Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability.

[EN] The SWItch/Sucrose Non-Fermenting (SWI/SNF) complexes are evolutionarily conserved, ATP-dependent chromatin remodelers crucial for multiple nuclear functions in eukaryotes. Recently, plant BCL-DOMAIN HOMOLOG (BDH) proteins were identified as shared subunits of all plant SWI/SNF complexes, signi...

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Detalhes bibliográficos
Autores: Candela-Ferre, Joan, Pérez-Alemany, Jaime, Lozano-Juste, Jorge|||0000-0001-7034-566X, Gallego Bartolomé, Javier, Diego-Martín, Borja, Pandey, Vijaya, Wohlschlegel, James
Formato: artículo
Fecha de publicación:2025
País:España
Recursos:Universitat Politècnica de València (UPV)
Repositorio:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
Idioma:inglés
OAI Identifier:oai:dnet:riunet______::69f1b00bc1e57bce6f191e9b864e232a
Acesso em linha:https://riunet.upv.es/handle/10251/235526
Access Level:acceso abierto
Palavra-chave:SWI/SNF
Chromatin
Remodeling
Arabidopsis
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dc.title.none.fl_str_mv Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability.
title Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability.
spellingShingle Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability.
Candela-Ferre, Joan
SWI/SNF
Chromatin
Remodeling
Arabidopsis
title_short Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability.
title_full Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability.
title_fullStr Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability.
title_full_unstemmed Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability.
title_sort Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability.
dc.creator.none.fl_str_mv Candela-Ferre, Joan
Pérez-Alemany, Jaime
Lozano-Juste, Jorge|||0000-0001-7034-566X
Gallego Bartolomé, Javier
Diego-Martín, Borja
Pandey, Vijaya
Wohlschlegel, James
author Candela-Ferre, Joan
author_facet Candela-Ferre, Joan
Pérez-Alemany, Jaime
Lozano-Juste, Jorge|||0000-0001-7034-566X
Gallego Bartolomé, Javier
Diego-Martín, Borja
Pandey, Vijaya
Wohlschlegel, James
author_role author
author2 Pérez-Alemany, Jaime
Lozano-Juste, Jorge|||0000-0001-7034-566X
Gallego Bartolomé, Javier
Diego-Martín, Borja
Pandey, Vijaya
Wohlschlegel, James
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Instituto Universitario Mixto de Biología Molecular y Celular de Plantas
European Social Fund
Generalitat Valenciana
Agencia Estatal de Investigación
European Regional Development Fund
Ministerio de Ciencia e Innovación
National Institutes of Health, EEUU
Repositorio Institucional de la Universitat Politècnica de València Riunet
dc.subject.none.fl_str_mv SWI/SNF
Chromatin
Remodeling
Arabidopsis
topic SWI/SNF
Chromatin
Remodeling
Arabidopsis
description [EN] The SWItch/Sucrose Non-Fermenting (SWI/SNF) complexes are evolutionarily conserved, ATP-dependent chromatin remodelers crucial for multiple nuclear functions in eukaryotes. Recently, plant BCL-DOMAIN HOMOLOG (BDH) proteins were identified as shared subunits of all plant SWI/SNF complexes, significantly impacting chromatin accessibility and various developmental processes in Arabidopsis. In this study, we performed a comprehensive characterization of bdh mutants, revealing the role of BDH in hypocotyl cell elongation. Through detailed analysis of BDH domains, we identified a plant-specific N-terminal domain that facilitates the interaction between BDH and the rest of the complex. Additionally, we uncovered the critical role of the BDH ß-hairpin domain, which is phylogenetically related to mammalian BCL7 SWI/ SNF subunits. While phylogenetic analyses did not identify BDH/BCL7 orthologs in fungi, structure prediction modeling demonstrated strong similarities between the SWI/ SNF catalytic modules of plants, animals, and fungi and revealed the yeast Rtt102 protein as a structural homolog of BDH and BCL7. This finding is supported by the ability of Rtt102 to interact with the Arabidopsis catalytic module subunit ARP7 and partially rescue the bdh mutant phenotypes. Further experiments revealed that BDH promotes the stability of the ARP4-ARP7 heterodimer, leading to the partial destabilization of ARP4 in the SWI/SNF complexes. In summary, our study unveils the molecular function of BDH proteins in plant SWI/SNF complexes and suggests that ß-hairpin-containing proteins are evolutionarily conserved subunits crucial for ARP heterodimer stability and SWI/SNF activity across eukaryotes.
