[{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","citation":{"mla":"Zhao, Ziyu, et al. “The Ycf48 Accessory Factor Occupies the Site of the Oxygen-Evolving Manganese Cluster during Photosystem II Biogenesis.” Nature Communications, vol. 14, 4681, Springer Nature, 2023, doi:10.1038/s41467-023-40388-6.","ieee":"Z. Zhao et al., “The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis,” Nature Communications, vol. 14. Springer Nature, 2023.","short":"Z. Zhao, I. Vercellino, J. Knoppová, R. Sobotka, J.W. Murray, P.J. Nixon, L.A. Sazanov, J. Komenda, Nature Communications 14 (2023).","ama":"Zhao Z, Vercellino I, Knoppová J, et al. The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis. Nature Communications. 2023;14. doi:10.1038/s41467-023-40388-6","apa":"Zhao, Z., Vercellino, I., Knoppová, J., Sobotka, R., Murray, J. W., Nixon, P. J., … Komenda, J. (2023). The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-023-40388-6","chicago":"Zhao, Ziyu, Irene Vercellino, Jana Knoppová, Roman Sobotka, James W. Murray, Peter J. Nixon, Leonid A Sazanov, and Josef Komenda. “The Ycf48 Accessory Factor Occupies the Site of the Oxygen-Evolving Manganese Cluster during Photosystem II Biogenesis.” Nature Communications. Springer Nature, 2023. https://doi.org/10.1038/s41467-023-40388-6.","ista":"Zhao Z, Vercellino I, Knoppová J, Sobotka R, Murray JW, Nixon PJ, Sazanov LA, Komenda J. 2023. The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis. Nature Communications. 14, 4681."},"title":"The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis","external_id":{"isi":["001042606700004"]},"article_processing_charge":"Yes","author":[{"last_name":"Zhao","full_name":"Zhao, Ziyu","first_name":"Ziyu"},{"last_name":"Vercellino","full_name":"Vercellino, Irene","orcid":"0000-0001-5618-3449","id":"3ED6AF16-F248-11E8-B48F-1D18A9856A87","first_name":"Irene"},{"first_name":"Jana","full_name":"Knoppová, Jana","last_name":"Knoppová"},{"first_name":"Roman","last_name":"Sobotka","full_name":"Sobotka, Roman"},{"last_name":"Murray","full_name":"Murray, James W.","first_name":"James W."},{"first_name":"Peter J.","full_name":"Nixon, Peter J.","last_name":"Nixon"},{"first_name":"Leonid A","id":"338D39FE-F248-11E8-B48F-1D18A9856A87","full_name":"Sazanov, Leonid A","orcid":"0000-0002-0977-7989","last_name":"Sazanov"},{"first_name":"Josef","last_name":"Komenda","full_name":"Komenda, Josef"}],"article_number":"4681","publication":"Nature Communications","day":"04","year":"2023","isi":1,"has_accepted_license":"1","date_created":"2023-08-13T22:01:13Z","doi":"10.1038/s41467-023-40388-6","date_published":"2023-08-04T00:00:00Z","acknowledgement":"P.J.N. and J.W.M. are grateful for the support of the Biotechnology & Biological Sciences Research Council (awards BB/L003260/1 and BB/P00931X/1). J. Knoppová, R.S. and J. Komenda were supported by the Czech Science Foundation (project 19-29225X) and by ERC project Photoredesign (no. 854126) and L.A.S. was supported by the Scientific Service Units (SSU) of IST Austria through resources provided by the Electron Microscopy Facility (EMF), the Life Science Facility (LSF) and the IST high-performance computing cluster.","oa":1,"publisher":"Springer Nature","quality_controlled":"1","ddc":["570"],"date_updated":"2023-12-13T12:06:56Z","department":[{"_id":"LeSa"}],"file_date_updated":"2023-08-14T07:01:12Z","_id":"14040","status":"public","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"article_type":"original","type":"journal_article","language":[{"iso":"eng"}],"file":[{"file_size":2315325,"date_updated":"2023-08-14T07:01:12Z","creator":"dernst","file_name":"2023_NatureComm_Zhao.pdf","date_created":"2023-08-14T07:01:12Z","content_type":"application/pdf","relation":"main_file","access_level":"open_access","success":1,"checksum":"3b9043df3d51c300f9be95eac3ff9d0b","file_id":"14044"}],"publication_status":"published","publication_identifier":{"eissn":["2041-1723"]},"license":"https://creativecommons.org/licenses/by/4.0/","volume":14,"oa_version":"Published Version","acknowledged_ssus":[{"_id":"EM-Fac"},{"_id":"LifeSc"},{"_id":"ScienComp"}],"abstract":[{"text":"Robust oxygenic photosynthesis requires a suite of accessory factors to ensure efficient