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

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dc.contributor.affiliationInstituto Universitario Mixto de Biología Molecular y Celular de Plantas
dc.contributor.authorCandela-Ferre, Joan
dc.contributor.authorPérez-Alemany, Jaime
dc.contributor.authorDiego-Martín, Borjaes_ES
dc.contributor.authorPandey, Vijayaes_ES
dc.contributor.authorWohlschlegel, Jameses_ES
dc.contributor.authorLozano-Juste, Jorge
dc.contributor.authorGallego Bartolomé, Javier
dc.contributor.funderEuropean Social Fundes_ES
dc.contributor.funderGeneralitat Valencianaes_ES
dc.contributor.funderAgencia Estatal de Investigaciónes_ES
dc.contributor.funderEuropean Regional Development Fundes_ES
dc.contributor.funderMinisterio de Ciencia e Innovaciónes_ES
dc.contributor.funderNational Institutes of Health, EEUUes_ES
dc.date.accessioned2026-05-28T11:59:50Z
dc.date.available2026-05-28T11:59:50Z
dc.date.issued2025-01-15es_ES
dc.description.abstract[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.es_ES
dc.description.accrualMethodSes_ES
dc.description.bibliographicCitationCandela-Ferre, Joan; Pérez-Alemany, Jaime; Diego-Martín, B.; Pandey, V.; Wohlschlegel, J.; Lozano-Juste, Jorge; Gallego Bartolomé, Javier (2025). Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability. Proceedings of the National Academy of Sciences of the United States of America (Online). 122(3). https://doi.org/10.1073/pnas.2413346122es_ES
dc.description.issue3es_ES
dc.description.referencesLuger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997). Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature, 389(6648), 251-260. https://doi.org/10.1038/38444es_ES
dc.description.referencesKornberg, R. D. (1974). Chromatin Structure: A Repeating Unit of Histones and DNA: Chromatin structure is based on a repeating unit of eight histone molecules and about 200 DNA base pairs. Science, 184(4139), 868-871. https://doi.org/10.1126/science.184.4139.868es_ES
dc.description.referencesKlemm, S. L., Shipony, Z., & Greenleaf, W. J. (2019). Chromatin accessibility and the regulatory epigenome. Nature Reviews Genetics, 20(4), 207-220. https://doi.org/10.1038/s41576-018-0089-8es_ES
dc.description.referencesMillán-Zambrano, G., Burton, A., Bannister, A. J., & Schneider, R. (2022). Histone post-translational modifications — cause and consequence of genome function. Nature Reviews Genetics, 23(9), 563-580. https://doi.org/10.1038/s41576-022-00468-7es_ES
dc.description.referencesClapier, C. R., Iwasa, J., Cairns, B. R., & Peterson, C. L. (2017). Mechanisms of action and regulation of ATP-dependent chromatin-remodelling complexes. Nature Reviews Molecular Cell Biology, 18(7), 407-422. https://doi.org/10.1038/nrm.2017.26es_ES
dc.description.referencesBieluszewski, T., Prakash, S., Roulé, T., & Wagner, D. (2023). The Role and Activity of SWI/SNF Chromatin Remodelers. Annual Review of Plant Biology, 74(1), 139-163. https://doi.org/10.1146/annurev-arplant-102820-093218es_ES
dc.description.referencesHodges, C., Kirkland, J. G., & Crabtree, G. R. (2016). The Many Roles of BAF (mSWI/SNF) and PBAF Complexes in Cancer. Cold Spring Harbor Perspectives in Medicine, 6(8), a026930. https://doi.org/10.1101/cshperspect.a026930es_ES
