--- _id: '8437' abstract: - lang: eng text: Chaperonins are ubiquitous protein assemblies present in bacteria, eukaryota, and archaea, facilitating the folding of proteins, preventing protein aggregation, and thus participating in maintaining protein homeostasis in the cell. During their functional cycle, they bind unfolded client proteins inside their double ring structure and promote protein folding by closing the ring chamber in an adenosine 5′-triphosphate (ATP)–dependent manner. Although the static structures of fully open and closed forms of chaperonins were solved by x-ray crystallography or electron microscopy, elucidating the mechanisms of such ATP-driven molecular events requires studying the proteins at the structural level under working conditions. We introduce an approach that combines site-specific nuclear magnetic resonance observation of very large proteins, enabled by advanced isotope labeling methods, with an in situ ATP regeneration system. Using this method, we provide functional insight into the 1-MDa large hsp60 chaperonin while processing client proteins and reveal how nucleotide binding, hydrolysis, and release control switching between closed and open states. While the open conformation stabilizes the unfolded state of client proteins, the internalization of the client protein inside the chaperonin cavity speeds up its functional cycle. This approach opens new perspectives to study structures and mechanisms of various ATP-driven biological machineries in the heat of action. article_number: eaau4196 article_processing_charge: No article_type: original author: - first_name: Guillaume full_name: Mas, Guillaume last_name: Mas - first_name: Jia-Ying full_name: Guan, Jia-Ying last_name: Guan - first_name: Elodie full_name: Crublet, Elodie last_name: Crublet - first_name: Elisa Colas full_name: Debled, Elisa Colas last_name: Debled - first_name: Christine full_name: Moriscot, Christine last_name: Moriscot - first_name: Pierre full_name: Gans, Pierre last_name: Gans - first_name: Guy full_name: Schoehn, Guy last_name: Schoehn - first_name: Pavel full_name: Macek, Pavel last_name: Macek - first_name: Paul full_name: Schanda, Paul id: 7B541462-FAF6-11E9-A490-E8DFE5697425 last_name: Schanda orcid: 0000-0002-9350-7606 - first_name: Jerome full_name: Boisbouvier, Jerome last_name: Boisbouvier citation: ama: Mas G, Guan J-Y, Crublet E, et al. Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. Science Advances. 2018;4(9). doi:10.1126/sciadv.aau4196 apa: Mas, G., Guan, J.-Y., Crublet, E., Debled, E. C., Moriscot, C., Gans, P., … Boisbouvier, J. (2018). Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. Science Advances. American Association for the Advancement of Science. https://doi.org/10.1126/sciadv.aau4196 chicago: Mas, Guillaume, Jia-Ying Guan, Elodie Crublet, Elisa Colas Debled, Christine Moriscot, Pierre Gans, Guy Schoehn, Pavel Macek, Paul Schanda, and Jerome Boisbouvier. “Structural Investigation of a Chaperonin in Action Reveals How Nucleotide Binding Regulates the Functional Cycle.” Science Advances. American Association for the Advancement of Science, 2018. https://doi.org/10.1126/sciadv.aau4196. ieee: G. Mas et al., “Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle,” Science Advances, vol. 4, no. 9. American Association for the Advancement of Science, 2018. ista: Mas G, Guan J-Y, Crublet E, Debled EC, Moriscot C, Gans P, Schoehn G, Macek P, Schanda P, Boisbouvier J. 2018. Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. Science Advances. 4(9), eaau4196. mla: Mas, Guillaume, et al. “Structural Investigation of a Chaperonin in Action Reveals How Nucleotide Binding Regulates the Functional Cycle.” Science Advances, vol. 4, no. 9, eaau4196, American Association for the Advancement of Science, 2018, doi:10.1126/sciadv.aau4196. short: G. Mas, J.-Y. Guan, E. Crublet, E.C. Debled, C. Moriscot, P. Gans, G. Schoehn, P. Macek, P. Schanda, J. Boisbouvier, Science Advances 4 (2018). date_created: 2020-09-18T10:04:51Z date_published: 2018-09-19T00:00:00Z date_updated: 2022-08-26T09:11:06Z day: '19' doi: 10.1126/sciadv.aau4196 extern: '1' intvolume: ' 4' issue: '9' language: - iso: eng month: '09' oa_version: None publication: Science Advances publication_identifier: issn: - 2375-2548 publication_status: published publisher: American Association for the Advancement of Science quality_controlled: '1' status: public title: Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle type: journal_article user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87 volume: 4 year: '2018' ...