ArticleBiophysical journal2020
Observing Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- A Bayesian Approach to Interpret Time-Resolved Experiments Using Molecular Simulations.ACS physical chemistry Au · 2026Article
- Current and future perspectives for structural biology at the Grenoble EPN campus: a comprehensive overview.Journal of synchrotron radiation · 2025Review
- Recent Progress in Solution Structure Studies of Photosynthetic Proteins Using Small-Angle Scattering Methods.Molecules (Basel, Switzerland) · 2023Review
- Characterization of a small tRNA-binding protein that interacts with the archaeal proteasome complex.Molecular microbiology · 2022Article
- Small-angle neutron scattering contrast variation studies of biological complexes: Challenges and triumphs.Current opinion in structural biology · 2022Review
- Approaches to Evaluate the Impact of a Small-Molecule Binder to a Noncatalytic Site of the Proteasome.Chembiochem : a European journal of chemical biology · 2021Article
- Hiding the Elephant in the Room with Experimental Neutrons.Biophysical journal · 2020Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.