Mahieu, E.; Covès, J.; Krüger, G.; Martel, A.; Moulin, M. et al.: Observing Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering. In: Biophysical Journal 119 (2020), Nr. 2, S. 375-388. DOI: https://doi.org/10.1016/j.bpj.2020.06.015
Zusammenfassung: | |
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. © 2020 Biophysical Society | |
Lizenzbestimmungen: | CC BY-NC-ND 4.0 Unported |
Publikationstyp: | Article |
Publikationsstatus: | publishedVersion |
Erstveröffentlichung: | 2020 |
Die Publikation erscheint in Sammlung(en): | Forschungszentren |
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