The structure of the R2T complex reveals a different architecture from the related HSP90 cochaperone R2TP

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dc.contributor.affiliationInstituto Universitario Mixto de Biología Molecular y Celular de Plantas
dc.contributor.authorPalacios-Abella, Albertoes_ES
dc.contributor.authorLópez-Perrote, Andréses_ES
dc.contributor.authorBoskovic, Jasminkaes_ES
dc.contributor.authorFonseca, Sandraes_ES
dc.contributor.authorUrbez Lagunas, Cristina
dc.contributor.authorRubio, Vicentees_ES
dc.contributor.authorLlorca, Oscares_ES
dc.contributor.authorALABADÍ DIEGO, DAVID
dc.contributor.funderMinisterio de Educaciónes_ES
dc.contributor.funderInstituto de Salud Carlos IIIes_ES
dc.contributor.funderAgencia Estatal de Investigaciónes_ES
dc.contributor.funderEuropean Regional Development Fundes_ES
dc.date.accessioned2026-05-06T09:33:06Z
dc.date.available2026-05-06T09:33:06Z
dc.date.issued2025-04-03es_ES
dc.description.abstract[EN] The R2TP complex is a specialized HSP90 cochaperone essential for the maturation of macromolecular complexes such as RNAPII and TORC1. R2TP is formed by a hetero-hexameric ring of AAA-ATPases RuvBL1 and RuvBL2, which interact with RPAP3 and PIH1D1. Several R2TP-like complexes have been described, but these are less well characterized. Here, we identified, characterized and determined the cryo-electron microscopy (cryo-EM) structure of R2T from Arabidopsis thaliana, which lacks PIH1D1 and is probably the only form of the complex in seed plants. In contrast to R2TP, R2T is organized as two rings of AtRuvBL1-AtRuvBL2a interacting back-to-back, with one AtRPAP3 anchored per ring. AtRPAP3 has no effect on the ATPase activity of AtRuvBL1-AtRuvBL2a and binds with a different stoichiometry than in human R2TP. We show that the interaction of AtRPAP3 with AtRuvBL2a and AtHSP90 occurs via a conserved mechanism. However, the distinct architectures of R2T and R2TP suggest differences in their functions and mechanisms.es_ES
dc.description.accrualMethodSes_ES
dc.description.bibliographicCitationPalacios-Abella, A.; López-Perrote, A.; Boskovic, J.; Fonseca, S.; Urbez Lagunas, Cristina; Rubio, V.; Llorca, O.... (2025). The structure of the R2T complex reveals a different architecture from the related HSP90 cochaperone R2TP. Structure. 33(4):740-752. https://doi.org/10.1016/j.str.2025.01.023es_ES
dc.description.issue4es_ES
dc.description.referencesSchopf, F. H., Biebl, M. M., & Buchner, J. (2017). The HSP90 chaperone machinery. Nature Reviews Molecular Cell Biology, 18(6), 345-360. https://doi.org/10.1038/nrm.2017.20es_ES
dc.description.referencesQueitsch, C., Sangster, T. A., & Lindquist, S. (2002). Hsp90 as a capacitor of phenotypic variation. Nature, 417(6889), 618-624. https://doi.org/10.1038/nature749es_ES
dc.description.referencesHoury, W. A., Bertrand, E., & Coulombe, B. (2018). The PAQosome, an R2TP-Based Chaperone for Quaternary Structure Formation. Trends in Biochemical Sciences, 43(1), 4-9. https://doi.org/10.1016/j.tibs.2017.11.001es_ES
dc.description.referencesZhao, R., Davey, M., Hsu, Y.-C., Kaplanek, P., Tong, A., Parsons, A. B., Krogan, N., Cagney, G., Mai, D., Greenblatt, J., Boone, C., Emili, A., & Houry, W. A. (2005). Navigating the Chaperone Network: An Integrative Map of Physical and Genetic Interactions Mediated by the Hsp90 Chaperone. Cell, 120(5), 715-727. https://doi.org/10.1016/j.cell.2004.12.024es_ES