dc.description.referencesShang, J.-Y., & He, X.-J. (2022). Chromatin‐remodeling complexes: Conserved and plant‐specific subunits in <i>Arabidopsis</i>. Journal of Integrative Plant Biology, 64(2), 499-515. Portico. https://doi.org/10.1111/jipb.13208es_ES
dc.description.referencesGuo, J., Cai, G., Li, Y.-Q., Zhang, Y.-X., Su, Y.-N., Yuan, D.-Y., Zhang, Z.-C., Liu, Z.-Z., Cai, X.-W., Guo, J., Li, L., Chen, S., & He, X.-J. (2022). Comprehensive characterization of three classes of Arabidopsis SWI/SNF chromatin remodelling complexes. Nature Plants, 8(12), 1423-1439. https://doi.org/10.1038/s41477-022-01282-zes_ES
dc.description.referencesFu, W., Yu, Y., Shu, J., Yu, Z., Zhong, Y., Zhu, T., Zhang, Z., Liang, Z., Cui, Y., Chen, C., & Li, C. (2023). Organization, genomic targeting, and assembly of three distinct SWI/SNF chromatin remodeling complexes in Arabidopsis. The Plant Cell, 35(7), 2464-2483. https://doi.org/10.1093/plcell/koad111es_ES
dc.description.referencesMashtalir, N., D’Avino, A. R., Michel, B. C., Luo, J., Pan, J., Otto, J. E., Zullow, H. J., McKenzie, Z. M., Kubiak, R. L., St. Pierre, R., Valencia, A. M., Poynter, S. J., Cassel, S. H., Ranish, J. A., & Kadoch, C. (2018). Modular Organization and Assembly of SWI/SNF Family Chromatin Remodeling Complexes. Cell, 175(5), 1272-1288. https://doi.org/10.1016/j.cell.2018.09.032es_ES
dc.description.referencesHernández-García, J., Diego-Martin, B., Kuo, P. H., Jami-Alahmadi, Y., Vashisht, A. A., Wohlschlegel, J., Jacobsen, S. E., Blázquez, M. A., & Gallego-Bartolomé, J. (2022). Comprehensive identification of SWI/SNF complex subunits underpins deep eukaryotic ancestry and reveals new plant components. Communications Biology, 5(1). https://doi.org/10.1038/s42003-022-03490-xes_ES
dc.description.referencesDiego-Martin, B., Pérez-Alemany, J., Candela-Ferre, J., Corbalán-Acedo, A., Pereyra, J., Alabadí, D., Jami-Alahmadi, Y., Wohlschlegel, J., & Gallego-Bartolomé, J. (2022). The TRIPLE PHD FINGERS proteins are required for SWI/SNF complex-mediated +1 nucleosome positioning and transcription start site determination in Arabidopsis. Nucleic Acids Research, 50(18), 10399-10417. https://doi.org/10.1093/nar/gkac826es_ES
dc.description.referencesSzerlong, H., Hinata, K., Viswanathan, R., Erdjument-Bromage, H., Tempst, P., & Cairns, B. R. (2008). The HSA domain binds nuclear actin-related proteins to regulate chromatin-remodeling ATPases. Nature Structural &amp; Molecular Biology, 15(5), 469-476. https://doi.org/10.1038/nsmb.1403es_ES
dc.description.referencesHan, Y., Reyes, A. A., Malik, S., & He, Y. (2020). Cryo-EM structure of SWI/SNF complex bound to a nucleosome. Nature, 579(7799), 452-455. https://doi.org/10.1038/s41586-020-2087-1es_ES
dc.description.referencesSchubert, H. L., Wittmeyer, J., Kasten, M. M., Hinata, K., Rawling, D. C., Héroux, A., Cairns, B. R., & Hill, C. P. (2013). Structure of an actin-related subcomplex of the SWI/SNF chromatin remodeler. Proceedings of the National Academy of Sciences, 110(9), 3345-3350. https://doi.org/10.1073/pnas.1215379110es_ES
dc.description.referencesClapier, Cedric R., Kasten, Margaret M., Parnell, Timothy J., Viswanathan, R., Szerlong, H., Sirinakis, G., Zhang, Y., & Cairns, Bradley R. (2016). Regulation of DNA Translocation Efficiency within the Chromatin Remodeler RSC/Sth1 Potentiates Nucleosome Sliding and Ejection. Molecular Cell, 62(3), 453-461. https://doi.org/10.1016/j.molcel.2016.03.032es_ES
