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dc.contributor.authorMahieu, Emilie
dc.contributor.authorCovès, Jacques
dc.contributor.authorKrüger, Georg
dc.contributor.authorMartel, Anne
dc.contributor.authorMoulin, Martine
dc.contributor.authorCarl, Nico
dc.contributor.authorHärtlein, Michael
dc.contributor.authorCarlomagno, Teresa
dc.contributor.authorFranzetti, Bruno
dc.contributor.authorGabel, Frank
dc.date.accessioned2020-09-04T10:50:05Z
dc.date.available2020-09-04T10:50:05Z
dc.date.issued2020-06-24
dc.identifier.citationBiophys J. 2020;119(2):375-388. doi:10.1016/j.bpj.2020.06.015.en_US
dc.identifier.pmid32640186
dc.identifier.doi10.1016/j.bpj.2020.06.015
dc.identifier.urihttp://hdl.handle.net/10033/622428
dc.description.abstractThe proteasome is a key player of regulated protein degradation in all kingdoms of life. Although recent atomic structures have provided snapshots on a number of conformations, data on substrate states and populations during the active degradation process in solution remain scarce. Here, we use time-resolved small-angle neutron scattering of a deuterium-labeled GFPssrA substrate and an unlabeled archaeal PAN-20S system to obtain direct structural information on substrate states during ATP-driven unfolding and subsequent proteolysis in solution. We find that native GFPssrA structures are degraded in a biexponential process, which correlates strongly with ATP hydrolysis, the loss of fluorescence, and the buildup of small oligopeptide products. Our solution structural data support a model in which the substrate is directly translocated from PAN into the 20S proteolytic chamber, after a first, to our knowledge, successful unfolding process that represents a point of no return and thus prevents dissociation of the complex and the release of harmful, aggregation-prone products.en_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleObserving Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering.en_US
dc.typeArticleen_US
dc.identifier.eissn1542-0086
dc.contributor.departmentHZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.en_US
dc.identifier.journalBiophysical journalen_US
dc.source.volume119
dc.source.issue2
dc.source.beginpage375
dc.source.endpage388
refterms.dateFOA2020-09-04T10:50:06Z
dc.source.journaltitleBiophysical journal
dc.source.countryUnited States


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Attribution-NonCommercial-ShareAlike 4.0 International
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-ShareAlike 4.0 International