dc.description.referencesNano, N., & Houry, W. A. (2013). Chaperone-like activity of the AAA+ proteins Rvb1 and Rvb2 in the assembly of various complexes. Philosophical Transactions of the Royal Society B: Biological Sciences, 368(1617), 20110399. https://doi.org/10.1098/rstb.2011.0399es_ES
dc.description.referencesKanemaki, M., Makino, Y., Yoshida, T., Kishimoto, T., Koga, A., Yamamoto, K., Yamamoto, M., Moncollin, V., Egly, J.-M., Muramatsu, M., & Tamura, T.-a. (1997). Molecular Cloning of a Rat 49-kDa TBP-Interacting Protein (TIP49) That Is Highly Homologous to the Bacterial RuvB. Biochemical and Biophysical Research Communications, 235(1), 64-68. https://doi.org/10.1006/bbrc.1997.6729es_ES
dc.description.referencesMajerská, J., Schrumpfová, P. P., Dokládal, L., Schořová, Š., Stejskal, K., Obořil, M., Honys, D., Kozáková, L., Polanská, P. S., & Sýkorová, E. (2016). Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo. Protoplasma, 254(4), 1547-1562. https://doi.org/10.1007/s00709-016-1042-3es_ES
dc.description.referencesHolt, B. F., Boyes, D. C., Ellerström, M., Siefers, N., Wiig, A., Kauffman, S., Grant, M. R., & Dangl, J. L. (2002). An Evolutionarily Conserved Mediator of Plant Disease Resistance Gene Function Is Required for Normal Arabidopsis Development. Developmental Cell, 2(6), 807-817. https://doi.org/10.1016/s1534-5807(02)00174-0es_ES
dc.description.referencesDauden, M. I., López-Perrote, A., & Llorca, O. (2021). RUVBL1–RUVBL2 AAA-ATPase: a versatile scaffold for multiple complexes and functions. Current Opinion in Structural Biology, 67, 78-85. https://doi.org/10.1016/j.sbi.2020.08.010es_ES
dc.description.referencesSilva, S. T. N., Brito, J. A., Arranz, R., Sorzano, C. Ó. S., Ebel, C., Doutch, J., Tully, M. D., Carazo, J.-M., Carrascosa, J. L., Matias, P. M., & Bandeiras, T. M. (2018). X-ray structure of full-length human RuvB-Like 2 – mechanistic insights into coupling between ATP binding and mechanical action. Scientific Reports, 8(1). https://doi.org/10.1038/s41598-018-31997-zes_ES
dc.description.referencesMatias, P. M., Gorynia, S., Donner, P., & Carrondo, M. A. (2006). Crystal Structure of the Human AAA+ Protein RuvBL1. Journal of Biological Chemistry, 281(50), 38918-38929. https://doi.org/10.1074/jbc.m605625200es_ES
dc.description.referencesIzumi, N., Yamashita, A., Iwamatsu, A., Kurata, R., Nakamura, H., Saari, B., Hirano, H., Anderson, P., & Ohno, S. (2010). AAA+ Proteins RUVBL1 and RUVBL2 Coordinate PIKK Activity and Function in Nonsense-Mediated mRNA Decay. Science Signaling, 3(116). https://doi.org/10.1126/scisignal.2000468es_ES
dc.description.referencesAssimon, V. A., Tang, Y., Vargas, J. D., Lee, G. J., Wu, Z. Y., Lou, K., Yao, B., Menon, M.-K., Pios, A., Perez, K. C., Madriaga, A., Buchowiecki, P. K., Rolfe, M., Shawver, L., Jiao, X., Le Moigne, R., Zhou, H.-J., & Anderson, D. J. (2019). CB-6644 Is a Selective Inhibitor of the RUVBL1/2 Complex with Anticancer Activity. ACS Chemical Biology, 14(2), 236-244. https://doi.org/10.1021/acschembio.8b00904es_ES
dc.description.referencesCandela-Ferre, J., Diego-Martin, B., Pérez-Alemany, J., & Gallego-Bartolomé, J. (2024). Mind the gap: Epigenetic regulation of chromatin accessibility in plants. Plant Physiology, 194(4), 1998-2016. https://doi.org/10.1093/plphys/kiae024es_ES