assembly and repair of the oxygen-evolving photosystem two (PSII) complex. The highly conserved Ycf48 assembly factor binds to the newly synthesized D1 reaction center polypeptide and promotes the initial steps of PSII assembly, but its binding site is unclear. Here we use cryo-electron microscopy to determine the structure of a cyanobacterial PSII D1/D2 reaction center assembly complex with Ycf48 attached. Ycf48, a 7-bladed beta propeller, binds to the amino-acid residues of D1 that ultimately ligate the water-oxidising Mn4CaO5 cluster, thereby preventing the premature binding of Mn2+ and Ca2+ ions and protecting the site from damage. Interactions with D2 help explain how Ycf48 promotes assembly of the D1/D2 complex. Overall, our work provides valuable insights into the early stages of PSII assembly and the structural changes that create the binding site for the Mn4CaO5 cluster.","lang":"eng"}],"intvolume":" 14","month":"08","scopus_import":"1"},{"quality_controlled":"1","publisher":"Springer Nature","date_created":"2021-10-24T22:01:35Z","doi":"10.1038/s41580-021-00415-0","date_published":"2022-02-01T00:00:00Z","page":"141–161","publication":"Nature Reviews Molecular Cell Biology","day":"01","year":"2022","isi":1,"title":"The assembly, regulation and function of the mitochondrial respiratory chain","article_processing_charge":"No","external_id":{"isi":["000705697100001"],"pmid":["34621061"]},"author":[{"last_name":"Vercellino","full_name":"Vercellino, Irene","orcid":" 0000-0001-5618-3449","id":"3ED6AF16-F248-11E8-B48F-1D18A9856A87","first_name":"Irene"},{"id":"338D39FE-F248-11E8-B48F-1D18A9856A87","first_name":"Leonid A","last_name":"Sazanov","orcid":"0000-0002-0977-7989","full_name":"Sazanov, Leonid A"}],"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","citation":{"ista":"Vercellino I, Sazanov LA. 2022. The assembly, regulation and function of the mitochondrial respiratory chain. Nature Reviews Molecular Cell Biology. 23, 141–161.","chicago":"Vercellino, Irene, and Leonid A Sazanov. “The Assembly, Regulation and Function of the Mitochondrial Respiratory Chain.” Nature Reviews Molecular Cell Biology. Springer Nature, 2022. https://doi.org/10.1038/s41580-021-00415-0.","ieee":"I. Vercellino and L. A. Sazanov, “The assembly, regulation and function of the mitochondrial respiratory chain,” Nature Reviews Molecular Cell Biology, vol. 23. Springer Nature, pp. 141–161, 2022.","short":"I. Vercellino, L.A. Sazanov, Nature Reviews Molecular Cell Biology 23 (2022) 141–161.","apa":"Vercellino, I., & Sazanov, L. A. (2022). The assembly, regulation and function of the mitochondrial respiratory chain. Nature Reviews Molecular Cell Biology. Springer Nature. https://doi.org/10.1038/s41580-021-00415-0","ama":"Vercellino I, Sazanov LA. The assembly, regulation and function of the mitochondrial respiratory chain. Nature Reviews Molecular Cell Biology. 2022;23:141–161. doi:10.1038/s41580-021-00415-0","mla":"Vercellino, Irene, and Leonid A. Sazanov. “The Assembly, Regulation and Function of the Mitochondrial Respiratory Chain.” Nature Reviews Molecular Cell Biology, vol. 23, Springer Nature, 2022, pp. 141–161, doi:10.1038/s41580-021-00415-0."},"intvolume":" 23","month":"02","scopus_import":"1","oa_version":"None","pmid":1,"abstract":[{"lang":"eng","text":"The mitochondrial oxidative phosphorylation system is central to cellular metabolism. It comprises five enzymatic complexes and two mobile electron carriers that work in a mitochondrial respiratory chain. By coupling the oxidation of reducing equivalents coming into mitochondria to the generation and subsequent dissipation of a proton gradient across the inner mitochondrial membrane, this electron transport chain drives the production of ATP, which is then used as a primary energy carrier in virtually all cellular processes. Minimal perturbations of the respiratory chain activity are linked to diseases; therefore, it is necessary to understand how these complexes are assembled and regulated and how they function. In this Review, we outline the latest assembly models for each individual complex, and we also highlight the recent discoveries indicating that the formation of larger assemblies, known as respiratory supercomplexes, originates from the association of the intermediates of individual complexes. We then discuss how recent cryo-electron microscopy structures have been key to answering open questions on the function of the electron transport chain in mitochondrial respiration and how supercomplexes and other factors, including metabolites, can regulate the activity of the single complexes. When relevant, we discuss how these mechanisms contribute to physiology and outline their deregulation in human diseases."