ArticleThe Journal of biological chemistry2012
Elucidating essential role of conserved carboxysomal protein CcmN reveals common feature of bacterial microcompartment assembly.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.
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99 citing papers in PubMed, 176 citations in OpenAlex.
- Employing Nanotechnology to Enhance Ethanol Production in Two Synechococcus elongatus Strains.Chembiochem : a European journal of chemical biology · 2026Article
- Overexpression of β-carboxysomes increases photosynthesis and growth in Synechocystis sp. PCC 6803.Plant physiology · 2026Article
- Functional and structural insights into cyanobacterial COThe Plant journal : for cell and molecular biology · 2026Review
- Many paths, similar destinations: viruses and bacterial microcompartments form polyhedra inside cells.Journal of virology · 2026Review
- Review
- Carbon dioxide concentration alters cyanobacterial carboxysome encapsulation and redox state in Synechococcus sp. PCC 7002.Communications biology · 2026Article
- Architectural and biochemical advances in understanding microbial COThe Plant journal : for cell and molecular biology · 2026Review
- [COResearch square · 2026Article
- Stages of biomolecular condensate formation in pro-β-carboxysome assembly.Nature plants · 2026Article
- A blueprint for biomolecular condensation driven by bacterial microcompartment encapsulation peptides.Nature communications · 2025Article
- A Two-Component Pseudo-Icosahedral Protein Nanocompartment with Variable Shell Composition and Irregular Tiling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Understanding carboxysomes to enhance carbon fixation in crops.Biochemical Society transactions · 2025Review
- Article
- Carboxysome Shell Protein CcmK2 Assembles into Monodisperse and pH-Reversible Microparticles.ACS nano · 2025Article
- Chaotrope-Based Approach for Rapid In Vitro Assembly and Loading of Bacterial Microcompartment Shells.ACS nano · 2025Article
- Article
- Towards assembling functional cyanobacterial β-carboxysomes in Oryza sativa chloroplasts.Functional & integrative genomics · 2025Article
- Promiscuous structural cross-compatibilities between major shell components of Klebsiella pneumoniae bacterial microcompartments.PloS one · 2025Article
- Rubisco packaging and stoichiometric composition of the native β-carboxysome in Synechococcus elongatus PCC7942.Plant physiology · 2024Article
- Characterization of a widespread sugar phosphate-processing bacterial microcompartment.Communications biology · 2024Article
39 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial microcompartments are organelles composed of a protein shell that surrounds functionally related proteins. Bioinformatic analysis of sequenced genomes indicates that homologs to shell protein genes are widespread among bacteria and suggests that the shell proteins are capable of encapsulating diverse enzymes. The carboxysome is a bacterial microcompartment that enhances CO(2) fixation in cyanobacteria and some chemoautotrophs by sequestering ribulose-1,5-bisphosphate carboxylase/oxygenase and carbonic anhydrase in the microcompartment shell. Here, we report the in vitro and in vivo characterization of CcmN, a protein of previously unknown function that is absolutely conserved in β-carboxysomal gene clusters. We show that CcmN localizes to the carboxysome and is essential for carboxysome biogenesis. CcmN has two functionally distinct regions separated by a poorly conserved linker. The N-terminal portion of the protein is important for interaction with CcmM and, by extension, ribulose-1,5-bisphosphate carboxylase/oxygenase and the carbonic anhydrase CcaA, whereas the C-terminal peptide is essential for interaction with the carboxysome shell. Deletion of the peptide abolishes carboxysome formation, indicating that its interaction with the shell is an essential step in microcompartment formation. Peptides with similar length and sequence properties to those in CcmN can be bioinformatically detected in a large number of diverse proteins proposed to be encapsulated in functionally distinct microcompartments, suggesting that this peptide and its interaction with its cognate shell proteins are common features of microcompartment assembly.
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