[{"ddc":["570"],"article_type":"original","publication_status":"published","author":[{"last_name":"Tluckova","id":"4AC7D980-F248-11E8-B48F-1D18A9856A87","first_name":"Katarina","full_name":"Tluckova, Katarina"},{"last_name":"Kaczmarek","id":"36FA4AFA-F248-11E8-B48F-1D18A9856A87","full_name":"Kaczmarek, Beata M","first_name":"Beata M"},{"last_name":"Testa Salmazo","id":"41F1F098-F248-11E8-B48F-1D18A9856A87","full_name":"Testa Salmazo, Anita P","first_name":"Anita P"},{"id":"2CB9DFE2-F248-11E8-B48F-1D18A9856A87","first_name":"Carrie A","full_name":"Bernecky, Carrie A","orcid":"0000-0003-0893-7036","last_name":"Bernecky"}],"oa_version":"Published Version","intvolume":"        32","APC_amount":"12348 EUR","month":"04","article_processing_charge":"Yes (in subscription journal)","year":"2025","oa":1,"publication":"Nature Structural & Molecular Biology","scopus_import":"1","department":[{"_id":"CaBe"}],"date_created":"2025-01-08T11:20:20Z","related_material":{"record":[{"status":"public","relation":"earlier_version","id":"14644"}]},"acknowledged_ssus":[{"_id":"LifeSc"},{"_id":"EM-Fac"},{"_id":"ScienComp"},{"_id":"PreCl"}],"has_accepted_license":"1","corr_author":"1","citation":{"ista":"Tluckova K, Kaczmarek BM, Testa Salmazo AP, Bernecky C. 2025. Mechanism of mammalian transcriptional repression by noncoding RNA. Nature Structural &#38; Molecular Biology. 32, 607–612.","mla":"Tluckova, Katarina, et al. “Mechanism of Mammalian Transcriptional Repression by Noncoding RNA.” <i>Nature Structural &#38; Molecular Biology</i>, vol. 32, Springer Nature, 2025, pp. 607–12, doi:<a href=\"https://doi.org/10.1038/s41594-024-01448-7\">10.1038/s41594-024-01448-7</a>.","ama":"Tluckova K, Kaczmarek BM, Testa Salmazo AP, Bernecky C. Mechanism of mammalian transcriptional repression by noncoding RNA. <i>Nature Structural &#38; Molecular Biology</i>. 2025;32:607-612. doi:<a href=\"https://doi.org/10.1038/s41594-024-01448-7\">10.1038/s41594-024-01448-7</a>","short":"K. Tluckova, B.M. Kaczmarek, A.P. Testa Salmazo, C. Bernecky, Nature Structural &#38; Molecular Biology 32 (2025) 607–612.","ieee":"K. Tluckova, B. M. Kaczmarek, A. P. Testa Salmazo, and C. Bernecky, “Mechanism of mammalian transcriptional repression by noncoding RNA,” <i>Nature Structural &#38; Molecular Biology</i>, vol. 32. Springer Nature, pp. 607–612, 2025.","apa":"Tluckova, K., Kaczmarek, B. M., Testa Salmazo, A. P., &#38; Bernecky, C. (2025). Mechanism of mammalian transcriptional repression by noncoding RNA. <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-024-01448-7\">https://doi.org/10.1038/s41594-024-01448-7</a>","chicago":"Tluckova, Katarina, Beata M Kaczmarek, Anita P Testa Salmazo, and Carrie Bernecky. “Mechanism of Mammalian Transcriptional Repression by Noncoding RNA.” <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature, 2025. <a href=\"https://doi.org/10.1038/s41594-024-01448-7\">https://doi.org/10.1038/s41594-024-01448-7</a>."},"OA_type":"hybrid","quality_controlled":"1","OA_place":"publisher","volume":32,"publication_identifier":{"issn":["1545-9993"],"eissn":["1545-9985"]},"acknowledgement":"We thank the members of the Bernecky laboratory for helpful discussions and A. Hlavata for providing Pol II for use in the fluorescence anisotropy binding assay. We thank V.-V. Hodirnau for SerialEM data collection and support with EPU data collection. We thank D. Slade (Max Perutz Laboratories and Medical University of Vienna, Vienna, Austria) for the wild-type TFIIF expression plasmid. We thank N. Thompson and R. Burgess (McArdle Laboratory for Cancer Research, University of Wisconsin-Madison, Madison, WI, USA) for the 8WG16 hybridoma cell line. We thank C. Plaschka and M. Loose for critical reading of the manuscript. This work was supported by Austrian Science Fund (FWF) grant no. P34185 (DOI 10.55776/P34185) (C.B.). The funders had no role in study design, data collection and analysis, decision to publish or preparation of the manuscript. This research was further supported by the Scientific Service Units of ISTA through resources provided by the Laboratory Support Facility, Electron Microscopy Facility, Scientific Computing and the Preclinical Facility.","day":"01","date_published":"2025-04-01T00:00:00Z","fulldoi":"https://doi.org/10.1038/s41594-024-01448-7","file":[{"file_size":9306639,"date_updated":"2025-04-16T08:17:27Z","checksum":"2919b30b271f395888e880076a680d73","relation":"main_file","date_created":"2025-04-16T08:17:27Z","success":1,"creator":"dernst","access_level":"open_access","file_id":"19573","file_name":"2025_NatureStrucMolBiol_Tluckova.pdf","content_type":"application/pdf"}],"isi":1,"language":[{"iso":"eng"}],"external_id":{"isi":["001390268000001"],"pmid":["39762629"]},"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)"},"file_date_updated":"2025-04-16T08:17:27Z","abstract":[{"lang":"eng","text":"Transcription by RNA polymerase II (Pol II) can be repressed by noncoding RNA, including the human RNA Alu. However, the mechanism by which endogenous RNAs repress transcription remains unclear. Here we present cryogenic-electron microscopy structures of Pol II bound to Alu RNA, which reveal that Alu RNA mimics how DNA and RNA bind to Pol II during transcription elongation. Further, we show how distinct domains of the general transcription factor TFIIF control repressive activity. Together, we reveal how a noncoding RNA can regulate mammalian gene expression."}],"title":"Mechanism of mammalian transcriptional repression by noncoding RNA","page":"607-612","date_updated":"2025-11-20T10:28:36Z","pmid":1,"project":[{"grant_number":"P34185","name":"Regulation of mammalian transcription by noncoding RNA","_id":"c08a6700-5a5b-11eb-8a69-82a722b2bc30"}],"type":"journal_article","status":"public","_id":"18778","doi":"10.1038/s41594-024-01448-7","publisher":"Springer Nature","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87"},{"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)"},"day":"01","date_published":"2025-02-01T00:00:00Z","language":[{"iso":"eng"}],"fulldoi":"https://doi.org/10.1038/s41594-024-01390-8","file":[{"relation":"main_file","date_created":"2025-04-23T07:02:33Z","success":1,"creator":"dernst","file_size":13724041,"checksum":"c641ad94afb28917b20425db676fc3ee","date_updated":"2025-04-23T07:02:33Z","content_type":"application/pdf","file_name":"2025_NatureStrucBio_Obr.pdf","access_level":"open_access","file_id":"19608"}],"isi":1,"external_id":{"isi":["001306564000001"],"pmid":["39242978"],"oaworkid":["W4402316284"]},"status":"public","_id":"17884","type":"journal_article","project":[{"grant_number":"P31445","_id":"26736D6A-B435-11E9-9278-68D0E5697425","call_identifier":"FWF","name":"Structural conservation and diversity in retroviral capsid"},{"_id":"9B9C98E0-BA93-11EA-9121-9846C619BF3A","name":"Structural characterization of spumavirus capsid assemblies to understand conserved Ortervirales assembly mechanisms","grant_number":"25762"}],"doi":"10.1038/s41594-024-01390-8","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Springer Nature","oaworkid":1,"abstract":[{"lang":"eng","text":"Human T cell leukemia virus type 1 (HTLV-1) immature particles differ in morphology from other retroviruses, suggesting a distinct way of assembly. Here we report the results of cryo-electron tomography studies of HTLV-1 virus-like particles assembled in vitro, as well as derived from cells. This work shows that HTLV-1 uses a distinct mechanism of Gag–Gag interactions to form the immature viral lattice. Analysis of high-resolution structural information from immature capsid (CA) tubular arrays reveals that the primary stabilizing component in HTLV-1 is the N-terminal domain of CA. Mutagenesis analysis supports this observation. This distinguishes HTLV-1 from other retroviruses, in which the stabilization is provided primarily by the C-terminal domain of CA. These results provide structural details of the quaternary arrangement of Gag for an immature deltaretrovirus and this helps explain why HTLV-1 particles are morphologically distinct."