dc.description.referencesJeronimo, C., Forget, D., Bouchard, A., Li, Q., Chua, G., Poitras, C., Thérien, C., Bergeron, D., Bourassa, S., Greenblatt, J., Chabot, B., Poirier, G. G., Hughes, T. R., Blanchette, M., Price, D. H., & Coulombe, B. (2007). Systematic Analysis of the Protein Interaction Network for the Human Transcription Machinery Reveals the Identity of the 7SK Capping Enzyme. Molecular Cell, 27(2), 262-274. https://doi.org/10.1016/j.molcel.2007.06.027es_ES
dc.description.referencesMartino, F., Pal, M., Muñoz-Hernández, H., Rodríguez, C. F., Núñez-Ramírez, R., Gil-Carton, D., Degliesposti, G., Skehel, J. M., Roe, S. M., Prodromou, C., Pearl, L. H., & Llorca, O. (2018). Author Correction: RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex. Nature Communications, 9(1). https://doi.org/10.1038/s41467-018-05546-1es_ES
dc.description.referencesAntonio, L. M., Martins, G. H., Aragão, A. Z. B., Quel, N. G., Zazeri, G., Houry, W. A., & Ramos, C. H. I. (2023). Unveiling the Role of Sorghum RPAP3 in the Function of R2TP Complex: Insights into Protein Assembly in Plants. Plants, 12(16), 2925. https://doi.org/10.3390/plants12162925es_ES
dc.description.referencesHořejší, Z., Stach, L., Flower, Thomas G., Joshi, D., Flynn, H., Skehel, J.  ., O’Reilly, Nicola J., Ogrodowicz, Roksana W., Smerdon, Stephen J., & Boulton, Simon J. (2014). Phosphorylation-Dependent PIH1D1 Interactions Define Substrate Specificity of the R2TP Cochaperone Complex. Cell Reports, 7(1), 19-26. https://doi.org/10.1016/j.celrep.2014.03.013es_ES
dc.description.referencesMaurizy, C., Quinternet, M., Abel, Y., Verheggen, C., Santo, P. E., Bourguet, M., C.F. Paiva, A., Bragantini, B., Chagot, M.-E., Robert, M.-C., Abeza, C., Fabre, P., Fort, P., Vandermoere, F., M.F. Sousa, P., Rain, J.-C., Charpentier, B., Cianférani, S., Bandeiras, T. M., et al. (2018). The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones. Nature Communications, 9(1). https://doi.org/10.1038/s41467-018-04431-1es_ES
dc.description.referencesSeraphim, T. V., Nano, N., Cheung, Y. W. S., Aluksanasuwan, S., Colleti, C., Mao, Y.-Q., Bhandari, V., Young, G., Höll, L., Phanse, S., Gordiyenko, Y., Southworth, D. R., Robinson, C. V., Thongboonkerd, V., Gava, L. M., Borges, J. C., Babu, M., Barbosa, L. R. S., Ramos, C. H. I., et al. (2022). Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes. Structure, 30(1), 156-171. https://doi.org/10.1016/j.str.2021.08.002es_ES
dc.description.referencesEwens, Caroline A., Su, M., Zhao, L., Nano, N., Houry, Walid A., & Southworth, Daniel R. (2016). Architecture and Nucleotide-Dependent Conformational Changes of the Rvb1-Rvb2 AAA+ Complex Revealed by Cryoelectron Microscopy. Structure, 24(5), 657-666. https://doi.org/10.1016/j.str.2016.03.018es_ES
dc.description.referencesLópez-Perrote, A., Muñoz-Hernández, H., Gil, D., & Llorca, O. (2012). Conformational transitions regulate the exposure of a DNA-binding domain in the RuvBL1–RuvBL2 complex. Nucleic Acids Research, 40(21), 11086-11099. https://doi.org/10.1093/nar/gks871es_ES
dc.description.referencesMuñoz-Hernández, H., Pal, M., Rodríguez, C. F., Fernandez-Leiro, R., Prodromou, C., Pearl, L. H., & Llorca, O. (2019). Structural mechanism for regulation of the AAA-ATPases RUVBL1-RUVBL2 in the R2TP co-chaperone revealed by cryo-EM. Science Advances, 5(5). https://doi.org/10.1126/sciadv.aaw1616es_ES
