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...
| Autores: | , , , , , , |
|---|---|
| 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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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 |
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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/ |
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info:eu-repo/semantics/openAccess |
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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/ |
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openAccess |
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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 |
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reponame:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia instname:Universitat Politècnica de València (UPV) |
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Universitat Politècnica de València (UPV) |
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RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia |
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RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia |
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1869416297892151296 |
| 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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15,812429 |