}],"file_date_updated":"2025-04-23T07:02:33Z","title":"Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice","page":"268-276","date_updated":"2026-03-16T12:55:18Z","pmid":1,"APC_amount":"12348 EUR","intvolume":"        32","oa_version":"Published Version","month":"02","oa":1,"year":"2025","article_processing_charge":"Yes (in subscription journal)","ddc":["570"],"author":[{"last_name":"Obr","id":"4741CA5A-F248-11E8-B48F-1D18A9856A87","full_name":"Obr, Martin","orcid":"0000-0003-1756-6564","first_name":"Martin"},{"last_name":"Percipalle","first_name":"Mathias","full_name":"Percipalle, Mathias","id":"4986e21c-eb97-11eb-a6c2-a4ef0b629971"},{"last_name":"Chernikova","id":"7dbaf460-fa9e-11eb-b0ca-bc7c7ff21ad0","first_name":"Darya","full_name":"Chernikova, Darya"},{"first_name":"Huixin","full_name":"Yang, Huixin","last_name":"Yang"},{"last_name":"Thader","first_name":"Andreas","full_name":"Thader, Andreas","id":"3A18A7B8-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Pinke","first_name":"Gergely","full_name":"Pinke, Gergely","id":"4D5303E6-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Porley","first_name":"Dario J","full_name":"Porley, Dario J","id":"2FD6EA6C-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Louis M.","full_name":"Mansky, Louis M.","last_name":"Mansky"},{"first_name":"Robert A.","full_name":"Dick, Robert A.","last_name":"Dick"},{"orcid":"0000-0003-4790-8078","full_name":"Schur, Florian KM","first_name":"Florian KM","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","last_name":"Schur"}],"article_type":"original","publication_status":"published","OA_place":"publisher","quality_controlled":"1","OA_type":"hybrid","volume":32,"publication_identifier":{"issn":["1545-9993"],"eissn":["1545-9985"]},"acknowledgement":"This work was funded by the Institute of Science and Technology Austria (ISTA) and the Austrian Science Fund (grant P31445 to F.K.M.S.). Access to high-resolution cryo-ET data acquisition at European Molecular Biology Laboratory (EMBL) Heidelberg was supported through the EMBL cryo-EM platform. We thank V.-V. Hodirnau at ISTA and W. Hagen and F. Weis at EMBL Heidelberg for support in cryo-ET data acquisition. This research was also supported by the scientific service units of ISTA through resources provided by Scientific Computing, the Life Science Facility, and the EM Facility. L.M.M. was supported by National Institutes of Health grants R01 GM151775 and R21 DE032878 and by the University of Minnesota Masonic Cancer Center. D.P. was supported by the DOC doctoral fellowship program of the Austrian Academy of Sciences. R.A.D was supported by the National Institute of Allergy and Infectious Diseases (grant R01AI147890). The funders had no role in study design, data collection and analysis, decision to publish or preparation of the manuscript. Specifically, we also want to thank A. Schlögl for computational support and J. Hansen and V. Vogt for critical comments on the manuscript. We also thank the other members of the Schur lab for helpful discussions and experimental advice.","publication":"Nature Structural & Molecular Biology","date_created":"2024-09-08T10:29:06Z","scopus_import":"1","department":[{"_id":"FlSc"},{"_id":"LeSa"}],"has_accepted_license":"1","acknowledged_ssus":[{"_id":"ScienComp"},{"_id":"LifeSc"},{"_id":"EM-Fac"}],"citation":{"chicago":"Obr, Martin, Mathias Percipalle, Darya Chernikova, Huixin Yang, Andreas Thader, Gergely Pinke, Darío Porley Esteves, Louis M. Mansky, Robert A. Dick, and Florian KM Schur. “Distinct Stabilization of the Human T Cell Leukemia Virus Type 1 Immature Gag Lattice.” <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature, 2025. <a href=\"https://doi.org/10.1038/s41594-024-01390-8\">https://doi.org/10.1038/s41594-024-01390-8</a>.","apa":"Obr, M., Percipalle, M., Chernikova, D., Yang, H., Thader, A., Pinke, G., … Schur, F. K. (2025). Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice. <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-024-01390-8\">https://doi.org/10.1038/s41594-024-01390-8</a>","ieee":"M. Obr <i>et al.</i>, “Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice,” <i>Nature Structural &#38; Molecular Biology</i>, vol. 32. Springer Nature, pp. 268–276, 2025.","short":"M. Obr, M. Percipalle, D. Chernikova, H. Yang, A. Thader, G. Pinke, D. Porley Esteves, L.M. Mansky, R.A. Dick, F.K. Schur, Nature Structural &#38; Molecular Biology 32 (2025) 268–276.","ama":"Obr M, Percipalle M, Chernikova D, et al. Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice. <i>Nature Structural &#38; Molecular Biology</i>. 2025;32:268-276. doi:<a href=\"https://doi.org/10.1038/s41594-024-01390-8\">10.1038/s41594-024-01390-8</a>","mla":"Obr, Martin, et al. “Distinct Stabilization of the Human T Cell Leukemia Virus Type 1 Immature Gag Lattice.” <i>Nature Structural &#38; Molecular Biology</i>, vol. 32, Springer Nature, 2025, pp. 268–76, doi:<a href=\"https://doi.org/10.1038/s41594-024-01390-8\">10.1038/s41594-024-01390-8</a>.","ista":"Obr M, Percipalle M, Chernikova D, Yang H, Thader A, Pinke G, Porley Esteves D, Mansky LM, Dick RA, Schur FK. 2025. Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice. Nature Structural &#38; Molecular Biology. 32, 268–276."},"corr_author":"1"},{"doi":"10.1038/s41594-023-01201-6","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","publisher":"Springer Nature","status":"public","_id":"14979","type":"journal_article","project":[{"_id":"26736D6A-B435-11E9-9278-68D0E5697425","name":"Structural conservation and diversity in retroviral capsid","call_identifier":"FWF","grant_number":"P31445"}],"page":"1114-1123","date_updated":"2026-04-07T12:59:44Z","pmid":1,"abstract":[{"lang":"eng","text":"Poxviruses are among the largest double-stranded DNA viruses, with members such as variola virus, monkeypox virus and the vaccination strain vaccinia virus (VACV). Knowledge about the structural proteins that form the viral core has remained sparse. While major core proteins have been annotated via indirect experimental evidence, their structures have remained elusive and they could not be assigned to individual core features. Hence, which proteins constitute which layers of the core, such as the palisade layer and the inner core wall, has remained enigmatic. Here we show, using a multi-modal cryo-electron microscopy (cryo-EM) approach in combination with AlphaFold molecular modeling, that trimers formed by the cleavage product of VACV protein A10 are the key component of the palisade layer. This allows us to place previously obtained descriptions of protein interactions within the core wall into perspective and to provide a detailed model of poxvirus core architecture. Importantly, we show that interactions within A10 trimers are likely generalizable over members of orthopox- and parapoxviruses."}],"file_date_updated":"2024-07-22T11:27:22Z","title":"Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade layer in poxvirus cores","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)"},"keyword":["Molecular Biology","Structural Biology"],"language":[{"iso":"eng"}],"isi":1,"fulldoi":"https://doi.org/10.1038/s41594-023-01201-6","file":[{"file_id":"17307","access_level":"open_access","content_type":"application/pdf","file_name":"2024_NatureStrucBio_Datler.pdf","checksum":"bda7bf65d81455480efaed8ca293b0db","date_updated":"2024-07-22T11:27:22Z","file_size":17485494,"creator":"dernst","success":1,"date_created":"2024-07-22T11:27:22Z","relation":"main_file"}],"external_id":{"pmid":["38316877"],"isi":["001158144600002"]},"day":"01","date_published":"2024-07-01T00:00:00Z","acknowledgement":"We thank A. Bergthaler (Research Center for Molecular Medicine of the Austrian Academy of Sciences) for providing VACV WR. We thank A. Nicholas and his team at the ISTA proteomics facility, and S. Elefante at the ISTA Scientific Computing facility for their support. We also thank F. Fäßler, D. Porley, T. Muthspiel and other members of the Schur group for support and helpful discussions. We also thank D. Castaño-Díez for support with Dynamo. We thank D. Farrell for his help optimizing the Rosetta protocol to refine the atomic model into the cryo-EM map with symmetry.\r\n\r\nF.K.M.S. acknowledges support from ISTA and EMBO. F.K.M.S. also received support from the Austrian Science Fund (FWF) grant P31445. This publication has been made possible in part by CZI grant DAF2021-234754 and grant https://doi.org/10.37921/812628ebpcwg from the Chan Zuckerberg Initiative DAF, an advised fund of Silicon Valley Community Foundation (funder https://doi.org/10.13039/100014989) awarded to F.K.M.S.