dc.description.referencesRivera-Calzada, A., Pal, M., Muñoz-Hernández, H., Luque-Ortega, J. R., Gil-Carton, D., Degliesposti, G., Skehel, J. M., Prodromou, C., Pearl, L. H., & Llorca, O. (2017). The Structure of the R2TP Complex Defines a Platform for Recruiting Diverse Client Proteins to the HSP90 Molecular Chaperone System. Structure, 25(7), 1145-1152. https://doi.org/10.1016/j.str.2017.05.016es_ES
dc.description.referencesJeganathan, A., Leong, V., Zhao, L., Huen, J., Nano, N., Houry, W. A., & Ortega, J. (2015). Yeast Rvb1 and Rvb2 Proteins Oligomerize As a Conformationally Variable Dodecamer with Low Frequency. Journal of Molecular Biology, 427(10), 1875-1886. https://doi.org/10.1016/j.jmb.2015.01.010es_ES
dc.description.referencesLakomek, K., Stoehr, G., Tosi, A., Schmailzl, M., & Hopfner, K.-P. (2015). Structural Basis for Dodecameric Assembly States and Conformational Plasticity of the Full-Length AAA+ ATPases Rvb1·Rvb2. Structure, 23(3), 483-495. https://doi.org/10.1016/j.str.2014.12.015es_ES
dc.description.referencesCloutier, P., Poitras, C., Faubert, D., Bouchard, A., Blanchette, M., Gauthier, M.-S., & Coulombe, B. (2019). Upstream ORF-Encoded ASDURF Is a Novel Prefoldin-like Subunit of the PAQosome. Journal of Proteome Research, 19(1), 18-27. https://doi.org/10.1021/acs.jproteome.9b00599es_ES
dc.description.referencesCloutier, P., Poitras, C., Durand, M., Hekmat, O., Fiola-Masson, É., Bouchard, A., Faubert, D., Chabot, B., & Coulombe, B. (2017). R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 to regulate assembly of U5 small nuclear ribonucleoprotein. Nature Communications, 8(1). https://doi.org/10.1038/ncomms15615es_ES
dc.description.referencesCloutier, P., Al-Khoury, R., Lavallée-Adam, M., Faubert, D., Jiang, H., Poitras, C., Bouchard, A., Forget, D., Blanchette, M., & Coulombe, B. (2009). High-resolution mapping of the protein interaction network for the human transcription machinery and affinity purification of RNA polymerase II-associated complexes. Methods, 48(4), 381-386. https://doi.org/10.1016/j.ymeth.2009.05.005es_ES
dc.description.referencesBoulon, S., Pradet-Balade, B., Verheggen, C., Molle, D., Boireau, S., Georgieva, M., Azzag, K., Robert, M.-C., Ahmad, Y., Neel, H., Lamond, A. I., & Bertrand, E. (2010). HSP90 and Its R2TP/Prefoldin-like Cochaperone Are Involved in the Cytoplasmic Assembly of RNA Polymerase II. Molecular Cell, 39(6), 912-924. https://doi.org/10.1016/j.molcel.2010.08.023es_ES
dc.description.referencesGómez‐Mínguez, Y., Palacios‐Abella, A., Costigliolo‐Rojas, C., Barber, M., Hernández‐Villa, L., Úrbez, C., & Alabadí, D. (2024). The prefoldin‐like protein <scp>AtURI</scp> exhibits characteristics of intrinsically disordered proteins. FEBS Letters, 598(5), 556-570. Portico. https://doi.org/10.1002/1873-3468.14811es_ES
dc.description.referencesBlanco-Touriñán, N., Esteve-Bruna, D., Serrano-Mislata, A., Esquinas-Ariza, R. M., Resentini, F., Forment, J., Carrasco-López, C., Novella-Rausell, C., Palacios-Abella, A., Carrasco, P., Salinas, J., Blázquez, M. Á., & Alabadí, D. (2021). A genetic approach reveals different modes of action of prefoldins. Plant Physiology, 187(3), 1534-1550. https://doi.org/10.1093/plphys/kiab348es_ES
dc.description.referencesVan Leene, J., Eeckhout, D., Cannoot, B., De Winne, N., Persiau, G., Van De Slijke, E., Vercruysse, L., Dedecker, M., Verkest, A., Vandepoele, K., Martens, L., Witters, E., Gevaert, K., & De Jaeger, G. (2014). An improved toolbox to unravel the plant cellular machinery by tandem affinity purification of Arabidopsis protein complexes. Nature Protocols, 10(1), 169-187. https://doi.org/10.1038/nprot.2014.199es_ES
