ReviewMicrobiology and molecular biology reviews : MMBR2013
Functions, compositions, and evolution of the two types of carboxysomes: polyhedral microcompartments that facilitate CO2 fixation in cyanobacteria and some proteobacteria.
Review in Microbiology and molecular biology reviews : MMBR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 205 papers.
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Who cites it
205 citing papers in PubMed, 418 citations in OpenAlex.
- Structural insights into the coupling mechanism of vectorial COProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Cyanobacterial conversion of COChemical science · 2026Review
- Rubisco kinetic diversity and effectiveness of CO2-concentrating mechanisms in aquatic photosynthetic organisms.Plant physiology · 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
- Functional and structural insights into cyanobacterial COThe Plant journal : for cell and molecular biology · 2026Review
- Article
- Functional characterization of bicarbonate transporters from the cyanobacterial SbtA2 family and subsequent expression in tobacco.Journal of experimental botany · 2026Article
- A molecular basis for stoichiometric enzyme encapsulation in the vitamin B2 biosynthesis compartment.Nature communications · 2026Article
- Architectural and biochemical advances in understanding microbial COThe Plant journal : for cell and molecular biology · 2026Review
- The molecular mechanism of the cyanobacterial bicarbonate importer CmpABCD activated by the intracellular nitrate.Nature communications · 2026Article
- Using Cryogenic Electron Tomography (cryoET) to Determine Rubisco Polymerization Constants in α-Carboxysomes.bioRxiv : the preprint server for biology · 2026Article
- Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction.Nature communications · 2026Article
- The kinetics and mobility of a ParA ATPase drive carboxysome distribution inbioRxiv : the preprint server for biology · 2026Article
- Recent insights into α-carboxysome structure, mechanism, and assembly.Journal of bacteriology · 2026Review
- Stages of biomolecular condensate formation in pro-β-carboxysome assembly.Nature plants · 2026Article
- Structure of Chlamydomonas reinhardtii LciA guided the engineering of FNT family proteins to gain bicarbonate transport activity.Nature plants · 2026Article
- The Role of Confinement in Biomineralization.Chemical reviews · 2025Review
- Unusual regulation of the COApplied and environmental microbiology · 2025Article
- Structure and encapsulation of carbonic anhydrase within the α-carboxysome.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
145 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyanobacteria are the globally dominant photoautotrophic lineage. Their success is dependent on a set of adaptations collectively termed the CO2-concentrating mechanism (CCM). The purpose of the CCM is to support effective CO2 fixation by enhancing the chemical conditions in the vicinity of the primary CO2-fixing enzyme, D-ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO), to promote the carboxylase reaction and suppress the oxygenase reaction. In cyanobacteria and some proteobacteria, this is achieved by encapsulation of RubisCO within carboxysomes, which are examples of a group of proteinaceous bodies called bacterial microcompartments. Carboxysomes encapsulate the CO2-fixing enzyme within the selectively permeable protein shell and simultaneously encapsulate a carbonic anhydrase enzyme for CO2 supply from a cytoplasmic bicarbonate pool. These bodies appear to have arisen twice and undergone a process of convergent evolution. While the gross structures of all known carboxysomes are ostensibly very similar, with shared gross features such as a selectively permeable shell layer, each type of carboxysome encapsulates a phyletically distinct form of RubisCO enzyme. Furthermore, the specific proteins forming structures such as the protein shell or the inner RubisCO matrix are not identical between carboxysome types. Each type has evolutionarily distinct forms of the same proteins, as well as proteins that are entirely unrelated to one another. In light of recent developments in the study of carboxysome structure and function, we present this review to summarize the knowledge of the structure and function of both types of carboxysome. We also endeavor to cast light on differing evolutionary trajectories which may have led to the differences observed in extant carboxysomes.
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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.