\r\n\r\nThis research was also supported by the Scientific Service Units (SSUs) of ISTA through resources provided by Scientific Computing (SciComp), the Life Science Facility (LSF), and the Electron Microscopy Facility (EMF). We also acknowledge the use of COSMIC45 and Colabfold46.","quality_controlled":"1","OA_place":"publisher","OA_type":"hybrid","publication_identifier":{"eissn":["1545-9985"],"issn":["1545-9993"]},"volume":31,"has_accepted_license":"1","acknowledged_ssus":[{"_id":"ScienComp"},{"_id":"LifeSc"},{"_id":"EM-Fac"}],"related_material":{"record":[{"relation":"dissertation_contains","status":"public","id":"18766"}],"link":[{"relation":"press_release","description":"News on ISTA Website","url":"https://ista.ac.at/en/news/down-to-the-core-of-poxviruses/"}]},"citation":{"ama":"Datler J, Hansen J, Thader A, et al. Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade layer in poxvirus cores. <i>Nature Structural &#38; Molecular Biology</i>. 2024;31:1114-1123. doi:<a href=\"https://doi.org/10.1038/s41594-023-01201-6\">10.1038/s41594-023-01201-6</a>","mla":"Datler, Julia, et al. “Multi-Modal Cryo-EM Reveals Trimers of Protein A10 to Form the Palisade Layer in Poxvirus Cores.” <i>Nature Structural &#38; Molecular Biology</i>, vol. 31, Springer Nature, 2024, pp. 1114–23, doi:<a href=\"https://doi.org/10.1038/s41594-023-01201-6\">10.1038/s41594-023-01201-6</a>.","ista":"Datler J, Hansen J, Thader A, Schlögl A, Bauer LW, Hodirnau V-V, Schur FK. 2024. Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade layer in poxvirus cores. Nature Structural &#38; Molecular Biology. 31, 1114–1123.","chicago":"Datler, Julia, Jesse Hansen, Andreas Thader, Alois Schlögl, Lukas W Bauer, Victor-Valentin Hodirnau, and Florian KM Schur. “Multi-Modal Cryo-EM Reveals Trimers of Protein A10 to Form the Palisade Layer in Poxvirus Cores.” <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature, 2024. <a href=\"https://doi.org/10.1038/s41594-023-01201-6\">https://doi.org/10.1038/s41594-023-01201-6</a>.","apa":"Datler, J., Hansen, J., Thader, A., Schlögl, A., Bauer, L. W., Hodirnau, V.-V., &#38; Schur, F. K. (2024). Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade layer in poxvirus cores. <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-023-01201-6\">https://doi.org/10.1038/s41594-023-01201-6</a>","ieee":"J. Datler <i>et al.</i>, “Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade layer in poxvirus cores,” <i>Nature Structural &#38; Molecular Biology</i>, vol. 31. Springer Nature, pp. 1114–1123, 2024.","short":"J. Datler, J. Hansen, A. Thader, A. Schlögl, L.W. Bauer, V.-V. Hodirnau, F.K. Schur, Nature Structural &#38; Molecular Biology 31 (2024) 1114–1123."},"corr_author":"1","publication":"Nature Structural & Molecular Biology","date_created":"2024-02-12T09:59:45Z","scopus_import":"1","department":[{"_id":"FlSc"},{"_id":"ScienComp"},{"_id":"EM-Fac"}],"year":"2024","oa":1,"article_processing_charge":"Yes (in subscription journal)","APC_amount":"11700 EUR","intvolume":"        31","oa_version":"Published Version","month":"07","author":[{"last_name":"Datler","id":"3B12E2E6-F248-11E8-B48F-1D18A9856A87","first_name":"Julia","orcid":"0000-0002-3616-8580","full_name":"Datler, Julia"},{"last_name":"Hansen","id":"1063c618-6f9b-11ec-9123-f912fccded63","first_name":"Jesse","full_name":"Hansen, Jesse","orcid":"0000-0001-7967-2085"},{"full_name":"Thader, Andreas","first_name":"Andreas","id":"3A18A7B8-F248-11E8-B48F-1D18A9856A87","last_name":"Thader"},{"last_name":"Schlögl","id":"45BF87EE-F248-11E8-B48F-1D18A9856A87","full_name":"Schlögl, Alois","orcid":"0000-0002-5621-8100","first_name":"Alois"},{"full_name":"Bauer, Lukas W","first_name":"Lukas W","id":"0c894dcf-897b-11ed-a09c-8186353224b0","last_name":"Bauer"},{"last_name":"Hodirnau","full_name":"Hodirnau, Victor-Valentin","orcid":"0000-0003-3904-947X","first_name":"Victor-Valentin","id":"3661B498-F248-11E8-B48F-1D18A9856A87"},{"id":"48AD8942-F248-11E8-B48F-1D18A9856A87","full_name":"Schur, Florian KM","orcid":"0000-0003-4790-8078","first_name":"Florian KM","last_name":"Schur"}],"publication_status":"published","article_type":"original","ddc":["570"]},{"month":"05","oa_version":"Published Version","intvolume":"        31","main_file_link":[{"url":"https://doi.org/10.1038/s41594-024-01239-0","open_access":"1"}],"oa":1,"year":"2024","article_processing_charge":"Yes (in subscription journal)","author":[{"full_name":"Kobayashi, Wataru","first_name":"Wataru","last_name":"Kobayashi"},{"first_name":"Anna H.","full_name":"Sappler, Anna H.","last_name":"Sappler"},{"last_name":"Bollschweiler","full_name":"Bollschweiler, Daniel","first_name":"Daniel"},{"full_name":"Kümmecke, Maximilian","first_name":"Maximilian","last_name":"Kümmecke"},{"last_name":"Basquin","full_name":"Basquin, Jérôme","first_name":"Jérôme"},{"last_name":"Arslantas","id":"36978b4e-2966-11ef-a72f-b3740ef1cd11","full_name":"Arslantas, Eda Nur","first_name":"Eda Nur"},{"last_name":"Ruangroengkulrith","first_name":"Siwat","full_name":"Ruangroengkulrith, Siwat"},{"last_name":"Hornberger","first_name":"Renate","full_name":"Hornberger, Renate"},{"first_name":"Karl","full_name":"Duderstadt, Karl","last_name":"Duderstadt"},{"first_name":"Kikuë","full_name":"Tachibana, Kikuë","last_name":"Tachibana"}],"article_type":"original","publication_status":"published","publication_identifier":{"eissn":["1545-9985"],"issn":["1545-9993"]},"volume":31,"quality_controlled":"1","OA_place":"publisher","OA_type":"hybrid","acknowledgement":"We are very grateful to K. Abe, L. G. Hernandez, C. Kobayashi, K. Straßer and M. Zaczek for their contributions and technical support. We thank N. Thomä for advice on SeEN-seq. We are grateful to A. Musacchio for insightful discussions. We thank J.-M. Peters for critical reading of the manuscript and all members of K.T.’s laboratory for discussions. We thank T. Schäfer at the cryo-EM facility for assistance in cryo-EM data collection, and R. H. Kim for sequencing at the NGS facility, MPIB. K.T. is an Honorary Professor at the Department of Biology, Ludwig-Maximilians-University, Munich. Funding: European Research Council grant ERC-CoG-818556 TotipotentZygotChrom (K.T.). European Research Council grant ERC-StG-804098 ReplisomeBypass (K.D.). Max Planck Society (K.T., K.D.).","date_created":"2024-12-11T09:10:54Z","scopus_import":"1","publication":"Nature Structural & Molecular Biology","citation":{"short":"W. Kobayashi, A.H. Sappler, D. Bollschweiler, M. Kümmecke, J. Basquin, E.N. Arslantas, S. Ruangroengkulrith, R. Hornberger, K. Duderstadt, K. Tachibana, Nature Structural &#38; Molecular Biology 31 (2024) 757–766.","apa":"Kobayashi, W., Sappler, A. H., Bollschweiler, D., Kümmecke, M., Basquin, J., Arslantas, E. N., … Tachibana, K. (2024). Nucleosome-bound NR5A2 structure reveals pioneer factor mechanism by DNA minor groove anchor competition. <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-024-01239-0\">https://doi.org/10.1038/s41594-024-01239-0</a>","ieee":"W. Kobayashi <i>et al.</i>, “Nucleosome-bound NR5A2 structure reveals pioneer factor mechanism by DNA minor groove anchor competition,” <i>Nature Structural &#38; Molecular Biology</i>, vol. 31. Springer Nature, pp. 757–766, 2024.","chicago":"Kobayashi, Wataru, Anna H. Sappler, Daniel Bollschweiler, Maximilian Kümmecke, Jérôme Basquin, Eda Nur Arslantas, Siwat Ruangroengkulrith, Renate Hornberger, Karl Duderstadt, and Kikuë Tachibana. “Nucleosome-Bound NR5A2 Structure Reveals Pioneer Factor Mechanism by DNA Minor Groove Anchor Competition.” <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature, 2024. <a href=\"https://doi.org/10.1038/s41594-024-01239-0\">https://doi.org/10.1038/s41594-024-01239-0</a>.","ista":"Kobayashi W, Sappler AH, Bollschweiler D, Kümmecke M, Basquin J, Arslantas EN, Ruangroengkulrith S, Hornberger R, Duderstadt K, Tachibana K. 2024. Nucleosome-bound NR5A2 structure reveals pioneer factor mechanism by DNA minor groove anchor competition. Nature Structural &#38; Molecular Biology. 31, 757–766.","mla":"Kobayashi, Wataru, et al. “Nucleosome-Bound NR5A2 Structure Reveals Pioneer Factor Mechanism by DNA Minor Groove Anchor Competition.” <i>Nature Structural &#38; Molecular Biology</i>, vol. 31, Springer Nature, 2024, pp. 757–66, doi:<a href=\"https://doi.org/10.1038/s41594-024-01239-0\">10.1038/s41594-024-01239-0</a>.","ama":"Kobayashi W, Sappler AH, Bollschweiler D, et al. Nucleosome-bound NR5A2 structure reveals pioneer factor mechanism by DNA minor groove anchor competition. <i>Nature Structural &#38; Molecular Biology</i>. 