dc.description.referencesClapier, C. R., & Cairns, B. R. (2009). The Biology of Chromatin Remodeling Complexes. Annual Review of Biochemistry, 78(1), 273-304. https://doi.org/10.1146/annurev.biochem.77.062706.153223es_ES
dc.description.referencesMeagher, R. B., Deal, R. B., Kandasamy, M. K., & McKinney, E. C. (2005). Nuclear Actin-Related Proteins as Epigenetic Regulators of Development. Plant Physiology, 139(4), 1576-1585. https://doi.org/10.1104/pp.105.072447es_ES
dc.description.referencesMashtalir, N., Suzuki, H., Farrell, D. P., Sankar, A., Luo, J., Filipovski, M., D’Avino, A. R., St. Pierre, R., Valencia, A. M., Onikubo, T., Roeder, R. G., Han, Y., He, Y., Ranish, J. A., DiMaio, F., Walz, T., & Kadoch, C. (2020). A Structural Model of the Endogenous Human BAF Complex Informs Disease Mechanisms. Cell, 183(3), 802-817. https://doi.org/10.1016/j.cell.2020.09.051es_ES
dc.description.referencesWischhof, L., Lee, H.-M., Tutas, J., Overkott, C., Tedt, E., Stork, M., Peitz, M., Brüstle, O., Ulas, T., Händler, K., Schultze, J. L., Ehninger, D., Nicotera, P., Salomoni, P., & Bano, D. (2022). BCL7A‐containing SWI/SNF/BAF complexes modulate mitochondrial bioenergetics during neural progenitor differentiation. The EMBO Journal, 41(23). https://doi.org/10.15252/embj.2022110595es_ES
dc.description.referencesD. Diaz BCL7 proteins metazoan-specific subunits of the mammalian SWI/SNF complex bind the nucleosome core particle. bioRxiv [Preprint] (2023). https://doi.org/10.1101/2023.03.17.532992 (Accessed 17 March 2023).es_ES
dc.description.referencesTuregun, B., Kast, D. J., & Dominguez, R. (2013). Subunit Rtt102 Controls the Conformation of the Arp7/9 Heterodimer and Its Interactions with Nucleotide and the Catalytic Subunit of SWI/SNF Remodelers. Journal of Biological Chemistry, 288(50), 35758-35768. https://doi.org/10.1074/jbc.m113.514083es_ES
dc.description.referencesVercruyssen, L., Verkest, A., Gonzalez, N., Heyndrickx, K. S., Eeckhout, D., Han, S.-K., Jégu, T., Archacki, R., Van Leene, J., Andriankaja, M., De Bodt, S., Abeel, T., Coppens, F., Dhondt, S., De Milde, L., Vermeersch, M., Maleux, K., Gevaert, K., Jerzmanowski, A., et al. (2014). ANGUSTIFOLIA3 Binds to SWI/SNF Chromatin Remodeling Complexes to Regulate Transcription during <i>Arabidopsis</i> Leaf Development. The Plant Cell, 26(1), 210-229. https://doi.org/10.1105/tpc.113.115907es_ES
dc.description.referencesStachula, P., Kapela, K., Malecka, E., Jaronczyk, K., Patryn, J., Siwirykow, N., Bucholc, M., Marczak, M., Kotlinski, M., & Archacki, R. (2023). BRM Complex in Arabidopsis Adopts ncBAF-like Composition and Requires BRD Subunits for Assembly and Stability. International Journal of Molecular Sciences, 24(4), 3917. https://doi.org/10.3390/ijms24043917es_ES
dc.description.referencesLei, Y., Yu, Y., Fu, W., Zhu, T., Wu, C., Zhang, Z., Yu, Z., Song, X., Xu, J., Liang, Z., Lü, P., & Li, C. (2024). BCL7A and BCL7B potentiate SWI/SNF-complex-mediated chromatin accessibility to regulate gene expression and vegetative phase transition in plants. Nature Communications, 15(1). https://doi.org/10.1038/s41467-024-45250-xes_ES
dc.description.referencesEklöf, J. M., & Brumer, H. (2010). The <i>XTH</i> Gene Family: An Update on Enzyme Structure, Function, and Phylogeny in Xyloglucan Remodeling. Plant Physiology, 153(2), 456-466. https://doi.org/10.1104/pp.110.156844es_ES
