ArticleNature structural & molecular biology2023
Structure of the preholoproteasome reveals late steps in proteasome core particle biogenesis.
Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026Review
- Magical moments in protease biology: proteasome autocatalytic activation and PI31-mediated inhibition.Trends in biochemical sciences · 2026Review
- Structural transitions in the stepwise assembly of proteasome core particles.Nature communications · 2026Article
- The α5-α6-α7-Pba3-Pba4 Complex: A Starting Unit in Proteasome Core Particle Assembly.Biomolecules · 2025Article
- Structural basis for allosteric modulation of M. tuberculosis proteasome core particle.Nature communications · 2025Article
- Evidence supporting a catalytic pentad mechanism for the proteasome and other N-terminal nucleophile enzymes.Nature communications · 2025Article
- Molecular basis for the stepwise and faithful maturation of the 20Science advances · 2025Article
- Structural roles of Ump1 and β-subunit propeptides in proteasome biogenesis.Life science alliance · 2024Article
- Structural basis of human 20S proteasome biogenesis.Nature communications · 2024Article
- Visualizing chaperone-mediated multistep assembly of the human 20S proteasome.Nature structural & molecular biology · 2024Article
- Mechanism of autocatalytic activation during proteasome assembly.Nature structural & molecular biology · 2024Article
- Visualizing chaperone-mediated multistep assembly of the human 20S proteasome.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Assembly of the proteasome's core particle (CP), a barrel-shaped chamber of four stacked rings, requires five chaperones and five subunit propeptides. Fusion of two half-CP precursors yields a complete structure but remains immature until active site maturation. Here, using Saccharomyces cerevisiae, we report a high-resolution cryogenic electron microscopy structure of preholoproteasome, a post-fusion assembly intermediate. Our data reveal how CP midline-spanning interactions induce local changes in structure, facilitating maturation. Unexpectedly, we find that cleavage may not be sufficient for propeptide release, as residual interactions with chaperones such as Ump1 hold them in place. We evaluated previous models proposing that dynamic conformational changes in chaperones drive CP fusion and autocatalytic activation by comparing preholoproteasome to pre-fusion intermediates. Instead, the data suggest a scaffolding role for the chaperones Ump1 and Pba1/Pba2. Our data clarify key aspects of CP assembly, suggest that undiscovered mechanisms exist to explain CP fusion/activation, and have relevance for diseases of defective CP biogenesis.
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Registered trials
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