2024;31:757-766. doi:<a href=\"https://doi.org/10.1038/s41594-024-01239-0\">10.1038/s41594-024-01239-0</a>"},"extern":"1","date_published":"2024-05-01T00:00:00Z","day":"01","language":[{"iso":"eng"}],"fulldoi":"https://doi.org/10.1038/s41594-024-01239-0","status":"public","_id":"18645","type":"journal_article","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Springer Nature","doi":"10.1038/s41594-024-01239-0","title":"Nucleosome-bound NR5A2 structure reveals pioneer factor mechanism by DNA minor groove anchor competition","abstract":[{"text":"Gene expression during natural and induced reprogramming is controlled by pioneer transcription factors that initiate transcription from closed chromatin. Nr5a2 is a key pioneer factor that regulates zygotic genome activation in totipotent embryos, pluripotency in embryonic stem cells and metabolism in adult tissues, but the mechanism of its pioneer activity remains poorly understood. Here, we present a cryo-electron microscopy structure of human NR5A2 bound to a nucleosome. The structure shows that the conserved carboxy-terminal extension (CTE) loop of the NR5A2 DNA-binding domain competes with a DNA minor groove anchor of the nucleosome and releases entry-exit site DNA. Mutational analysis showed that NR5A2 D159 of the CTE is dispensable for DNA binding but required for stable nucleosome association and persistent DNA ‘unwrapping’. These findings suggest that NR5A2 belongs to an emerging class of pioneer factors that can use DNA minor groove anchor competition to destabilize nucleosomes and facilitate gene expression during reprogramming.","lang":"eng"}],"page":"757-766","date_updated":"2024-12-11T10:56:35Z"},{"day":"01","date_published":"2024-07-01T00:00:00Z","external_id":{"isi":["001196897300001"],"pmid":["38575788"]},"language":[{"iso":"eng"}],"fulldoi":"https://doi.org/10.1038/s41594-024-01255-0","isi":1,"file":[{"access_level":"open_access","file_id":"15392","embargo":"2025-01-01","file_name":"megacomplex_submit_NSMB_withFigures.pdf","content_type":"application/pdf","file_size":24424729,"checksum":"21f05d188762acd7f49a97f3d09c8d9f","date_updated":"2025-01-01T23:30:03Z","date_created":"2024-05-14T11:57:56Z","relation":"main_file","creator":"lsazanov"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)"},"title":"SCAF1 drives the compositional diversity of mammalian respirasomes","abstract":[{"text":"Supercomplexes of the respiratory chain are established constituents of the oxidative phosphorylation system, but their role in mammalian metabolism has been hotly debated. Although recent studies have shown that different tissues/organs are equipped with specific sets of supercomplexes, depending on their metabolic needs, the notion that supercomplexes have a role in the regulation of metabolism has been challenged. However, irrespective of the mechanistic conclusions, the composition of various high molecular weight supercomplexes remains uncertain. Here, using cryogenic electron microscopy, we demonstrate that mammalian (mouse) tissues contain three defined types of ‘respirasome’, supercomplexes made of CI, CIII2 and CIV. The stoichiometry and position of CIV differs in the three respirasomes, of which only one contains the supercomplex-associated factor SCAF1, whose involvement in respirasome formation has long been contended. Our structures confirm that the ‘canonical’ respirasome (the C-respirasome, CICIII2CIV) does not contain SCAF1, which is instead associated to a different respirasome (the CS-respirasome), containing a second copy of CIV. We also identify an alternative respirasome (A-respirasome), with CIV bound to the ‘back’ of CI, instead of the ‘toe’. This structural characterization of mouse mitochondrial supercomplexes allows us to hypothesize a mechanistic basis for their specific role in different metabolic conditions.","lang":"eng"}],"file_date_updated":"2025-01-01T23:30:03Z","pmid":1,"page":"1061-1071","date_updated":"2025-11-24T08:35:04Z","status":"public","_id":"15323","project":[{"grant_number":"101020697","_id":"627abdeb-2b32-11ec-9570-ec31a97243d3","call_identifier":"H2020","name":"Structure and mechanism of respiratory chain molecular machines"}],"type":"journal_article","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Springer Nature","doi":"10.1038/s41594-024-01255-0","ddc":["572"],"author":[{"id":"3ED6AF16-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-5618-3449","full_name":"Vercellino, Irene","first_name":"Irene","last_name":"Vercellino"},{"first_name":"Leonid A","orcid":"0000-0002-0977-7989","full_name":"Sazanov, Leonid A","id":"338D39FE-F248-11E8-B48F-1D18A9856A87","last_name":"Sazanov"}],"article_type":"original","publication_status":"published","month":"07","intvolume":"        31","oa_version":"Submitted Version","oa":1,"year":"2024","article_processing_charge":"No","date_created":"2024-04-14T22:01:03Z","department":[{"_id":"LeSa"}],"scopus_import":"1","publication":"Nature Structural and Molecular Biology","citation":{"ieee":"I. Vercellino and L. A. Sazanov, “SCAF1 drives the compositional diversity of mammalian respirasomes,” <i>Nature Structural and Molecular Biology</i>, vol. 31. Springer Nature, pp. 1061–1071, 2024.","apa":"Vercellino, I., &#38; Sazanov, L. A. (2024). SCAF1 drives the compositional diversity of mammalian respirasomes. <i>Nature Structural and Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-024-01255-0\">https://doi.org/10.1038/s41594-024-01255-0</a>","short":"I. Vercellino, L.A. Sazanov, Nature Structural and Molecular Biology 31 (2024) 1061–1071.","chicago":"Vercellino, Irene, and Leonid A Sazanov. “SCAF1 Drives the Compositional Diversity of Mammalian Respirasomes.” <i>Nature Structural and Molecular Biology</i>. Springer Nature, 2024. <a href=\"https://doi.org/10.1038/s41594-024-01255-0\">https://doi.org/10.1038/s41594-024-01255-0</a>.","ista":"Vercellino I, Sazanov LA. 2024. SCAF1 drives the compositional diversity of mammalian respirasomes. Nature Structural and Molecular Biology. 31, 1061–1071.","ama":"Vercellino I, Sazanov LA. SCAF1 drives the compositional diversity of mammalian respirasomes. <i>Nature Structural and Molecular Biology</i>. 2024;31:1061-1071. doi:<a href=\"https://doi.org/10.1038/s41594-024-01255-0\">10.1038/s41594-024-01255-0</a>","mla":"Vercellino, Irene, and Leonid A. Sazanov. “SCAF1 Drives the Compositional Diversity of Mammalian Respirasomes.” <i>Nature Structural and Molecular Biology</i>, vol. 31, Springer Nature, 2024, pp. 1061–71, doi:<a href=\"https://doi.org/10.1038/s41594-024-01255-0\">10.1038/s41594-024-01255-0</a>."},"corr_author":"1","acknowledged_ssus":[{"_id":"EM-Fac"},{"_id":"LifeSc"},{"_id":"PreCl"},{"_id":"ScienComp"}],"has_accepted_license":"1","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/s41594-025-01721-3"}]},"volume":31,"ec_funded":1,"publication_identifier":{"eissn":["1545-9985"],"issn":["1545-9993"]},"quality_controlled":"1","acknowledgement":"Supercomplexes of the respiratory chain are established constituents of the oxidative phosphorylation system, but their role in mammalian metabolism has been hotly debated. Although recent studies have shown that different tissues/organs are equipped with specific sets of supercomplexes, depending on their metabolic needs, the notion that supercomplexes have a role in the regulation of metabolism has been challenged. However, irrespective of the mechanistic conclusions, the composition of various high molecular weight supercomplexes remains uncertain. Here, using cryogenic electron microscopy, we demonstrate that mammalian (mouse) tissues contain three defined types of ‘respirasome’, supercomplexes made of CI, CIII2 and CIV. The stoichiometry and position of CIV differs in the three respirasomes, of which only one contains the supercomplex-associated factor SCAF1, whose involvement in respirasome formation has long been contended. Our structures confirm that the ‘canonical’ respirasome (the C-respirasome, CICIII2CIV) does not contain SCAF1, which is instead associated to a different respirasome (the CS-respirasome), containing a second copy of CIV. We also identify an alternative respirasome (A-respirasome), with CIV bound to the ‘back’ of CI, instead of the ‘toe’. This structural characterization of mouse mitochondrial supercomplexes allows us to hypothesize a mechanistic basis for their specific role in different metabolic conditions."