dc.description.referencesJumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., Bridgland, A., Meyer, C., Kohl, S. A. A., Ballard, A. J., Cowie, A., Romera-Paredes, B., Nikolov, S., Jain, R., Adler, J., et al. (2021). Highly accurate protein structure prediction with AlphaFold. Nature, 596(7873), 583-589. https://doi.org/10.1038/s41586-021-03819-2es_ES
dc.description.referencesJones, D. T., & Cozzetto, D. (2014). DISOPRED3: precise disordered region predictions with annotated protein-binding activity. Bioinformatics, 31(6), 857-863. https://doi.org/10.1093/bioinformatics/btu744es_ES
dc.description.referencesR. Evans Protein complex prediction with AlphaFold-multimer. bioRxiv [Preprint] (2022). https://doi.org/10.1101/2021.10.04.463034 (Accessed 10 March 2022).es_ES
dc.description.referencesHe, S., Wu, Z., Tian, Y., Yu, Z., Yu, J., Wang, X., Li, J., Liu, B., & Xu, Y. (2020). Structure of nucleosome-bound human BAF complex. Science, 367(6480), 875-881. https://doi.org/10.1126/science.aaz9761es_ES
dc.description.referencesBezhani, S., Winter, C., Hershman, S., Wagner, J. D., Kennedy, J. F., Kwon, C. S., Pfluger, J., Su, Y., & Wagner, D. (2007). Unique, Shared, and Redundant Roles for the <i>Arabidopsis</i> SWI/SNF Chromatin Remodeling ATPases BRAHMA and SPLAYED. The Plant Cell, 19(2), 403-416. https://doi.org/10.1105/tpc.106.048272es_ES
dc.description.referencesSang, Y., Silva‐Ortega, C. O., Wu, S., Yamaguchi, N., Wu, M.-F., Pfluger, J., Gillmor, C. S., Gallagher, K. L., & Wagner, D. (2012). Mutations in two non‐canonical Arabidopsis SWI2/SNF2 chromatin remodeling ATPases cause embryogenesis and stem cell maintenance defects. The Plant Journal, 72(6), 1000-1014. Portico. https://doi.org/10.1111/tpj.12009es_ES
dc.description.referencesJégu, T., Veluchamy, A., Ramirez-Prado, J. S., Rizzi-Paillet, C., Perez, M., Lhomme, A., Latrasse, D., Coleno, E., Vicaire, S., Legras, S., Jost, B., Rougée, M., Barneche, F., Bergounioux, C., Crespi, M., Mahfouz, M. M., Hirt, H., Raynaud, C., & Benhamed, M. (2017). The Arabidopsis SWI/SNF protein BAF60 mediates seedling growth control by modulating DNA accessibility. Genome Biology, 18(1). https://doi.org/10.1186/s13059-017-1246-7es_ES
dc.description.referencesZhu, T., Wei, C., Yu, Y., Zhang, Z., Zhu, J., Liang, Z., Song, X., Fu, W., Cui, Y., Wang, Z.-Y., & Li, C. (2024). The BAS chromatin remodeler determines brassinosteroid-induced transcriptional activation and plant growth in Arabidopsis. Developmental Cell, 59(7), 924-939. https://doi.org/10.1016/j.devcel.2024.01.021es_ES
dc.description.referencesArchacki, R., Buszewicz, D., Sarnowski, T. J., Sarnowska, E., Rolicka, A. T., Tohge, T., Fernie, A. R., Jikumaru, Y., Kotlinski, M., Iwanicka-Nowicka, R., Kalisiak, K., Patryn, J., Halibart-Puzio, J., Kamiya, Y., Davis, S. J., Koblowska, M. K., & Jerzmanowski, A. (2013). BRAHMA ATPase of the SWI/SNF Chromatin Remodeling Complex Acts as a Positive Regulator of Gibberellin-Mediated Responses in Arabidopsis. PLoS ONE, 8(3), e58588. https://doi.org/10.1371/journal.pone.0058588es_ES
dc.description.referencesFolta, A., Severing, E. I., Krauskopf, J., van de Geest, H., Verver, J., Nap, J.-P., & Mlynarova, L. (2014). Over-expression of Arabidopsis AtCHR23 chromatin remodeling ATPase results in increased variability of growth and gene expression. BMC Plant Biology, 14(1). https://doi.org/10.1186/1471-2229-14-76es_ES