}],"volume":23,"language":[{"iso":"eng"}],"publication_status":"published","publication_identifier":{"eissn":["1471-0080"],"issn":["1471-0072"]},"status":"public","type":"journal_article","article_type":"original","_id":"10182","department":[{"_id":"LeSa"}],"date_updated":"2023-08-02T06:55:42Z"},{"department":[{"_id":"SiHi"},{"_id":"LeSa"}],"date_updated":"2023-08-04T10:28:04Z","type":"journal_article","article_type":"letter_note","status":"public","_id":"12282","issue":"8","volume":135,"publication_status":"published","publication_identifier":{"eissn":["1477-9137"],"issn":["0021-9533"]},"language":[{"iso":"eng"}],"scopus_import":"1","intvolume":" 135","month":"04","abstract":[{"text":"From a simple thought to a multicellular movement","lang":"eng"}],"pmid":1,"oa_version":"None","article_processing_charge":"No","external_id":{"isi":["000798123600015"],"pmid":["35438168"]},"author":[{"first_name":"Nicole","id":"4CD6AAC6-F248-11E8-B48F-1D18A9856A87","last_name":"Amberg","full_name":"Amberg, Nicole","orcid":"0000-0002-3183-8207"},{"first_name":"Melissa A","id":"4C9372C4-F248-11E8-B48F-1D18A9856A87","last_name":"Stouffer","full_name":"Stouffer, Melissa A"},{"first_name":"Irene","id":"3ED6AF16-F248-11E8-B48F-1D18A9856A87","full_name":"Vercellino, Irene","orcid":"0000-0001-5618-3449","last_name":"Vercellino"}],"title":"Operation STEM fatale – how an equity, diversity and inclusion initiative has brought us to reflect on the current challenges in cell biology and science as a whole","citation":{"chicago":"Amberg, Nicole, Melissa A Stouffer, and Irene Vercellino. “Operation STEM Fatale – How an Equity, Diversity and Inclusion Initiative Has Brought Us to Reflect on the Current Challenges in Cell Biology and Science as a Whole.” Journal of Cell Science. The Company of Biologists, 2022. https://doi.org/10.1242/jcs.260017.","ista":"Amberg N, Stouffer MA, Vercellino I. 2022. Operation STEM fatale – how an equity, diversity and inclusion initiative has brought us to reflect on the current challenges in cell biology and science as a whole. Journal of Cell Science. 135(8), 260017.","mla":"Amberg, Nicole, et al. “Operation STEM Fatale – How an Equity, Diversity and Inclusion Initiative Has Brought Us to Reflect on the Current Challenges in Cell Biology and Science as a Whole.” Journal of Cell Science, vol. 135, no. 8, 260017, The Company of Biologists, 2022, doi:10.1242/jcs.260017.","short":"N. Amberg, M.A. Stouffer, I. Vercellino, Journal of Cell Science 135 (2022).","ieee":"N. Amberg, M. A. Stouffer, and I. Vercellino, “Operation STEM fatale – how an equity, diversity and inclusion initiative has brought us to reflect on the current challenges in cell biology and science as a whole,” Journal of Cell Science, vol. 135, no. 8. The Company of Biologists, 2022.","ama":"Amberg N, Stouffer MA, Vercellino I. Operation STEM fatale – how an equity, diversity and inclusion initiative has brought us to reflect on the current challenges in cell biology and science as a whole. Journal of Cell Science. 2022;135(8). doi:10.1242/jcs.260017","apa":"Amberg, N., Stouffer, M. A., & Vercellino, I. (2022). Operation STEM fatale – how an equity, diversity and inclusion initiative has brought us to reflect on the current challenges in cell biology and science as a whole. Journal of Cell Science. The Company of Biologists. https://doi.org/10.1242/jcs.260017"},"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","article_number":"260017","date_created":"2023-01-16T10:03:14Z","date_published":"2022-04-19T00:00:00Z","doi":"10.1242/jcs.260017","year":"2022","isi":1,"publication":"Journal of Cell Science","day":"19","publisher":"The Company of Biologists","quality_controlled":"1","acknowledgement":"The authors want to thank Professors Carrie Bernecky, Tom Henzinger, Martin Loose and Gaia Novarino for accepting to be interviewed, thus giving significant contribution to the discussion that lead to this article."