},{"author":[{"full_name":"Isbel, Luke","first_name":"Luke","last_name":"Isbel"},{"first_name":"Murat","full_name":"Iskar, Murat","last_name":"Iskar"},{"full_name":"Durdu, Sevi","first_name":"Sevi","last_name":"Durdu"},{"last_name":"Weiss","first_name":"Joscha","full_name":"Weiss, Joscha"},{"full_name":"Grand, Ralph S.","first_name":"Ralph S.","last_name":"Grand"},{"last_name":"Hietter-Pfeiffer","full_name":"Hietter-Pfeiffer, Eric","first_name":"Eric"},{"first_name":"Zuzanna","full_name":"Kozicka, Zuzanna","last_name":"Kozicka"},{"full_name":"Michael, Alicia","orcid":"0000-0002-6080-839X","first_name":"Alicia","id":"6437c950-2a03-11ee-914d-d6476dd7b75c","last_name":"Michael"},{"full_name":"Burger, Lukas","first_name":"Lukas","last_name":"Burger"},{"full_name":"Thomä, Nicolas H.","first_name":"Nicolas H.","last_name":"Thomä"},{"first_name":"Dirk","full_name":"Schübeler, Dirk","last_name":"Schübeler"}],"article_type":"original","publication_status":"published","month":"06","intvolume":"        30","oa_version":"Published Version","issue":"7","main_file_link":[{"url":"https://doi.org/10.1038/s41594-023-01021-8","open_access":"1"}],"oa":1,"year":"2023","article_processing_charge":"No","date_created":"2024-03-21T07:53:24Z","scopus_import":"1","publication":"Nature Structural & Molecular Biology","citation":{"short":"L. Isbel, M. Iskar, S. Durdu, J. Weiss, R.S. Grand, E. Hietter-Pfeiffer, Z. Kozicka, A.K. Michael, L. Burger, N.H. Thomä, D. Schübeler, Nature Structural &#38; Molecular Biology 30 (2023) 948–957.","apa":"Isbel, L., Iskar, M., Durdu, S., Weiss, J., Grand, R. S., Hietter-Pfeiffer, E., … Schübeler, D. (2023). Readout of histone methylation by Trim24 locally restricts chromatin opening by p53. <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-023-01021-8\">https://doi.org/10.1038/s41594-023-01021-8</a>","ieee":"L. Isbel <i>et al.</i>, “Readout of histone methylation by Trim24 locally restricts chromatin opening by p53,” <i>Nature Structural &#38; Molecular Biology</i>, vol. 30, no. 7. Springer Nature, pp. 948–957, 2023.","chicago":"Isbel, Luke, Murat Iskar, Sevi Durdu, Joscha Weiss, Ralph S. Grand, Eric Hietter-Pfeiffer, Zuzanna Kozicka, et al. “Readout of Histone Methylation by Trim24 Locally Restricts Chromatin Opening by P53.” <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature, 2023. <a href=\"https://doi.org/10.1038/s41594-023-01021-8\">https://doi.org/10.1038/s41594-023-01021-8</a>.","ista":"Isbel L, Iskar M, Durdu S, Weiss J, Grand RS, Hietter-Pfeiffer E, Kozicka Z, Michael AK, Burger L, Thomä NH, Schübeler D. 2023. Readout of histone methylation by Trim24 locally restricts chromatin opening by p53. Nature Structural &#38; Molecular Biology. 30(7), 948–957.","mla":"Isbel, Luke, et al. “Readout of Histone Methylation by Trim24 Locally Restricts Chromatin Opening by P53.” <i>Nature Structural &#38; Molecular Biology</i>, vol. 30, no. 7, Springer Nature, 2023, pp. 948–57, doi:<a href=\"https://doi.org/10.1038/s41594-023-01021-8\">10.1038/s41594-023-01021-8</a>.","ama":"Isbel L, Iskar M, Durdu S, et al. Readout of histone methylation by Trim24 locally restricts chromatin opening by p53. <i>Nature Structural &#38; Molecular Biology</i>. 2023;30(7):948-957. doi:<a href=\"https://doi.org/10.1038/s41594-023-01021-8\">10.1038/s41594-023-01021-8</a>"},"extern":"1","volume":30,"publication_identifier":{"eissn":["1545-9985"],"issn":["1545-9993"]},"quality_controlled":"1","day":"29","date_published":"2023-06-29T00:00:00Z","external_id":{"pmid":["37386214"]},"language":[{"iso":"eng"}],"fulldoi":"https://doi.org/10.1038/s41594-023-01021-8","keyword":["Molecular Biology","Structural Biology"],"title":"Readout of histone methylation by Trim24 locally restricts chromatin opening by p53","abstract":[{"text":"The genomic binding sites of the transcription factor (TF) and tumor suppressor p53 are unusually diverse with regard to their chromatin features, including histone modifications, raising the possibility that the local chromatin environment can contextualize p53 regulation. Here, we show that epigenetic characteristics of closed chromatin, such as DNA methylation, do not influence the binding of p53 across the genome. Instead, the ability of p53 to open chromatin and activate its target genes is locally restricted by its cofactor Trim24. Trim24 binds to both p53 and unmethylated histone 3 lysine 4 (H3K4), thereby preferentially localizing to those p53 sites that reside in closed chromatin, whereas it is deterred from accessible chromatin by H3K4 methylation. The presence of Trim24 increases cell viability upon stress and enables p53 to affect gene expression as a function of the local chromatin state. These findings link H3K4 methylation to p53 function and illustrate how specificity in chromatin can be achieved, not by TF-intrinsic sensitivity to histone modifications, but by employing chromatin-sensitive cofactors that locally modulate TF function.","lang":"eng"}],"pmid":1,"page":"948-957","date_updated":"2024-03-25T12:37:20Z","status":"public","_id":"15149","type":"journal_article","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Springer Nature","doi":"10.1038/s41594-023-01021-8"},{"intvolume":"        29","issue":"9","oa_version":"Published Version","month":"09","oa":1,"year":"2022","article_processing_charge":"No","ddc":["570"],"author":[{"first_name":"Michael","full_name":"Prattes, Michael","last_name":"Prattes"},{"last_name":"Grishkovskaya","full_name":"Grishkovskaya, Irina","first_name":"Irina"},{"id":"3661B498-F248-11E8-B48F-1D18A9856A87","first_name":"Victor-Valentin","full_name":"Hodirnau, Victor-Valentin","last_name":"Hodirnau"},{"first_name":"Christina","full_name":"Hetzmannseder, Christina","last_name":"Hetzmannseder"},{"last_name":"Zisser","first_name":"Gertrude","full_name":"Zisser, Gertrude"},{"last_name":"Sailer","first_name":"Carolin","full_name":"Sailer, Carolin"},{"last_name":"Kargas","full_name":"Kargas, Vasileios","first_name":"Vasileios"},{"last_name":"Loibl","first_name":"Mathias","full_name":"Loibl, Mathias"},{"full_name":"Gerhalter, Magdalena","first_name":"Magdalena","last_name":"Gerhalter"},{"last_name":"Kofler","first_name":"Lisa","full_name":"Kofler, Lisa"},{"last_name":"Warren","first_name":"Alan J.","full_name":"Warren, Alan J."},{"first_name":"Florian","full_name":"Stengel, Florian","last_name":"Stengel"},{"last_name":"Haselbach","full_name":"Haselbach, David","first_name":"David"},{"full_name":"Bergler, Helmut","first_name":"Helmut","last_name":"Bergler"}],"article_type":"original","publication_status":"published","quality_controlled":"1","publication_identifier":{"issn":["1545-9993"],"eissn":["1545-9985"]},"volume":29,"acknowledgement":"We thank M. Fromont-Racine, A. Johnson, J. Woolford, S. Rospert, J. P. G. Ballesta and\r\nE. Hurt for supplying antibodies. The work was supported by Boehringer Ingelheim (to\r\nD. H.), the Austrian Science Foundation FWF (grants 32536 and 32977 to H. B.), the\r\nUK Medical Research Council (MR/T012412/1 to A. J. W.) and the German Research\r\nFoundation (Emmy Noether Programme STE 2517/1-1 and STE 2517/5-1 to F.S.). We\r\nthank Norberto Escudero-Urquijo, Pablo Castro-Hartmann and K. Dent, Cambridge\r\nInstitute for Medical Research, for their help in cryo-EM during early phases of this\r\nproject. This research was supported by the Scientific Service Units of IST Austria through\r\nresources provided by the Electron Microscopy Facility. We thank S. Keller, Institute of\r\nMolecular Biosciences (Biophysics), University Graz for support with the quantification of\r\nthe SPR particle release assay. We thank I. Schaffner, University of Natural Resources and\r\nLife Sciences, Vienna for her help in early stages of the SPR experiments.","publication":"Nature Structural & Molecular Biology","date_created":"2023-01-16T09:59:06Z","scopus_import":"1","department":[{"_id":"EM-Fac"}],"has_accepted_license":"1","acknowledged_ssus":[{"_id":"EM-Fac"}],"citation":{"chicago":"Prattes, Michael, Irina Grishkovskaya, Victor-Valentin Hodirnau, Christina Hetzmannseder, Gertrude Zisser, Carolin Sailer, Vasileios Kargas, et al. “Visualizing Maturation Factor Extraction from the Nascent Ribosome by the AAA-ATPase Drg1.” <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature, 2022. <a href=\"https://doi.org/10.1038/s41594-022-00832-5\">https://doi.org/10.1038/s41594-022-00832-5</a>.","apa":"Prattes, M., Grishkovskaya, I., Hodirnau, V.