publishDate 2025
dc.date.none.fl_str_mv 2025
2025-01-15
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://riunet.upv.es/handle/10251/235526
url https://riunet.upv.es/handle/10251/235526
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Agencia Estatal de Investigación http://dx.doi.org/10.13039/501100011033 Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020 PID2019-108577GA-I00 FUNCION DE LAS PROTEINS PHD EN COMPLEJOS DE REMODELACION DE CROMATINA SWI%2FSNF EN PLANTAS
Agencia Estatal de Investigación http://dx.doi.org/10.13039/501100011033 Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023 PID2021-128826OA-I00 DISEÑO DE PEQUEÑAS MOLÉCULAS Y DESCUBRIMIENTO DE NUEVAS DIANAS PARA ACTIVAR LA RESISTENCA A LA SEQUIA DE PLANTAS DE COSECHA.
Agencia Estatal de Investigación http://dx.doi.org/10.13039/501100011033 Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023 PID2022-140355NB-I00 PAPEL DE LA REMODELACION DE LA CROMATINA EN LA SELECCION DEL SITIO DE INICIO DE LA TRANSCRIPCION EN PLANTAS
Generalitat Valenciana https://doi.org/10.13039/501100003359 CISEJI%2F2022%2F26
Generalitat Valenciana https://doi.org/10.13039/501100003359 AGROALNEXT%2F2022%2F067
National Institutes of Health, EEUU https://doi.org/10.13039/100000002 R35GM153408
Ministerio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 RYC2018-024108-I
Ministerio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 PRE2020-094943
Ministerio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 RYC2020-029097-I
Ministerio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 CNS2023-145540
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Reconocimiento - No comercial - Sin obra derivada (by-nc-nd)
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Reconocimiento - No comercial - Sin obra derivada (by-nc-nd)
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Proceedings of the National Academy of Sciences
publisher.none.fl_str_mv Proceedings of the National Academy of Sciences
dc.source.none.fl_str_mv reponame:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
instname:Universitat Politècnica de València (UPV)
instname_str Universitat Politècnica de València (UPV)
reponame_str RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
collection RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
repository.name.fl_str_mv
repository.mail.fl_str_mv
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spelling Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability.Candela-Ferre, JoanPérez-Alemany, JaimeLozano-Juste, Jorge|||0000-0001-7034-566XGallego Bartolomé, JavierDiego-Martín, BorjaPandey, VijayaWohlschlegel, JamesSWI/SNFChromatinRemodelingArabidopsis[EN] The SWItch/Sucrose Non-Fermenting (SWI/SNF) complexes are evolutionarily conserved, ATP-dependent chromatin remodelers crucial for multiple nuclear functions in eukaryotes. Recently, plant BCL-DOMAIN HOMOLOG (BDH) proteins were identified as shared subunits of all plant SWI/SNF complexes, significantly impacting chromatin accessibility and various developmental processes in Arabidopsis. In this study, we performed a comprehensive characterization of bdh mutants, revealing the role of BDH in hypocotyl cell elongation. Through detailed analysis of BDH domains, we identified a plant-specific N-terminal domain that facilitates the interaction between BDH and the rest of the complex. Additionally, we uncovered the critical role of the BDH ß-hairpin domain, which is phylogenetically related to mammalian BCL7 SWI/ SNF subunits. While phylogenetic analyses did not identify BDH/BCL7 orthologs in fungi, structure prediction modeling demonstrated strong similarities between the SWI/ SNF catalytic modules of plants, animals, and fungi and revealed the yeast Rtt102 protein as a structural homolog of BDH and BCL7. This finding is supported by