ArticleMolecular microbiology2021
The McdAB system positions α-carboxysomes in proteobacteria.
Article in Molecular microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed, 47 citations in OpenAlex.
- Bacterial ribonucleoprotein bodies maintain an acidic pH environment as a mechanism of enzyme regulation.Nature communications · 2026Article
- Bacterial Sentience Is Determined by the Stochastic, Chaotic, and Deterministic Behavior of Cytoplasmic Particles.Current issues in molecular biology · 2026Review
- 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
- Assembly and Functional Coordination of Two Families of Metabolic Organelles in Salmonella.Microbial biotechnology · 2026Article
- Molecular insights into phycobilisome assembly pathway reveal crystalline bodies in cyanobacteria.bioRxiv : the preprint server for biology · 2025Article
- Article
- Molecular basis of the biogenesis of a protein organelle for ethanolamine utilization.Science advances · 2025Article
- Brownian ratchet mechanisms for carboxysome positioning in bacteria.Current opinion in microbiology · 2025Review
- A blueprint for biomolecular condensation driven by bacterial microcompartment encapsulation peptides.Nature communications · 2025Article
- Organizing organelles: bacterial strategies for localizing intracellular compartments.Current opinion in microbiology · 2025Review
- Robust Synthetic Biology Toolkit to Advance Carboxysome Study and Redesign.ACS synthetic biology · 2025Article
- Tuning the interaction of a ParA-type ATPase with its partner separates bacterial organelle positioning from partitioning.Research square · 2025Article
- Tuning the interaction of a ParA-type ATPase with its partner separates bacterial organelle positioning from partitioning.bioRxiv : the preprint server for biology · 2025Article
- Revealing the diversity of bacterial and archaeal organelles via comparative genomics.Molecular biology of the cell · 2025Review
- An invariant C-terminal tryptophan in McdB mediates its interaction and positioning function with carboxysomes.Molecular biology of the cell · 2024Article
- Positioning of cellular components by the ParA/MinD family of ATPases.Current opinion in microbiology · 2024Review
- A programmable reaction-diffusion system for spatiotemporal cell signaling circuit design.Cell · 2024Article
- Intrinsically disordered CsoS2 acts as a general molecular thread for α-carboxysome shell assembly.Nature communications · 2023Article
- Dissecting the phase separation and oligomerization activities of the carboxysome positioning protein McdB.eLife · 2023Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carboxysomes are protein-based organelles essential for carbon fixation in cyanobacteria and proteobacteria. Previously, we showed that the cyanobacterial nucleoid is used to equally space out β-carboxysomes across cell lengths by a two-component system (McdAB) in the model cyanobacterium Synechococcus elongatus PCC 7942. More recently, we found that McdAB systems are widespread among β-cyanobacteria, which possess β-carboxysomes, but are absent in α-cyanobacteria, which possess structurally and phyletically distinct α-carboxysomes. Cyanobacterial α-carboxysomes are thought to have arisen in proteobacteria and then horizontally transferred into cyanobacteria, which suggests that α-carboxysomes in proteobacteria may also lack the McdAB system. Here, using the model chemoautotrophic proteobacterium Halothiobacillus neapolitanus, we show that a McdAB system distinct from that of β-cyanobacteria operates to position α-carboxysomes across cell lengths. We further show that this system is widespread among α-carboxysome-containing proteobacteria and that cyanobacteria likely inherited an α-carboxysome operon from a proteobacterium lacking the mcdAB locus. These results demonstrate that McdAB is a cross-phylum two-component system necessary for positioning both α- and β-carboxysomes. The findings have further implications for understanding the positioning of other protein-based bacterial organelles involved in diverse metabolic processes. PLAIN LANGUAGE SUMMARY: Cyanobacteria are well known to fix atmospheric CO
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