ArticleThe EMBO journal1992
Subunit stoichiometry and three-dimensional arrangement in proteasomes from Thermoplasma acidophilum.
Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 181 citations in OpenAlex.
- Mechanisms and Design Principles of Proteolysis-Targeting Chimeras and Their Emerging Applications.ACS pharmacology & translational science · 2026Review
- Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025Review
- Visualizing Proteasome Activity and Intracellular Localization Using Fluorescent Proteins and Activity-Based Probes.Frontiers in molecular biosciences · 2019Article
- Structural insights into the functional cycle of the ATPase module of the 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Molecular and functional characterization of a putative PA28γ proteasome activator orthologue in Schistosoma mansoni.Molecular and biochemical parasitology · 2013Article
- Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The C terminus of Rpt3, an ATPase subunit of PA700 (19 S) regulatory complex, is essential for 26 S proteasome assembly but not for activation.The Journal of biological chemistry · 2010Article
- Toward an integrated structural model of the 26S proteasome.Molecular & cellular proteomics : MCP · 2010Article
- A voyage to the inner space of cells.Protein science : a publication of the Protein Society · 2005Article
- Substrate affinity and substrate specificity of proteasomes with RNase activity.Molecular biology reports · 2003Article
- Lysine 188 substitutions convert the pattern of proteasome activation by REGgamma to that of REGs alpha and beta.The EMBO journal · 2001Article
- Functional regulation of immunoproteasomes and transporter associated with antigen processing.Immunologic research · 2001Review
- The proteasome: a macromolecular assembly designed for controlled proteolysis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 1999Review
- Involvement of proteasomal subunits zeta and iota in RNA degradation.The Biochemical journal · 1997Article
- Subunit arrangement in the human 20S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Purification and Characterization of a Proteasome from the Hyperthermophilic Archaeon Pyrococcus furiosus.Applied and environmental microbiology · 1997Article
- Eubacterial proteasomes.Molecular biology reports · 1997Review
- Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis.The EMBO journal · 1996Article
- Proteasome alpha-type subunit C9 is a primary target of autoantibodies in sera of patients with myositis and systemic lupus erythematosus.The Journal of experimental medicine · 1996Article
- Proteasome complex as a potential cellular target of hepatitis B virus X protein.Journal of virology · 1996Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proteasome or multicatalytic proteinase from the archaebacterium Thermoplasma acidophilum is a 700 kDa multisubunit protein complex. Unlike proteasomes from eukaryotic cells which are composed of 10-20 different subunits, the Thermoplasma proteasome is made of only two types of subunit, alpha and beta, which have molecular weights of 25.8 and 22.3 kDa, respectively. In this communication we present a three-dimensional stoichiometric model of the archaebacterial proteasome deduced from electron microscopic investigations. The techniques which we have used include image analysis of negatively stained single particles, image analysis of metal decorated small three-dimensional crystals after freeze-etching and STEM mass measurements of freeze-dried particles. The archaebacterial and eukaryotic proteasomes are almost identical in size and shape; the subunits are arranged in four rings which are stacked together such that they collectively form a barrel-shaped complex. According to a previous immunoelectron microscopic investigation, the alpha-subunits form the two outer rings of the stack, while the two rings composed of beta-subunits, which are supposed to carry the active sites, are sandwiched between them. Each of the alpha- and beta-rings contains seven subunits; hence the stoichiometry of the whole proteasome is alpha 14 beta 14 and the symmetry is 7-fold. Image simulation experiments indicate that the alpha- and beta-subunits are not in register along the cylinder axis; rather it appears that the beta-rings are rotated with respect to the alpha-rings by approximately 25 degrees. In contrast to some previous reports we have not been able to find stoichiometric amounts of RNA associated with highly purified proteolytically active proteasome preparations.
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