dc.description.referencesMiedes, E., Suslov, D., Vandenbussche, F., Kenobi, K., Ivakov, A., Van Der Straeten, D., Lorences, E. P., Mellerowicz, E. J., Verbelen, J.-P., & Vissenberg, K. (2013). Xyloglucan endotransglucosylase/hydrolase (XTH) overexpression affects growth and cell wall mechanics in etiolated Arabidopsis hypocotyls. Journal of Experimental Botany, 64(8), 2481-2497. https://doi.org/10.1093/jxb/ert107es_ES
dc.description.referencesDhar, S., Kim, J., Yoon, E. K., Jang, S., Ko, K., & Lim, J. (2022). SHORT-ROOT Controls Cell Elongation in the Etiolated Arabidopsis Hypocotyl. Molecules and Cells, 45(4), 243-256. https://doi.org/10.14348/molcells.2021.5008es_ES
dc.description.referencesBaliñas-Gavira, C., Rodríguez, M. I., Andrades, A., Cuadros, M., Álvarez-Pérez, J. C., Álvarez-Prado, Á. F., de Yébenes, V. G., Sánchez-Hernández, S., Fernández-Vigo, E., Muñoz, J., Martín, F., Ramiro, A. R., Martínez-Climent, J. A., & Medina, P. P. (2020). Frequent mutations in the amino-terminal domain of BCL7A impair its tumor suppressor role in DLBCL. Leukemia, 34(10), 2722-2735. https://doi.org/10.1038/s41375-020-0919-5es_ES
dc.description.referencesSen, P., Luo, J., Hada, A., Hailu, S. G., Dechassa, M. L., Persinger, J., Brahma, S., Paul, S., Ranish, J., & Bartholomew, B. (2017). Loss of Snf5 Induces Formation of an Aberrant SWI/SNF Complex. Cell Reports, 18(9), 2135-2147. https://doi.org/10.1016/j.celrep.2017.02.017es_ES
dc.description.referencesKunert, F., Metzner, F. J., Jung, J., Höpfler, M., Woike, S., Schall, K., Kostrewa, D., Moldt, M., Chen, J.-X., Bantele, S., Pfander, B., Eustermann, S., & Hopfner, K.-P. (2022). Structural mechanism of extranucleosomal DNA readout by the INO80 complex. Science Advances, 8(49). https://doi.org/10.1126/sciadv.add3189es_ES
dc.description.referencesEspinosa-Cores, L., Bouza-Morcillo, L., Barrero-Gil, J., Jiménez-Suárez, V., Lázaro, A., Piqueras, R., Jarillo, J. A., & Piñeiro, M. (2020). Insights Into the Function of the NuA4 Complex in Plants. Frontiers in Plant Science, 11. https://doi.org/10.3389/fpls.2020.00125es_ES
dc.description.referencesGerhold, C. B., & Gasser, S. M. (2014). INO80 and SWR complexes: relating structure to function in chromatin remodeling. Trends in Cell Biology, 24(11), 619-631. https://doi.org/10.1016/j.tcb.2014.06.004es_ES
dc.description.referencesTuregun, B., Baker, R. W., Leschziner, A. E., & Dominguez, R. (2018). Actin-related proteins regulate the RSC chromatin remodeler by weakening intramolecular interactions of the Sth1 ATPase. Communications Biology, 1(1). https://doi.org/10.1038/s42003-017-0002-6es_ES
dc.description.referencesLivak, K. J., & Schmittgen, T. D. (2001). Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method. Methods, 25(4), 402-408. https://doi.org/10.1006/meth.2001.1262es_ES
dc.description.referencesMirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2022). ColabFold: making protein folding accessible to all. Nature Methods, 19(6), 679-682. https://doi.org/10.1038/s41592-022-01488-1es_ES
dc.description.referencesRamírez, F., Dündar, F., Diehl, S., Grüning, B. A., & Manke, T. (2014). deepTools: a flexible platform for exploring deep-sequencing data. Nucleic Acids Research, 42(W1), W187-W191. https://doi.org/10.1093/nar/gku365es_ES
dc.description.referencesJ. Candela-Ferre Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability. NCBI-Gene Expression Omnibus. https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE268510. Deposited 28 May 2024.es_ES