},{"quality_controlled":"1","publisher":"Springer Nature","acknowledgement":"We thank the pre-clinical facility of the IST Austria and A. Venturino for assistance with the animals; and V.-V. Hodirnau for assistance during the Titan Krios data collection, performed at the IST Austria. The data processing was performed at the IST high-performance computing cluster. This project has received funding from the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska-Curie grant agreement no. 754411.","date_published":"2021-10-14T00:00:00Z","doi":"10.1038/s41586-021-03927-z","date_created":"2021-10-17T22:01:17Z","page":"364-367","day":"14","publication":"Nature","isi":1,"year":"2021","project":[{"call_identifier":"H2020","_id":"260C2330-B435-11E9-9278-68D0E5697425","grant_number":"754411","name":"ISTplus - Postdoctoral Fellowships"}],"title":"Structure and assembly of the mammalian mitochondrial supercomplex CIII2CIV","author":[{"full_name":"Vercellino, Irene","orcid":"0000-0001-5618-3449","last_name":"Vercellino","first_name":"Irene","id":"3ED6AF16-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Leonid A","id":"338D39FE-F248-11E8-B48F-1D18A9856A87","last_name":"Sazanov","full_name":"Sazanov, Leonid A","orcid":"0000-0002-0977-7989"}],"article_processing_charge":"No","external_id":{"pmid":["34616041"],"isi":["000704581600001"]},"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","citation":{"ista":"Vercellino I, Sazanov LA. 2021. Structure and assembly of the mammalian mitochondrial supercomplex CIII2CIV. Nature. 598(7880), 364–367.","chicago":"Vercellino, Irene, and Leonid A Sazanov. “Structure and Assembly of the Mammalian Mitochondrial Supercomplex CIII2CIV.” Nature. Springer Nature, 2021. https://doi.org/10.1038/s41586-021-03927-z.","ieee":"I. Vercellino and L. A. Sazanov, “Structure and assembly of the mammalian mitochondrial supercomplex CIII2CIV,” Nature, vol. 598, no. 7880. Springer Nature, pp. 364–367, 2021.","short":"I. Vercellino, L.A. Sazanov, Nature 598 (2021) 364–367.","apa":"Vercellino, I., & Sazanov, L. A. (2021). Structure and assembly of the mammalian mitochondrial supercomplex CIII2CIV. Nature. Springer Nature. https://doi.org/10.1038/s41586-021-03927-z","ama":"Vercellino I, Sazanov LA. Structure and assembly of the mammalian mitochondrial supercomplex CIII2CIV. Nature. 2021;598(7880):364-367. doi:10.1038/s41586-021-03927-z","mla":"Vercellino, Irene, and Leonid A. Sazanov. “Structure and Assembly of the Mammalian Mitochondrial Supercomplex CIII2CIV.” Nature, vol. 598, no. 7880, Springer Nature, 2021, pp. 364–67, doi:10.1038/s41586-021-03927-z."},"month":"10","intvolume":" 598","scopus_import":"1","oa_version":"None","pmid":1,"abstract":[{"lang":"eng","text":"The enzymes of the mitochondrial electron transport chain are key players of cell metabolism. Despite being active when isolated, in vivo they associate into supercomplexes1, whose precise role is debated. Supercomplexes CIII2CIV1-2 (refs. 2,3), CICIII2 (ref. 4) and CICIII2CIV (respirasome)5,6,7,8,9,10 exist in mammals, but in contrast to CICIII2 and the respirasome, to date the only known eukaryotic structures of CIII2CIV1-2 come from Saccharomyces cerevisiae11,12 and plants13, which have different organization. Here we present the first, to our knowledge, structures of mammalian (mouse and ovine) CIII2CIV and its assembly intermediates, in different conformations. We describe the assembly of CIII2CIV from the CIII2 precursor to the final CIII2CIV conformation, driven by the insertion of the N terminus of the assembly factor SCAF1 (ref. 14) deep into CIII2, while its C terminus is integrated into CIV. Our structures (which include CICIII2 and the respirasome) also confirm that SCAF1 is exclusively required for the assembly of CIII2CIV and has no role in the assembly of the respirasome. We show that CIII2 is asymmetric due to the presence of only one copy of subunit 9, which straddles both monomers and prevents the attachment of a second copy of SCAF1 to CIII2, explaining the presence of one copy of CIV in CIII2CIV in mammals. Finally, we show that CIII2 and CIV gain catalytic advantage when assembled into the supercomplex and propose a role for CIII2CIV in fine tuning the efficiency of electron transfer in the electron transport chain."