Observing Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering.
dc.contributor.author | Mahieu, Emilie | |
dc.contributor.author | Covès, Jacques | |
dc.contributor.author | Krüger, Georg | |
dc.contributor.author | Martel, Anne | |
dc.contributor.author | Moulin, Martine | |
dc.contributor.author | Carl, Nico | |
dc.contributor.author | Härtlein, Michael | |
dc.contributor.author | Carlomagno, Teresa | |
dc.contributor.author | Franzetti, Bruno | |
dc.contributor.author | Gabel, Frank | |
dc.date.accessioned | 2020-09-04T10:50:05Z | |
dc.date.available | 2020-09-04T10:50:05Z | |
dc.date.issued | 2020-06-24 | |
dc.identifier.citation | Biophys J. 2020;119(2):375-388. doi:10.1016/j.bpj.2020.06.015. | en_US |
dc.identifier.pmid | 32640186 | |
dc.identifier.doi | 10.1016/j.bpj.2020.06.015 | |
dc.identifier.uri | http://hdl.handle.net/10033/622428 | |
dc.description.abstract | The 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.iso | en | en_US |
dc.publisher | Elsevier | en_US |
dc.rights | Attribution-NonCommercial-ShareAlike 4.0 International | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.title | Observing Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering. | en_US |
dc.type | Article | en_US |
dc.identifier.eissn | 1542-0086 | |
dc.contributor.department | HZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany. | en_US |
dc.identifier.journal | Biophysical journal | en_US |
dc.source.volume | 119 | |
dc.source.issue | 2 | |
dc.source.beginpage | 375 | |
dc.source.endpage | 388 | |
refterms.dateFOA | 2020-09-04T10:50:06Z | |
dc.source.journaltitle | Biophysical journal | |
dc.source.country | United States |