Observing Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering.
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Authors
Mahieu, EmilieCovès, Jacques
Krüger, Georg
Martel, Anne
Moulin, Martine
Carl, Nico
Härtlein, Michael
Carlomagno, Teresa

Franzetti, Bruno
Gabel, Frank
Issue Date
2020-06-24
Metadata
Show full item recordAbstract
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.Citation
Biophys J. 2020;119(2):375-388. doi:10.1016/j.bpj.2020.06.015.Affiliation
HZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.Publisher
ElsevierJournal
Biophysical journalPubMed ID
32640186Type
ArticleLanguage
enEISSN
1542-0086ae974a485f413a2113503eed53cd6c53
10.1016/j.bpj.2020.06.015
Scopus Count
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- Creative Commons
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-ShareAlike 4.0 International
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