-V., Hetzmannseder, C., Zisser, G., Sailer, C., … Bergler, H. (2022). Visualizing maturation factor extraction from the nascent ribosome by the AAA-ATPase Drg1. <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-022-00832-5\">https://doi.org/10.1038/s41594-022-00832-5</a>","ieee":"M. Prattes <i>et al.</i>, “Visualizing maturation factor extraction from the nascent ribosome by the AAA-ATPase Drg1,” <i>Nature Structural &#38; Molecular Biology</i>, vol. 29, no. 9. Springer Nature, pp. 942–953, 2022.","short":"M. Prattes, I. Grishkovskaya, V.-V. Hodirnau, C. Hetzmannseder, G. Zisser, C. Sailer, V. Kargas, M. Loibl, M. Gerhalter, L. Kofler, A.J. Warren, F. Stengel, D. Haselbach, H. Bergler, Nature Structural &#38; Molecular Biology 29 (2022) 942–953.","mla":"Prattes, Michael, et al. “Visualizing Maturation Factor Extraction from the Nascent Ribosome by the AAA-ATPase Drg1.” <i>Nature Structural &#38; Molecular Biology</i>, vol. 29, no. 9, Springer Nature, 2022, pp. 942–53, doi:<a href=\"https://doi.org/10.1038/s41594-022-00832-5\">10.1038/s41594-022-00832-5</a>.","ama":"Prattes M, Grishkovskaya I, Hodirnau V-V, et al. Visualizing maturation factor extraction from the nascent ribosome by the AAA-ATPase Drg1. <i>Nature Structural &#38; Molecular Biology</i>. 2022;29(9):942-953. doi:<a href=\"https://doi.org/10.1038/s41594-022-00832-5\">10.1038/s41594-022-00832-5</a>","ista":"Prattes M, Grishkovskaya I, Hodirnau V-V, Hetzmannseder C, Zisser G, Sailer C, Kargas V, Loibl M, Gerhalter M, Kofler L, Warren AJ, Stengel F, Haselbach D, Bergler H. 2022. Visualizing maturation factor extraction from the nascent ribosome by the AAA-ATPase Drg1. Nature Structural &#38; Molecular Biology. 29(9), 942–953."},"keyword":["Molecular Biology","Structural Biology"],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","short":"CC BY (4.0)"},"date_published":"2022-09-12T00:00:00Z","day":"12","language":[{"iso":"eng"}],"fulldoi":"https://doi.org/10.1038/s41594-022-00832-5","file":[{"date_created":"2023-01-30T10:00:04Z","relation":"main_file","creator":"dernst","success":1,"file_size":9935057,"date_updated":"2023-01-30T10:00:04Z","checksum":"2d5c3ec01718fefd7553052b0b8a0793","file_name":"2022_NatureStrucMolecBio_Prattes.pdf","content_type":"application/pdf","access_level":"open_access","file_id":"12447"}],"isi":1,"external_id":{"pmid":["36097293"],"isi":["000852942100004"]},"status":"public","_id":"12262","type":"journal_article","doi":"10.1038/s41594-022-00832-5","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","publisher":"Springer Nature","abstract":[{"text":"The AAA-ATPase Drg1 is a key factor in eukaryotic ribosome biogenesis that initiates cytoplasmic maturation of the large ribosomal subunit. Drg1 releases the shuttling maturation factor Rlp24 from pre-60S particles shortly after nuclear export, a strict requirement for downstream maturation. The molecular mechanism of release remained elusive. Here, we report a series of cryo-EM structures that captured the extraction of Rlp24 from pre-60S particles by Saccharomyces cerevisiae Drg1. These structures reveal that Arx1 and the eukaryote-specific rRNA expansion segment ES27 form a joint docking platform that positions Drg1 for efficient extraction of Rlp24 from the pre-ribosome. The tips of the Drg1 N domains thereby guide the Rlp24 C terminus into the central pore of the Drg1 hexamer, enabling extraction by a hand-over-hand translocation mechanism. Our results uncover substrate recognition and processing by Drg1 step by step and provide a comprehensive mechanistic picture of the conserved modus operandi of AAA-ATPases.","lang":"eng"}],"file_date_updated":"2023-01-30T10:00:04Z","title":"Visualizing maturation factor extraction from the nascent ribosome by the AAA-ATPase Drg1","date_updated":"2023-08-04T09:52:20Z","page":"942-953","pmid":1},{"quality_controlled":"1","volume":30,"publication_identifier":{"eissn":["1545-9985"],"issn":["1545-9993"]},"publication":"Nature Structural & Molecular Biology","scopus_import":"1","date_created":"2024-03-20T10:41:45Z","extern":"1","citation":{"mla":"Yelland, James N., et al. “A Single 2′-O-Methylation of Ribosomal RNA Gates Assembly of a Functional Ribosome.” <i>Nature Structural &#38; Molecular Biology</i>, vol. 30, Springer Nature, 2022, pp. 91–98, doi:<a href=\"https://doi.org/10.1038/s41594-022-00891-8\">10.1038/s41594-022-00891-8</a>.","ama":"Yelland JN, Bravo JPK, Black JJ, Taylor DW, Johnson AW. A single 2′-O-methylation of ribosomal RNA gates assembly of a functional ribosome. <i>Nature Structural &#38; Molecular Biology</i>. 2022;30:91-98. doi:<a href=\"https://doi.org/10.1038/s41594-022-00891-8\">10.1038/s41594-022-00891-8</a>","ista":"Yelland JN, Bravo JPK, Black JJ, Taylor DW, Johnson AW. 2022. A single 2′-O-methylation of ribosomal RNA gates assembly of a functional ribosome. Nature Structural &#38; Molecular Biology. 30, 91–98.","chicago":"Yelland, James N., Jack Peter Kelly Bravo, Joshua J. Black, David W. Taylor, and Arlen W. Johnson. “A Single 2′-O-Methylation of Ribosomal RNA Gates Assembly of a Functional Ribosome.” <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature, 2022. <a href=\"https://doi.org/10.1038/s41594-022-00891-8\">https://doi.org/10.1038/s41594-022-00891-8</a>.","short":"J.N. Yelland, J.P.K. Bravo, J.J. Black, D.W. Taylor, A.W. Johnson, Nature Structural &#38; Molecular Biology 30 (2022) 91–98.","apa":"Yelland, J. N., Bravo, J. P. K., Black, J. J., Taylor, D. W., &#38; Johnson, A. W. (2022). A single 2′-O-methylation of ribosomal RNA gates assembly of a functional ribosome. <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-022-00891-8\">https://doi.org/10.1038/s41594-022-00891-8</a>","ieee":"J. N. Yelland, J. P. K. Bravo, J. J. Black, D. W. Taylor, and A. W. Johnson, “A single 2′-O-methylation of ribosomal RNA gates assembly of a functional ribosome,” <i>Nature Structural &#38; Molecular Biology</i>, vol. 30. Springer Nature, pp. 91–98, 2022."},"main_file_link":[{"url":"https://doi.org/10.1038/s41594-022-00891-8","open_access":"1"}],"oa_version":"Published Version","intvolume":"        30","month":"12","article_processing_charge":"Yes (in subscription journal)","year":"2022","oa":1,"publication_status":"published","article_type":"original","author":[{"full_name":"Yelland, James N.","first_name":"James N.","last_name":"Yelland"},{"id":"96aecfa5-8931-11ee-af30-aa6a5d6eee0e","first_name":"Jack Peter Kelly","full_name":"Bravo, Jack Peter Kelly","orcid":"0000-0003-0456-0753","last_name":"Bravo"},{"last_name":"Black","first_name":"Joshua J.","full_name":"Black, Joshua J."},{"first_name":"David W.","full_name":"Taylor, David W.","last_name":"Taylor"},{"last_name":"Johnson","first_name":"Arlen W.","full_name":"Johnson, Arlen W."}],"type":"journal_article","status":"public","_id":"15131","doi":"10.1038/s41594-022-00891-8","publisher":"Springer Nature","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","abstract":[{"text":"RNA modifications are widespread in biology and abundant in ribosomal RNA. However, the importance of these modifications is not well understood. We show that methylation of a single nucleotide, in the catalytic center of the large subunit, gates ribosome assembly. Massively parallel mutational scanning of the essential nuclear GTPase Nog2 identified important interactions with rRNA, particularly with the 2′-<jats:italic>O</jats:italic>-methylated A-site base Gm2922. We found that methylation of G2922 is needed for assembly and efficient nuclear export of the large subunit. Critically, we identified single amino acid changes in Nog2 that completely bypass dependence on G2922 methylation and used cryoelectron microscopy to directly visualize how methylation flips Gm2922 into the active site channel of Nog2. This work demonstrates that a single RNA modification is a critical checkpoint in ribosome biogenesis, suggesting that such modifications can play an important role in regulation and assembly of macromolecular machines.","lang":"eng"}],"title":"A single 2′-O-methylation of ribosomal RNA gates assembly of a functional ribosome","date_updated":"2024-06-04T06:27:09Z","page":"91-98","pmid":1,"keyword":["Molecular Biology","Structural