dc.description.referencesSchořová, Š., Fajkus, J., Záveská Drábková, L., Honys, D., & Schrumpfová, P. P. (2019). The plant Pontin and Reptin homologues, Ruv<scp>BL</scp>1 and Ruv<scp>BL</scp>2a, colocalize with <scp>TERT</scp> and <scp>TRB</scp> proteins <i>in vivo</i>, and participate in telomerase biogenesis. The Plant Journal, 98(2), 195-212. Portico. https://doi.org/10.1111/tpj.14306es_ES
dc.description.referencesLópez-Perrote, A., Hug, N., González-Corpas, A., Rodríguez, C. F., Serna, M., García-Martín, C., Boskovic, J., Fernandez-Leiro, R., Caceres, J. F., & Llorca, O. (2020). Regulation of RUVBL1-RUVBL2 AAA-ATPases by the nonsense-mediated mRNA decay factor DHX34, as evidenced by Cryo-EM. eLife, 9. CLOCKSS. https://doi.org/10.7554/elife.63042es_ES
dc.description.referencesKrishna. (2001). The Hsp90 family of proteins in Arabidopsis thaliana. Cell Stress Chaperones. 6. doi:10.1379/1466-1268(2001)006<0238:THFOPI>2.0.CO;2.es_ES
dc.description.referencesSamaras. (2020). ProteomicsDB: A multi-omics and multi-organism resource for life science research. Nucleic Acids Res. 48.es_ES
dc.description.referencesSotta, N., Shantikumar, L., Sakamoto, T., Matsunaga, S., & Fujiwara, T. (2016). <i>TPR5</i>is involved in directional cell division and is essential for the maintenance of meristem cell organization in<i>Arabidopsis thaliana</i>. Journal of Experimental Botany, 67(8), 2401-2411. https://doi.org/10.1093/jxb/erw043es_ES
dc.description.referencesGorynia, S., Bandeiras, T. M., Pinho, F. G., McVey, C. E., Vonrhein, C., Round, A., Svergun, D. I., Donner, P., Matias, P. M., & Carrondo, M. A. (2011). Structural and functional insights into a dodecameric molecular machine – The RuvBL1/RuvBL2 complex. Journal of Structural Biology, 176(3), 279-291. https://doi.org/10.1016/j.jsb.2011.09.001es_ES
dc.description.referencesNiewiarowski, A., Bradley, Alison S., Gor, J., McKay, Adam R., Perkins, Stephen J., & Tsaneva, Irina R. (2010). Oligomeric assembly and interactions within the human RuvB-like RuvBL1 and RuvBL2 complexes. Biochemical Journal, 429(1), 113-125. https://doi.org/10.1042/bj20100489es_ES
dc.description.referencesGarcía-Martín, C., López-Perrote, A., Boskovic, J., & Llorca, O. (2024). Mechanism of allosteric inhibition of RUVBL1-RUVBL2 ATPase by the small molecule CB-6644. Cell Reports Physical Science, 5(6), 101982. https://doi.org/10.1016/j.xcrp.2024.101982es_ES
dc.description.referencesSerna, M., González-Corpas, A., Cabezudo, S., López-Perrote, A., Degliesposti, G., Zarzuela, E., Skehel, J., Muñoz, J., & Llorca, O. (2021). CryoEM of RUVBL1–RUVBL2–ZNHIT2, a complex that interacts with pre-mRNA-processing-splicing factor 8. Nucleic Acids Research, 50(2), 1128-1146. https://doi.org/10.1093/nar/gkab1267es_ES
dc.description.referencesHenri, J., Chagot, M.-E., Bourguet, M., Abel, Y., Terral, G., Maurizy, C., Aigueperse, C., Georgescauld, F., Vandermoere, F., Saint-Fort, R., Behm-Ansmant, I., Charpentier, B., Pradet-Balade, B., Verheggen, C., Bertrand, E., Meyer, P., Cianférani, S., Manival, X., & Quinternet, M. (2018). Deep Structural Analysis of RPAP3 and PIH1D1, Two Components of the HSP90 Co-chaperone R2TP Complex. Structure, 26(9), 1196-1209. https://doi.org/10.1016/j.str.2018.06.002es_ES