the ability of Rtt102 to interact with the Arabidopsis catalytic module subunit ARP7 and partially rescue the bdh mutant phenotypes. Further experiments revealed that BDH promotes the stability of the ARP4-ARP7 heterodimer, leading to the partial destabilization of ARP4 in the SWI/SNF complexes. In summary, our study unveils the molecular function of BDH proteins in plant SWI/SNF complexes and suggests that ß-hairpin-containing proteins are evolutionarily conserved subunits crucial for ARP heterodimer stability and SWI/SNF activity across eukaryotes.We thank Rafa Ruiz-Partida for advice on selecting BDH protein mutations. This work was supported by grants: NIH R35GM153408 (to J.W.); RYC2018-024108-I (to J.G.-B.) and RYC2020-029097-I (to J.L.-J.) funded by MCIN/AEI/10.13039/501100011033 and by ESF Investing in your future ; PID2019-108577GA-I00 (to J.G.-B.) funded by MCIN/AEI/10.13039/501100011033; PID2022-140355NB-I00 (to J.G.-B.) and PID2021-128826OA-I00 (to J.L.-J.) funded by MICIU/AEI/10.13039/501100011033 and by ERDF/UE; CNS2023-145540 (to J.L.-J.) funded by MICIU/AEI/10.13039/501100011033 and by European Union NextGenerationEU/PRTR; CISEJI/2022/26 (to J.L.-J.) from Generalitat Valenciana (GVA); and AGROALNEXT/2022/067 supported by MICIN with funding from European Union NextGenerationEU (PRTR-C17.I1) and by Generalitat Valenciana. Also, PRE2020-094943 contract (to J.C.-F.) from the Spanish Ministry of Science and Innovation; CIACIF/2021/432 contract (to J.P.-A.) from the Generalitat Valenciana; and FPU19/05694 contract (to B.D.-M.) from the Spanish Ministry of Universities.Proceedings of the National Academy of SciencesInstituto Universitario Mixto de Biología Molecular y Celular de PlantasEuropean Social FundGeneralitat ValencianaAgencia Estatal de InvestigaciónEuropean Regional Development FundMinisterio de Ciencia e InnovaciónNational Institutes of Health, EEUURepositorio Institucional de la Universitat Politècnica de València Riunet20252025-01-15journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://riunet.upv.es/handle/10251/235526reponame:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valénciainstname:Universitat Politècnica de València (UPV)InglésengAgencia Estatal de Investigación http://dx.doi.org/10.13039/501100011033 Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020 PID2019-108577GA-I00 FUNCION DE LAS PROTEINS PHD EN COMPLEJOS DE REMODELACION DE CROMATINA SWI%2FSNF EN PLANTASAgencia Estatal de Investigación http://dx.doi.org/10.13039/501100011033 Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023 PID2021-128826OA-I00 DISEÑO DE PEQUEÑAS MOLÉCULAS Y DESCUBRIMIENTO DE NUEVAS DIANAS PARA ACTIVAR LA RESISTENCA A LA SEQUIA DE PLANTAS DE COSECHA.Agencia Estatal de Investigación http://dx.doi.org/10.13039/501100011033 Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023 PID2022-140355NB-I00 PAPEL DE LA REMODELACION DE LA CROMATINA EN LA SELECCION DEL SITIO DE INICIO DE LA TRANSCRIPCION EN PLANTASGeneralitat Valenciana https://doi.org/10.13039/501100003359 CISEJI%2F2022%2F26Generalitat Valenciana https://doi.org/10.13039/501100003359 AGROALNEXT%2F2022%2F067National Institutes of Health, EEUU https://doi.org/10.13039/100000002 R35GM153408Ministerio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 RYC2018-024108-IMinisterio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 PRE2020-094943Ministerio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 RYC2020-029097-IMinisterio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 CNS2023-145540open accesshttp://purl.org/coar/access_right/c_abf2Reconocimiento - No comercial - Sin obra derivada (by-nc-nd) http://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:dnet:riunet______::69f1b00bc1e57bce6f191e9b864e232a2026-06-13T07:49:27Z
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