Biology"],"day":"19","date_published":"2022-12-19T00:00:00Z","fulldoi":"https://doi.org/10.1038/s41594-022-00891-8","language":[{"iso":"eng"}],"external_id":{"pmid":["36536102"]}},{"author":[{"id":"4D5303E6-F248-11E8-B48F-1D18A9856A87","first_name":"Gergely","full_name":"Pinke, Gergely","last_name":"Pinke"},{"last_name":"Zhou","first_name":"Long","orcid":"0000-0002-1864-8951","full_name":"Zhou, Long","id":"3E751364-F248-11E8-B48F-1D18A9856A87"},{"orcid":"0000-0002-0977-7989","full_name":"Sazanov, Leonid A","first_name":"Leonid A","id":"338D39FE-F248-11E8-B48F-1D18A9856A87","last_name":"Sazanov"}],"article_type":"original","publication_status":"published","month":"11","oa_version":"None","intvolume":"        27","issue":"11","year":"2020","article_processing_charge":"No","date_created":"2020-09-28T08:59:27Z","department":[{"_id":"LeSa"}],"scopus_import":"1","publication":"Nature Structural and Molecular Biology","citation":{"chicago":"Pinke, Gergely, Long Zhou, and Leonid A Sazanov. “Cryo-EM Structure of the Entire Mammalian F-Type ATP Synthase.” <i>Nature Structural and Molecular Biology</i>. Springer Nature, 2020. <a href=\"https://doi.org/10.1038/s41594-020-0503-8\">https://doi.org/10.1038/s41594-020-0503-8</a>.","short":"G. Pinke, L. Zhou, L.A. Sazanov, Nature Structural and Molecular Biology 27 (2020) 1077–1085.","ieee":"G. Pinke, L. Zhou, and L. A. Sazanov, “Cryo-EM structure of the entire mammalian F-type ATP synthase,” <i>Nature Structural and Molecular Biology</i>, vol. 27, no. 11. Springer Nature, pp. 1077–1085, 2020.","apa":"Pinke, G., Zhou, L., &#38; Sazanov, L. A. (2020). Cryo-EM structure of the entire mammalian F-type ATP synthase. <i>Nature Structural and Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-020-0503-8\">https://doi.org/10.1038/s41594-020-0503-8</a>","ama":"Pinke G, Zhou L, Sazanov LA. Cryo-EM structure of the entire mammalian F-type ATP synthase. <i>Nature Structural and Molecular Biology</i>. 2020;27(11):1077-1085. doi:<a href=\"https://doi.org/10.1038/s41594-020-0503-8\">10.1038/s41594-020-0503-8</a>","mla":"Pinke, Gergely, et al. “Cryo-EM Structure of the Entire Mammalian F-Type ATP Synthase.” <i>Nature Structural and Molecular Biology</i>, vol. 27, no. 11, Springer Nature, 2020, pp. 1077–85, doi:<a href=\"https://doi.org/10.1038/s41594-020-0503-8\">10.1038/s41594-020-0503-8</a>.","ista":"Pinke G, Zhou L, Sazanov LA. 2020. Cryo-EM structure of the entire mammalian F-type ATP synthase. Nature Structural and Molecular Biology. 27(11), 1077–1085."},"acknowledged_ssus":[{"_id":"EM-Fac"},{"_id":"ScienComp"}],"related_material":{"link":[{"url":"https://ist.ac.at/en/news/structure-of-atpase-solved/","description":"News on IST Homepage","relation":"press_release"}]},"volume":27,"publication_identifier":{"issn":["1545-9993"],"eissn":["1545-9985"]},"quality_controlled":"1","acknowledgement":"We thank J. Novacek from CEITEC (Brno, Czech Republic) for assistance with collecting the FEI Krios dataset and iNEXT for providing access to CEITEC. We thank the IST Austria EM facility for access and assistance with collecting the FEI Glacios dataset. Data processing was performed at the IST high-performance computing cluster. This work has been supported by iNEXT EM HEDC (proposal 4506), funded by the Horizon 2020 Programme of the European Commission.","day":"01","date_published":"2020-11-01T00:00:00Z","external_id":{"pmid":["32929284"],"isi":["000569299400004"]},"language":[{"iso":"eng"}],"isi":1,"fulldoi":"https://doi.org/10.1038/s41594-020-0503-8","title":"Cryo-EM structure of the entire mammalian F-type ATP synthase","abstract":[{"text":"The majority of adenosine triphosphate (ATP) powering cellular processes in eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo, determined by cryo-electron microscopy. Subunits in the membrane domain are arranged in the ‘proton translocation cluster’ attached to the c-ring and a more distant ‘hook apparatus’ holding subunit e. Unexpectedly, this subunit is anchored to a lipid ‘plug’ capping the c-ring. We present a detailed proton translocation pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled c-ring, suggesting permeability transition pore opening. We propose a model for the permeability transition pore opening, whereby subunit e pulls the lipid plug out of the c-ring. Our structure will allow the design of drugs for many emerging applications in medicine.","lang":"eng"}],"pmid":1,"page":"1077-1085","date_updated":"2025-07-10T11:57:09Z","status":"public","_id":"8581","type":"journal_article","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Springer Nature","doi":"10.1038/s41594-020-0503-8"},{"citation":{"ama":"Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. Dynamics and interactions of AAC3 in DPC are not functionally relevant. <i>Nature Structural &#38; Molecular Biology</i>. 2018;25(9):745-747. doi:<a href=\"https://doi.org/10.1038/s41594-018-0127-4\">10.1038/s41594-018-0127-4</a>","mla":"Kurauskas, Vilius, et al. “Dynamics and Interactions of AAC3 in DPC Are Not Functionally Relevant.” <i>Nature Structural &#38; Molecular Biology</i>, vol. 25, no. 9, Springer Nature, 2018, pp. 745–47, doi:<a href=\"https://doi.org/10.1038/s41594-018-0127-4\">10.1038/s41594-018-0127-4</a>.","ista":"Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. 2018. Dynamics and interactions of AAC3 in DPC are not functionally relevant. Nature Structural &#38; Molecular Biology. 25(9), 745–747.","chicago":"Kurauskas, Vilius, Audrey Hessel, François Dehez, Christophe Chipot, Beate Bersch, and Paul Schanda. “Dynamics and Interactions of AAC3 in DPC Are Not Functionally Relevant.” <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41594-018-0127-4\">https://doi.org/10.1038/s41594-018-0127-4</a>.","short":"V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, P. Schanda, Nature Structural &#38; Molecular Biology 25 (2018) 745–747.","apa":"Kurauskas, V., Hessel, A., Dehez, F., Chipot, C., Bersch, B., &#38; Schanda, P. (2018). Dynamics and interactions of AAC3 in DPC are not functionally relevant. <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-018-0127-4\">https://doi.org/10.1038/s41594-018-0127-4</a>","ieee":"V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, and P. Schanda, “Dynamics and interactions of AAC3 in DPC are not functionally relevant,” <i>Nature Structural &#38; Molecular Biology</i>, vol. 25, no. 9. Springer Nature, pp. 745–747, 2018."},"extern":"1","date_updated":"2021-01-12T08:19:16Z","page":"745-747","title":"Dynamics and interactions of AAC3 in DPC are not functionally relevant","date_created":"2020-09-18T10:04:59Z","publication":"Nature Structural & Molecular Biology","publisher":"Springer Nature","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","doi":"10.1038/s41594-018-0127-4","type":"journal_article","_id":"8438","volume":25,"publication_identifier":{"issn":["1545-9993","1545-9985"]},"status":"public","quality_controlled":"1","fulldoi":"https://doi.org/10.1038/s41594-018-0127-4","publication_status":"published","article_type":"letter_note","author":[{"last_name":"Kurauskas","first_name":"Vilius","full_name":"Kurauskas, Vilius"},{"last_name":"Hessel","full_name":"Hessel, Audrey","first_name":"Audrey"},{"last_name":"Dehez","full_name":"Dehez, François","first_name":"François"},{"last_name":"Chipot","first_name":"Christophe","full_name":"Chipot, Christophe"},{"last_name":"Bersch","full_name":"Bersch, Beate","first_name":"Beate"},{"last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"}],"language":[{"iso":"eng"}],"date_published":"2018-09-03T00:00:00Z","day":"03","article_processing_charge":"No","year":"2018","month":"09","intvolume":"        25","issue":"9","oa_version":"None","keyword":["Molecular Biology","Structural Biology"]},{"day":"05","date_published":"2017-10-05T00:00:00Z","file":[{"relation":"main_file","date_created":"2019-11-07T12:51:07Z","creator":"lsazanov","file_size":4118385,"checksum":"9bc7e8c41b43636dd7566289e511f096","date_updated":"2020-07-14T12:46:36Z","file_name":"29893_2_merged_1501257589_red.pdf","content_type":"application/pdf","access_level":"open_access","file_id":"6993"}],"fulldoi":"https://doi.org/10.1038/nsmb.3460","isi":1,"publist_id":"7304","language":[{"iso":"eng"}],"external_id":{"isi":["000412278000006"]},"type":"journal_article","project":[{"grant_number":"701309","_id":"2590DB08-B435-11E9-9278-68D0E5697425","name":"Atomic Resolution Structures of Mitochondrial Respiratory Chain Supercomplexes","call_identifier":"H2020"}],"_id":"515","status":"public","doi":"10.1038/nsmb.3460","publisher":"Nature Publishing Group","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","file_date_updated":"2020-07-14T12:46:36Z","abstract":[{"lang":"eng","text":"The oxidative phosphorylation electron transport chain (OXPHOS-ETC) of the inner mitochondrial membrane is composed of five large protein complexes, named CI-CV. These complexes convert energy from the food we eat into ATP, a small molecule used to power a multitude of essential reactions throughout the cell. OXPHOS-ETC complexes are organized into supercomplexes (SCs) of defined stoichiometry: CI forms a supercomplex with CIII2 and CIV (SC I+III2+IV, known as the respirasome), as well as with CIII2 alone (SC I+III2). CIII2 forms a supercomplex with CIV (SC III2+IV) and CV forms dimers (CV2). Recent cryo-EM studies have revealed the structures of SC I+III2+IV and SC I+III2. Furthermore, recent work has shed light on the assembly and function of the SCs. Here we review and compare these recent studies and discuss how they have advanced our understanding of mitochondrial electron transport."