dc.description.referencesRoe, S. M., Prodromou, C., O’Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1999). Structural Basis for Inhibition of the Hsp90 Molecular Chaperone by the Antitumor Antibiotics Radicicol and Geldanamycin. Journal of Medicinal Chemistry, 42(2), 260-266. https://doi.org/10.1021/jm980403yes_ES
dc.description.referencesGano, J. J., & Simon, J. A. (2010). A Proteomic Investigation of Ligand-dependent HSP90 Complexes Reveals CHORDC1 as a Novel ADP-dependent HSP90-interacting Protein. Molecular &amp; Cellular Proteomics, 9(2), 255-270. https://doi.org/10.1074/mcp.m900261-mcp200es_ES
dc.description.referencesZhou, C. Y., Stoddard, C. I., Johnston, J. B., Trnka, M. J., Echeverria, I., Palovcak, E., Sali, A., Burlingame, A. L., Cheng, Y., & Narlikar, G. J. (2017). Regulation of Rvb1/Rvb2 by a Domain within the INO80 Chromatin Remodeling Complex Implicates the Yeast Rvbs as Protein Assembly Chaperones. Cell Reports, 19(10), 2033-2044. https://doi.org/10.1016/j.celrep.2017.05.029es_ES
dc.description.referencesEckert, K., Saliou, J.-M., Monlezun, L., Vigouroux, A., Atmane, N., Caillat, C., Quevillon-Chéruel, S., Madiona, K., Nicaise, M., Lazereg, S., Van Dorsselaer, A., Sanglier-Cianférani, S., Meyer, P., & Moréra, S. (2010). The Pih1-Tah1 Cochaperone Complex Inhibits Hsp90 Molecular Chaperone ATPase Activity. Journal of Biological Chemistry, 285(41), 31304-31312. https://doi.org/10.1074/jbc.m110.138263es_ES
dc.description.referencesLynham, J., & Houry, W. A. (2022). The Role of Hsp90-R2TP in Macromolecular Complex Assembly and Stabilization. Biomolecules, 12(8), 1045. https://doi.org/10.3390/biom12081045es_ES
dc.description.referencesToullec, D., Elías-Villalobos, A., Faux, C., Noly, A., Lledo, G., Séveno, M., & Helmlinger, D. (2021). The Hsp90 cochaperone TTT promotes cotranslational maturation of PIKKs prior to complex assembly. Cell Reports, 37(3), 109867. https://doi.org/10.1016/j.celrep.2021.109867es_ES
dc.description.referencesBowman, J. L., Kohchi, T., Yamato, K. T., Jenkins, J., Shu, S., Ishizaki, K., Yamaoka, S., Nishihama, R., Nakamura, Y., Berger, F., Adam, C., Aki, S. S., Althoff, F., Araki, T., Arteaga-Vazquez, M. A., Balasubrmanian, S., Barry, K., Bauer, D., Boehm, C. R., et al. (2017). Insights into Land Plant Evolution Garnered from the Marchantia polymorpha Genome. Cell, 171(2), 287-304. https://doi.org/10.1016/j.cell.2017.09.030es_ES
dc.description.referencesKoncz, C., & Schell, J. (1986). The promoter of TL-DNA gene 5 controls the tissue-specific expression of chimaeric genes carried by a novel type of Agrobacterium binary vector. Molecular and General Genetics MGG, 204(3), 383-396. https://doi.org/10.1007/bf00331014es_ES
dc.description.referencesBelda-Palazón, B., Ruiz, L., Martí, E., Tárraga, S., Tiburcio, A. F., Culiáñez, F., Farràs, R., Carrasco, P., & Ferrando, A. (2012). Aminopropyltransferases Involved in Polyamine Biosynthesis Localize Preferentially in the Nucleus of Plant Cells. PLoS ONE, 7(10), e46907. https://doi.org/10.1371/journal.pone.0046907es_ES
dc.description.referencesEarley, K. W., Haag, J. R., Pontes, O., Opper, K., Juehne, T., Song, K., & Pikaard, C. S. (2006). Gateway‐compatible vectors for plant functional genomics and proteomics. The Plant Journal, 45(4), 616-629. Portico. https://doi.org/10.1111/j.1365-313x.2005.02617.xes_ES
dc.description.referencesZivanov, J., Nakane, T., Forsberg, B. O., Kimanius, D., Hagen, W. J., Lindahl, E., & Scheres, S. H. (2018). New tools for automated high-resolution cryo-EM structure determination in RELION-3. eLife, 7. CLOCKSS. https://doi.org/10.7554/elife.42166es_ES
