ArticleNature communications2022
Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Unlocking the bacterial condensome: from "dark matter" to design.Molecular biology of the cell · 2026Article
- Mechanistic insights into lenacapavir-induced off-pathway HIV-1 capsid assembly.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- 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
- Robust Synthetic Biology Toolkit to Advance Carboxysome Study and Redesign.ACS synthetic biology · 2025Article
- Hierarchical metabolic engineering for rewiring cellular metabolism.FEMS microbiology reviews · 2025Review
- Promiscuous structural cross-compatibilities between major shell components of Klebsiella pneumoniae bacterial microcompartments.PloS one · 2025Article
- Electrochemical cofactor recycling of bacterial microcompartments.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Modeling bacterial microcompartment architectures for enhanced cyanobacterial carbon fixation.Frontiers in plant science · 2024Review
- Inferring assembly-curving trends of bacterial micro-compartment shell hexamers from crystal structure arrangements.PLoS computational biology · 2023Article
- Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology.Nature communications · 2022Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Engineering subcellular organization in microbes shows great promise in addressing bottlenecks in metabolic engineering efforts; however, rules guiding selection of an organization strategy or platform are lacking. Here, we study compartment morphology as a factor in mediating encapsulated pathway performance. Using the 1,2-propanediol utilization microcompartment (Pdu MCP) system from Salmonella enterica serovar Typhimurium LT2, we find that we can shift the morphology of this protein nanoreactor from polyhedral to tubular by removing vertex protein PduN. Analysis of the metabolic function between these Pdu microtubes (MTs) shows that they provide a diffusional barrier capable of shielding the cytosol from a toxic pathway intermediate, similar to native MCPs. However, kinetic modeling suggests that the different surface area to volume ratios of MCP and MT structures alters encapsulated pathway performance. Finally, we report a microscopy-based assay that permits rapid assessment of Pdu MT formation to enable future engineering efforts on these structures.
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