}],"title":"Clarifying the supercomplex: The higher-order organization of the mitochondrial electron transport chain","date_updated":"2025-09-18T09:47:41Z","page":"800 - 808","oa_version":"Submitted Version","issue":"10","intvolume":"        24","month":"10","article_processing_charge":"No","oa":1,"year":"2017","ddc":["572"],"article_type":"original","publication_status":"published","author":[{"last_name":"Letts","first_name":"James A","orcid":"0000-0002-9864-3586","full_name":"Letts, James A","id":"322DA418-F248-11E8-B48F-1D18A9856A87"},{"id":"338D39FE-F248-11E8-B48F-1D18A9856A87","full_name":"Sazanov, Leonid A","orcid":"0000-0002-0977-7989","first_name":"Leonid A","last_name":"Sazanov"}],"quality_controlled":"1","volume":24,"publication_identifier":{"issn":["1545-9993"]},"ec_funded":1,"publication":"Nature Structural and Molecular Biology","department":[{"_id":"LeSa"}],"scopus_import":"1","date_created":"2018-12-11T11:46:54Z","has_accepted_license":"1","corr_author":"1","citation":{"short":"J.A. Letts, L.A. Sazanov, Nature Structural and Molecular Biology 24 (2017) 800–808.","apa":"Letts, J. A., &#38; Sazanov, L. A. (2017). Clarifying the supercomplex: The higher-order organization of the mitochondrial electron transport chain. <i>Nature Structural and Molecular Biology</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/nsmb.3460\">https://doi.org/10.1038/nsmb.3460</a>","ieee":"J. A. Letts and L. A. Sazanov, “Clarifying the supercomplex: The higher-order organization of the mitochondrial electron transport chain,” <i>Nature Structural and Molecular Biology</i>, vol. 24, no. 10. Nature Publishing Group, pp. 800–808, 2017.","chicago":"Letts, James A, and Leonid A Sazanov. “Clarifying the Supercomplex: The Higher-Order Organization of the Mitochondrial Electron Transport Chain.” <i>Nature Structural and Molecular Biology</i>. Nature Publishing Group, 2017. <a href=\"https://doi.org/10.1038/nsmb.3460\">https://doi.org/10.1038/nsmb.3460</a>.","ista":"Letts JA, Sazanov LA. 2017. Clarifying the supercomplex: The higher-order organization of the mitochondrial electron transport chain. Nature Structural and Molecular Biology. 24(10), 800–808.","ama":"Letts JA, Sazanov LA. Clarifying the supercomplex: The higher-order organization of the mitochondrial electron transport chain. <i>Nature Structural and Molecular Biology</i>. 2017;24(10):800-808. doi:<a href=\"https://doi.org/10.1038/nsmb.3460\">10.1038/nsmb.3460</a>","mla":"Letts, James A., and Leonid A. Sazanov. “Clarifying the Supercomplex: The Higher-Order Organization of the Mitochondrial Electron Transport Chain.” <i>Nature Structural and Molecular Biology</i>, vol. 24, no. 10, Nature Publishing Group, 2017, pp. 800–08, doi:<a href=\"https://doi.org/10.1038/nsmb.3460\">10.1038/nsmb.3460</a>."}},{"date_published":"2004-12-12T00:00:00Z","day":"12","external_id":{"pmid":["15592479"]},"language":[{"iso":"eng"}],"fulldoi":"https://doi.org/10.1038/nsmb870","publist_id":"3554","_id":"3141","status":"public","type":"journal_article","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","publisher":"Nature Publishing Group","doi":"10.1038/nsmb870","title":"Conformational changes in the Arp2 3 complex leading to actin nucleation","abstract":[{"text":"The two actin-related subunits of the Arp2/3 complex, Arp2 and Arp3, are proposed to form a pseudo actin dimer that nucleates actin polymerization. However, in the crystal structure of the inactive complex, they are too far apart to form such a nucleus. Here, we show using EM that yeast and bovine Arp2/3 complexes exist in a distribution among open, intermediate and closed conformations. The crystal structure docks well into the open conformation. The activator WASp binds at the cleft between Arp2 and Arp3, and all WASp-bound complexes are closed. The inhibitor coronin binds near the p35 subunit, and all coronin-bound complexes are open. Activating and loss-of-function mutations in the p35 subunit skew conformational distribution in opposite directions, closed and open, respectively. We conclude that WASp stabilizes p35-dependent closure of the complex, holding Arp2 and Arp3 closer together to nucleate an actin filament.","lang":"eng"}],"pmid":1,"page":"26 - 31","date_updated":"2026-07-15T12:44:10Z","month":"12","oa_version":"None","intvolume":"        12","issue":"1","year":"2004","article_processing_charge":"No","author":[{"last_name":"Rodal","full_name":"Rodal, Avital","first_name":"Avital"},{"full_name":"Sokolova, Olga","first_name":"Olga","last_name":"Sokolova"},{"first_name":"Deborah","full_name":"Robins, Deborah","last_name":"Robins"},{"last_name":"Daugherty","first_name":"Karen","full_name":"Daugherty, Karen"},{"id":"37B36620-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-2279-1061","full_name":"Hippenmeyer, Simon","first_name":"Simon","last_name":"Hippenmeyer"},{"full_name":"Riezman, Howard","first_name":"Howard","last_name":"Riezman"},{"last_name":"Grigorieff","first_name":"Nikolaus","full_name":"Grigorieff, Nikolaus"},{"first_name":"Bruce","full_name":"Goode, Bruce","last_name":"Goode"}],"publication_status":"published","article_type":"original","volume":12,"publication_identifier":{"issn":["1545-9993"],"eissn":["1545-9985"]},"OA_type":"closed access","das_tickbox":"1","date_created":"2018-12-11T12:01:38Z","publication":"Nature Structural and Molecular Biology","citation":{"ista":"Rodal A, Sokolova O, Robins D, Daugherty K, Hippenmeyer S, Riezman H, Grigorieff N, Goode B. 2004. Conformational changes in the Arp2 3 complex leading to actin nucleation. Nature Structural and Molecular Biology. 12(1), 26–31.","mla":"Rodal, Avital, et al. “Conformational Changes in the Arp2 3 Complex Leading to Actin Nucleation.” <i>Nature Structural and Molecular Biology</i>, vol. 12, no. 1, Nature Publishing Group, 2004, pp. 26–31, doi:<a href=\"https://doi.org/10.1038/nsmb870\">10.1038/nsmb870</a>.","ama":"Rodal A, Sokolova O, Robins D, et al. Conformational changes in the Arp2 3 complex leading to actin nucleation. <i>Nature Structural and Molecular Biology</i>. 2004;12(1):26-31. doi:<a href=\"https://doi.org/10.1038/nsmb870\">10.1038/nsmb870</a>","apa":"Rodal, A., Sokolova, O., Robins, D., Daugherty, K., Hippenmeyer, S., Riezman, H., … Goode, B. (2004). Conformational changes in the Arp2 3 complex leading to actin nucleation. <i>Nature Structural and Molecular Biology</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/nsmb870\">https://doi.org/10.1038/nsmb870</a>","ieee":"A. Rodal <i>et al.</i>, “Conformational changes in the Arp2 3 complex leading to actin nucleation,” <i>Nature Structural and Molecular Biology</i>, vol. 12, no. 1. Nature Publishing Group, pp. 26–31, 2004.","short":"A. Rodal, O. Sokolova, D. Robins, K. Daugherty, S. Hippenmeyer, H. Riezman, N. Grigorieff, B. Goode, Nature Structural and Molecular Biology 12 (2004) 26–31.","chicago":"Rodal, Avital, Olga Sokolova, Deborah Robins, Karen Daugherty, Simon Hippenmeyer, Howard Riezman, Nikolaus Grigorieff, and Bruce Goode. “Conformational Changes in the Arp2 3 Complex Leading to Actin Nucleation.” <i>Nature Structural and Molecular Biology</i>. Nature Publishing Group, 2004. <a href=\"https://doi.org/10.1038/nsmb870\">https://doi.org/10.1038/nsmb870</a>."},"extern":"1"}]