dc.description.referencesPunjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017). cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nature Methods, 14(3), 290-296. https://doi.org/10.1038/nmeth.4169es_ES
dc.description.referencesPettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004). UCSF Chimera—A visualization system for exploratory research and analysis. Journal of Computational Chemistry, 25(13), 1605-1612. Portico. https://doi.org/10.1002/jcc.20084es_ES
dc.description.referencesCroll, T. I. (2018). <i>ISOLDE</i>: a physically realistic environment for model building into low-resolution electron-density maps. Acta Crystallographica Section D Structural Biology, 74(6), 519-530. https://doi.org/10.1107/s2059798318002425es_ES
dc.description.referencesEmsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010). Features and development of <i>Coot</i>. Acta Crystallographica Section D Biological Crystallography, 66(4), 486-501. https://doi.org/10.1107/s0907444910007493es_ES
dc.description.referencesCurtis, M. D., & Grossniklaus, U. (2003). A Gateway Cloning Vector Set for High-Throughput Functional Analysis of Genes in Planta. Plant Physiology, 133(2), 462-469. https://doi.org/10.1104/pp.103.027979es_ES
dc.description.referencesEsteve-Bruna, D., Carrasco-López, C., Blanco-Touriñán, N., Iserte, J., Calleja-Cabrera, J., Perea-Resa, C., Úrbez, C., Carrasco, P., Yanovsky, M. J., Blázquez, M. A., Salinas, J., & Alabadí, D. (2020). Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis. Nucleic Acids Research, 48(11), 6280-6293. https://doi.org/10.1093/nar/gkaa354es_ES
dc.description.referencesAntosz, W., Pfab, A., Ehrnsberger, H. F., Holzinger, P., Köllen, K., Mortensen, S. A., Bruckmann, A., Schubert, T., Längst, G., Griesenbeck, J., Schubert, V., Grasser, M., & Grasser, K. D. (2017). The Composition of the Arabidopsis RNA Polymerase II Transcript Elongation Complex Reveals the Interplay between Elongation and mRNA Processing Factors. The Plant Cell, 29(4), 854-870. https://doi.org/10.1105/tpc.16.00735es_ES
dc.description.referencesGarcía-Nafría, J., Watson, J. F., & Greger, I. H. (2016). IVA cloning: A single-tube universal cloning system exploiting bacterial In Vivo Assembly. Scientific Reports, 6(1). https://doi.org/10.1038/srep27459es_ES
dc.description.referencesZheng, S. Q., Palovcak, E., Armache, J.-P., Verba, K. A., Cheng, Y., & Agard, D. A. (2017). MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nature Methods, 14(4), 331-332. https://doi.org/10.1038/nmeth.4193es_ES
dc.description.referencesZhang, K. (2016). Gctf: Real-time CTF determination and correction. Journal of Structural Biology, 193(1), 1-12. https://doi.org/10.1016/j.jsb.2015.11.003es_ES
dc.description.referencesYang, Z., Zeng, X., Zhao, Y., & Chen, R. (2023). AlphaFold2 and its applications in the fields of biology and medicine. Signal Transduction and Targeted Therapy, 8(1). https://doi.org/10.1038/s41392-023-01381-zes_ES
dc.description.referencesAfonine, P. V., Poon, B. K., Read, R. J., Sobolev, O. V., Terwilliger, T. C., Urzhumtsev, A., & Adams, P. D. (2018). Real-space refinement in <i>PHENIX</i> for cryo-EM and crystallography. Acta Crystallographica Section D Structural Biology, 74(6), 531-544. https://doi.org/10.1107/s2059798318006551es_ES
dc.description.referencesWebb. (2016). Comparative protein structure modeling using MODELLER. Curr. Protoc. Bioinformatics. 54.es_ES
