(Hw) CTCF chromatin insulator transcription BTB domain Biology (General) QH301-705.5 Chemistry QD1-999 Marat Sabirov Anastasia Popovich Konstantin Boyko Alena Nikolaeva Olga Kyrchanova Oksana Maksimenko Vladimir Popov Pavel Georgiev Artem Bonchuk Mechanisms of CP190 Interaction with Architectural Proteins in Drosophila Melanogaster
description	Most of the known Drosophila architectural proteins interact with an important cofactor, CP190, that contains three domains (BTB, M, and D) that are involved in protein–protein interactions. The highly conserved N-terminal CP190 BTB domain forms a stable homodimer that interacts with unstructured regions in the three best-characterized architectural proteins: dCTCF, Su(Hw), and Pita. Here, we identified two new CP190 partners, CG4730 and CG31365, that interact with the BTB domain. The CP190 BTB resembles the previously characterized human BCL6 BTB domain, which uses its hydrophobic groove to specifically associate with unstructured regions of several transcriptional repressors. Using GST pull-down and yeast two-hybrid assays, we demonstrated that mutations in the hydrophobic groove strongly affect the affinity of CP190 BTB for the architectural proteins. In the yeast two-hybrid assay, we found that architectural proteins use various mechanisms to improve the efficiency of interaction with CP190. Pita and Su(Hw) have two unstructured regions that appear to simultaneously interact with hydrophobic grooves in the BTB dimer. In dCTCF and CG31365, two adjacent regions interact simultaneously with the hydrophobic groove of the BTB and the M domain of CP190. Finally, CG4730 interacts with the BTB, M, and D domains of CP190 simultaneously. These results suggest that architectural proteins use different mechanisms to increase the efficiency of interaction with CP190.
format	article
author	Marat Sabirov Anastasia Popovich Konstantin Boyko Alena Nikolaeva Olga Kyrchanova Oksana Maksimenko Vladimir Popov Pavel Georgiev Artem Bonchuk
author_facet	Marat Sabirov Anastasia Popovich Konstantin Boyko Alena Nikolaeva Olga Kyrchanova Oksana Maksimenko Vladimir Popov Pavel Georgiev Artem Bonchuk
author_sort	Marat Sabirov
title	Mechanisms of CP190 Interaction with Architectural Proteins in Drosophila Melanogaster
title_short	Mechanisms of CP190 Interaction with Architectural Proteins in Drosophila Melanogaster
title_full	Mechanisms of CP190 Interaction with Architectural Proteins in Drosophila Melanogaster
title_fullStr	Mechanisms of CP190 Interaction with Architectural Proteins in Drosophila Melanogaster
title_full_unstemmed	Mechanisms of CP190 Interaction with Architectural Proteins in Drosophila Melanogaster
title_sort	mechanisms of cp190 interaction with architectural proteins in drosophila melanogaster
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/d5a6bdea5b2243b79c6cafb7e4885325
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_version_	1718411833846530048

Mechanisms of CP190 Interaction with Architectural Proteins in Drosophila Melanogaster

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