}],"acknowledged_ssus":[{"_id":"PreCl"},{"_id":"EM-Fac"},{"_id":"ScienComp"}],"volume":598,"related_material":{"link":[{"description":"News on IST Webpage","url":"https://ist.ac.at/en/news/boosting-the-cells-power-house/","relation":"press_release"}]},"issue":"7880","ec_funded":1,"language":[{"iso":"eng"}],"publication_identifier":{"eissn":["1476-4687"],"issn":["0028-0836"]},"publication_status":"published","status":"public","article_type":"original","type":"journal_article","_id":"10146","department":[{"_id":"LeSa"}],"date_updated":"2023-08-14T08:01:21Z"},{"license":"https://creativecommons.org/licenses/by-nc/4.0/","issue":"9","volume":5,"publication_status":"published","publication_identifier":{"eissn":["23752548"]},"language":[{"iso":"eng"}],"file":[{"file_size":1236101,"date_updated":"2020-07-14T12:47:44Z","creator":"kschuh","file_name":"2019_AAAS_Qi.pdf","date_created":"2019-10-02T11:13:54Z","content_type":"application/pdf","relation":"main_file","access_level":"open_access","file_id":"6928","checksum":"b2256c9117655bc15f621ba0babf219f"}],"scopus_import":"1","intvolume":" 5","month":"09","oa_version":"Published Version","department":[{"_id":"LeSa"}],"file_date_updated":"2020-07-14T12:47:44Z","date_updated":"2023-08-30T06:55:31Z","ddc":["570"],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","image":"/images/cc_by_nc.png","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)"},"type":"journal_article","status":"public","_id":"6919","date_created":"2019-09-29T22:00:45Z","date_published":"2019-09-18T00:00:00Z","doi":"10.1126/sciadv.aaw6490","year":"2019","isi":1,"has_accepted_license":"1","publication":"Science Advances","day":"18","oa":1,"publisher":"American Association for the Advancement of Science","quality_controlled":"1","article_processing_charge":"No","external_id":{"isi":["000491128800062"]},"author":[{"last_name":"Qi","full_name":"Qi, Chao","first_name":"Chao"},{"last_name":"Minin","full_name":"Minin, Giulio Di","first_name":"Giulio Di"},{"last_name":"Vercellino","full_name":"Vercellino, Irene","orcid":"0000-0001-5618-3449","first_name":"Irene","id":"3ED6AF16-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Anton","full_name":"Wutz, Anton","last_name":"Wutz"},{"full_name":"Korkhov, Volodymyr M.","last_name":"Korkhov","first_name":"Volodymyr M."}],"title":"Structural basis of sterol recognition by human hedgehog receptor PTCH1","citation":{"short":"C. Qi, G.D. Minin, I. Vercellino, A. Wutz, V.M. Korkhov, Science Advances 5 (2019).","ieee":"C. Qi, G. D. Minin, I. Vercellino, A. Wutz, and V. M. Korkhov, “Structural basis of sterol recognition by human hedgehog receptor PTCH1,” Science Advances, vol. 5, no. 9. American Association for the Advancement of Science, 2019.","ama":"Qi C, Minin GD, Vercellino I, Wutz A, Korkhov VM. Structural basis of sterol recognition by human hedgehog receptor PTCH1. Science Advances. 2019;5(9). doi:10.1126/sciadv.aaw6490","apa":"Qi, C., Minin, G. D., Vercellino, I., Wutz, A., & Korkhov, V. M. (2019). Structural basis of sterol recognition by human hedgehog receptor PTCH1. Science Advances. American Association for the Advancement of Science. https://doi.org/10.1126/sciadv.aaw6490","mla":"Qi, Chao, et al. “Structural Basis of Sterol Recognition by Human Hedgehog Receptor PTCH1.” Science Advances, vol. 5, no. 9, eaaw6490, American Association for the Advancement of Science, 2019, doi:10.1126/sciadv.aaw6490.","ista":"Qi C, Minin GD, Vercellino I, Wutz A, Korkhov VM. 2019. Structural basis of sterol recognition by human hedgehog receptor PTCH1. Science Advances. 5(9), eaaw6490.","chicago":"Qi, Chao, Giulio Di Minin, Irene Vercellino, Anton Wutz, and Volodymyr M. Korkhov. “Structural Basis of Sterol Recognition by Human Hedgehog Receptor PTCH1.” Science Advances. American Association for the Advancement of Science, 2019. https://doi.org/10.1126/sciadv.aaw6490."},"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","article_number":"eaaw6490"}]