dc.description.referencesJ. Candela-Ferre Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability. NCBI-Gene Expression Omnibus. https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE268511. Deposited 28 May 2024.es_ES
dc.description.referencesC. Li W. Fu Y. Yu Organization genomic targeting and assembly of three distinct SWI/SNF chromatin remodeling complexes in Arabidopsis. NCBI-Gene Expression Omnibus. https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE218841. Deposited 27 November 2022.es_ES
dc.description.referencesX. He Three classes of Arabidopsis SWI/SNF chromatin remodeling complexes differentially regulate development by affecting chromatin accessibility. NCBI-Gene Expression Omnibus. https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE193095. Deposited 5 January 2022.es_ES
dc.description.referencesJ. Gallego-Bartolomé Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability. MassIVE. https://massive.ucsd.edu/ProteoSAFe/dataset.jsp?task=2f76b69679cf42cca2c20866ffcf251c. Deposited 11 June 2024.es_ES
dc.description.referencesJ. Candela-Ferre Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability. Mendeley Data. https://data.mendeley.com/datasets/37jzt2bgth/1. Deposited 27 December 2024.es_ES
dc.description.sponsorshipWe 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.es_ES
dc.description.volume122es_ES
dc.identifier.doi10.1073/pnas.2413346122es_ES
dc.identifier.eissn1091-6490es_ES
dc.identifier.pmcidPMC11761322es_ES
dc.identifier.pmid39823297es_ES
dc.identifier.urihttps://riunet.upv.es/handle/10251/235526
dc.languageIngléses_ES
dc.publisherProceedings of the National Academy of Scienceses_ES
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of America (Online)es_ES
dc.relation.pasarelaS\561094es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-108577GA-I00/ES/FUNCION DE LAS PROTEINS PHD EN COMPLEJOS DE REMODELACION DE CROMATINA SWI%2FSNF EN PLANTAS/es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2021-128826OA-I00/ES/DISEÑO DE PEQUEÑAS MOLÉCULAS Y DESCUBRIMIENTO DE NUEVAS DIANAS PARA ACTIVAR LA RESISTENCA A LA SEQUIA DE PLANTAS DE COSECHA./es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-140355NB-I00/ES/PAPEL DE LA REMODELACION DE LA CROMATINA EN LA SELECCION DEL SITIO DE INICIO DE LA TRANSCRIPCION EN PLANTAS/es_ES
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dc.relation.projectIDinfo:eu-repo/grantAgreement/GVA//AGROALNEXT%2F2022%2F067/es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/NIH//R35GM153408/es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/MICINN//RYC2018-024108-I/es_ES
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dc.relation.projectIDinfo:eu-repo/grantAgreement/MICINN//RYC2020-029097-I/es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/MICINN//CNS2023-145540/es_ES
dc.relation.publisherversionhttps://doi.org/10.1073/pnas.2413346122es_ES
dc.rightsReconocimiento - No comercial - Sin obra derivada (by-nc-nd)es_ES
dc.rights.accessRightsAbiertoes_ES
dc.subjectSWI/SNFes_ES
dc.subjectChromatines_ES
dc.subjectRemodelinges_ES
dc.subjectArabidopsises_ES
dc.titlePlant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability.es_ES
dc.typeArtículoes_ES
dc.type.versioninfo:eu-repo/semantics/publishedVersiones_ES
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