ArticlePloS one2009
The pentameric vertex proteins are necessary for the icosahedral carboxysome shell to function as a CO2 leakage barrier.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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Who cites it
81 citing papers in PubMed, 132 citations in OpenAlex.
- Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.Biochemistry · 2026Review
- From fundamental understanding to engineering of carboxysomes for biotechnological applications.Plant communications · 2026Review
- "Air-Lock" gating mechanism of CsoS1D for metabolite translocation through the α-carboxysome shell.Plant physiology · 2026Article
- Recent insights into α-carboxysome structure, mechanism, and assembly.Journal of bacteriology · 2026Review
- Assembly and Functional Coordination of Two Families of Metabolic Organelles in Salmonella.Microbial biotechnology · 2026Article
- Structure and encapsulation of carbonic anhydrase within the α-carboxysome.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular basis of the biogenesis of a protein organelle for ethanolamine utilization.Science advances · 2025Article
- Robust Synthetic Biology Toolkit to Advance Carboxysome Study and Redesign.ACS synthetic biology · 2025Article
- Quantitative Measurement of Molecular Permeability to a Synthetic Bacterial Microcompartment Shell System.ACS synthetic biology · 2025Article
- Molecular principles of the assembly and construction of a carboxysome shell.Science advances · 2024Article
- Label-Free Anti-Brownian Trapping of Single Nanoparticles in Solution.The journal of physical chemistry. C, Nanomaterials and interfaces · 2024Article
- Article
- Evidence of a putative COEnvironmental microbiology reports · 2024Article
- α-Carboxysome Size Is Controlled by the Disordered Scaffold Protein CsoS2.Biochemistry · 2024Article
- Modeling bacterial microcompartment architectures for enhanced cyanobacterial carbon fixation.Frontiers in plant science · 2024Review
- Identification of a carbonic anhydrase-Rubisco complex within the alpha-carboxysome.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Monatomic ions influence substrate permeation across bacterial microcompartment shells.Scientific reports · 2023Article
- Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly.Nature communications · 2023Article
- Heterologous Assembly of Pleomorphic Bacterial Microcompartment Shell Architectures Spanning the Nano- to Microscale.Advanced materials (Deerfield Beach, Fla.) · 2023Article
- Towards engineering a hybrid carboxysome.Photosynthesis research · 2023Article
21 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCarboxysomes are polyhedral protein microcompartments found in many autotrophic bacteria; they encapsulate the CO(2) fixing enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) within a thin protein shell and provide an environment that enhances the catalytic capabilities of the enzyme. Two types of shell protein constituents are common to carboxysomes and related microcompartments of heterotrophic bacteria, and the genes for these proteins are found in a large variety of bacteria. METHODOLOGY/PRINCIPAL
findingsWe have created a Halothiobacillus neapolitanus knockout mutant that does not produce the two paralogous CsoS4 proteins thought to occupy the vertices of the icosahedral carboxysomes and related microcompartments. Biochemical and ultrastructural analyses indicated that the mutant predominantly forms carboxysomes of normal appearance, in addition to some elongated microcompartments. Despite their normal shape, purified mutant carboxysomes are functionally impaired, although the activities of the encapsulated enzymes are not negatively affected. CONCLUSIONS/SIGNIFICANCE: In the absence of the CsoS4 proteins the carboxysome shell loses its limited permeability to CO(2) and is no longer able to provide the catalytic advantage RubisCO derives from microcompartmentalization. This study presents direct evidence that the diffusion barrier property of the carboxysome shell contributes significantly to the biological function of the carboxysome.
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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 OpenQuestion graph.