ArticleScientific reports2015
Disassembly of the self-assembled, double-ring structure of proteasome α7 homo-tetradecamer by α6.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026Review
- Structural Fluctuations of the Human Proteasome α7 Homo-Tetradecamer Double Ring Imply the Proteasomal α-Ring Assembly Mechanism.International journal of molecular sciences · 2021Article
- Supramolecular tholos-like architecture constituted by archaeal proteins without functional annotation.Scientific reports · 2020Article
- Overexpression of PSMA7 predicts poor prognosis in patients with gastric cancer.Oncology letters · 2019Article
- Proteasome subunit α1 overexpression preferentially drives canonical proteasome biogenesis and enhances stress tolerance in yeast.Scientific reports · 2019Article
- Mutational and Combinatorial Control of Self-Assembling and Disassembling of Human Proteasome α Subunits.International journal of molecular sciences · 2019Article
- Molecular and Structural Basis of the Proteasome α Subunit Assembly Mechanism Mediated by the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer.International journal of molecular sciences · 2019Article
- SDS-induced oligomerization of Lys49-phospholipase AScientific reports · 2019Article
- Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation.Frontiers in molecular biosciences · 2019Review
- Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase.Communications biology · 2019Article
- Expression, Functional Characterization, and Preliminary Crystallization of the Cochaperone Prefoldin from the Thermophilic FungusInternational journal of molecular sciences · 2018Article
- Dynamic structural states of ClpB involved in its disaggregation function.Nature communications · 2018Article
- Structural insights on the dynamics of proteasome formation.Biophysical reviews · 2018Review
- RecA requires two molecules of Mg2+ ions for its optimal strand exchange activity in vitro.Nucleic acids research · 2018Article
- Two-step process for disassembly mechanism of proteasome α7 homo-tetradecamer by α6 revealed by high-speed atomic force microscopy.Scientific reports · 2017Article
- Proteasome Structure and Assembly.Journal of molecular biology · 2017Review
- A Comprehensive Study of the Interaction between Peptidoglycan Fragments and the Extracellular Domain of Mycobacterium tuberculosis Ser/Thr Kinase PknB.Chembiochem : a European journal of chemical biology · 2017Article
- New insight into the dynamical system of αB-crystallin oligomers.Scientific reports · 2016Article
- Article
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8 authors.
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Abstract
The 20S core particle of the eukaryotic proteasome is composed of two α- and two β-rings, each of which is a hetero-heptamer composed of seven homologous but distinct subunits. Although formation of the eukaryotic proteasome is a highly ordered process assisted by assembly chaperones, α7, an α-ring component, has the unique property of self-assembling into a homo-tetradecamer. We used biophysical methods to characterize the oligomeric states of this proteasome subunit and its interaction with α6, which makes direct contacts with α7 in the proteasome α-ring. We determined a crystal structure of the α7 tetradecamer, which has a double-ring structure. Sedimentation velocity analytical ultracentrifugation and mass spectrometric analysis under non-denaturing conditions revealed that α7 exclusively exists as homo-tetradecamer in solution and that its double-ring structure is disassembled upon the addition of α6, resulting in a 1:7 hetero-octameric α6-α7 complex. Our findings suggest that proteasome formation involves the disassembly of non-native oligomers, which are assembly intermediates.
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