dc.description.sponsorshipThe authors thank Prof. Toru Fujiwara (The University of Tokyo, Tokyo, Japan) for providing seeds of tpr5-2 and pAtRPAP3:AtRPAP3-GFP tpr5-2 Arabidopsis lines, and Johanne Le Coq and Carmen Garc & imath;a-Mart & imath;n for help in EM sample preparation and imaging. This research was funded by grants PID2019109925GB-I00 and PID2022-141447NB-I00 to D.A. and by grants PID2020114429RB-I00 and PID2023-146110NB-I00 to O.L. funded by the Spanish MCIN/AEI/10.13039/501100011033 and by the European Union Regional Development Fund (ERDF) "A way of making Europe". A.P.-A. was supported by a Ministerio de Educacion predoctoral contract (FPU17/05186). O.L. laboratory also had the support from the National Institute of Health Carlos III to CNIO. Cryo-EM data used in this work for the structure of R2T was obtained at the Diamond Light Source cryo-EM facility at the UK's National Electron Bio-imaging Center (eBIC) under BAG Proposal No BI26876 "Stop cancer-structural studies of macromolecular complexes involved in cancer by cryo-EM".es_ES
dc.description.upvformatpfin752es_ES
dc.description.upvformatpinicio740es_ES
dc.description.volume33es_ES
dc.identifier.doi10.1016/j.str.2025.01.023es_ES
dc.identifier.issn0969-2126es_ES
dc.identifier.pmid40015274es_ES
dc.identifier.urihttps://riunet.upv.es/handle/10251/234939
dc.languageIngléses_ES
dc.publisherElsevieres_ES
dc.relation.ispartofStructurees_ES
dc.relation.pasarelaS\581256es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-109925GB-I00/ES/PAPEL DE LAS PREFOLDIN-LIKE EN SEÑALIZACION AMBIENTAL Y HOMEOSTASIS DE PROTEINAS EN ARABIDOPSIS/es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2020-114429RB-I00/ES/BASES ESTRUCTURALES Y MOLECULARES DEL ENSAMBLAJE Y ACTIVACION DEL COMPLEJO MTORC1 POR EL SISTEMA CHAPERONA R2TP-HSP90 /es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-141447NB-I00/ES/REGULACION POST-TRANSCRIPCIONAL DE LA RESPUESTA DE LA PLANTA A ALTAS TEMPERATURAS POR EL COMPLEJO R2TP%2FPREFOLDIN-LIKE/es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2023-146110NB-I00/ES/BASES ESTRUCTURALES Y MECANISMOS EN EL ENSAMBLAJE Y ACTIVACION DE LAS QUINASAS DE LA FAMILIA PIKK/es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ME//FPU17%2F05186/es_ES
dc.relation.publisherversionhttps://doi.org/10.1016/j.str.2025.01.023es_ES
dc.rightsReconocimiento - No comercial - Sin obra derivada (by-nc-nd)es_ES
dc.rights.accessRightsAbiertoes_ES
dc.subjectR2TP complexes_ES
dc.subjectHSP90 cochaperonees_ES
dc.subjectArabidopsis thalianaes_ES
dc.subjectCryo-electron microscopyes_ES
dc.subjectAAA-ATPaseses_ES
dc.subjectProtein interactionses_ES
dc.titleThe structure of the R2T complex reveals a different architecture from the related HSP90 cochaperone R2TPes_ES
dc.typeArtículoes_ES
dc.type.versioninfo:eu-repo/semantics/publishedVersiones_ES
dspace.entity.typePublication
person.identifier247069
person.identifier266783
person.identifier.orcid0000-0001-9345-7322
person.identifier.orcid0000-0001-8492-6713
relation.isAuthorOfPublicationcff61cd3-5b61-4e1d-82a4-02ae85bed1d5
relation.isAuthorOfPublication1f621e29-53a4-48b8-9078-820c290fae99
relation.isAuthorOfPublication.latestForDiscoverycff61cd3-5b61-4e1d-82a4-02ae85bed1d5
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upv.uuidcc650ada-9a11-4816-91a1-a72df881b0b6es_ES

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