ArticleNature communications2018
De novo targeting to the cytoplasmic and luminal side of bacterial microcompartments.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed.
- From fundamental understanding to engineering of carboxysomes for biotechnological applications.Plant communications · 2026Review
- Robust Synthetic Biology Toolkit to Advance Carboxysome Study and Redesign.ACS synthetic biology · 2025Article
- Interfacing bacterial microcompartment shell proteins with genetically encoded condensates.Protein science : a publication of the Protein Society · 2025Article
- Bacterial microcompartments as a next-generation metabolic engineering tool: utilizing nature's solution for confining challenging catabolic pathways.Biochemical Society transactions · 2024Review
- Nanoengineering Carboxysome Shells for Protein Cages with Programmable Cargo Targeting.ACS nano · 2024Article
- Functionalization of bacterial microcompartment shell interior with cysteine containing peptides enhances the iron and cobalt loading capacity.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024Article
- Towards using bacterial microcompartments as a platform for spatial metabolic engineering in the industrially important and metabolically versatileFrontiers in bioengineering and biotechnology · 2024Article
- Heterologous Assembly of Pleomorphic Bacterial Microcompartment Shell Architectures Spanning the Nano- to Microscale.Advanced materials (Deerfield Beach, Fla.) · 2023Article
- Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology.Nature communications · 2022Article
- Chemical probing provides insight into the native assembly state of a bacterial microcompartment.Structure (London, England : 1993) · 2022Article
- Toward a glycyl radical enzyme containing synthetic bacterial microcompartment to produce pyruvate from formate and acetate.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Protein scaffolds: A tool for multi-enzyme assembly.Biotechnology reports (Amsterdam, Netherlands) · 2021Review
- Advances in the World of Bacterial Microcompartments.Trends in biochemical sciences · 2021Review
- Bacterial metabolosomes: new insights into their structure and bioengineering.Microbial biotechnology · 2021Article
- MCPdb: The bacterial microcompartment database.PloS one · 2021Article
- Engineered bacterial microcompartments: apps for programming metabolism.Current opinion in biotechnology · 2020Review
- Prokaryotic Organelles: Bacterial Microcompartments inEcoSal Plus · 2020Review
- Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles.Nature communications · 2020Article
- Article
- Bacterial microcompartments: catalysis-enhancing metabolic modules for next generation metabolic and biomedical engineering.BMC biology · 2019Review
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Bacterial microcompartments, BMCs, are proteinaceous organelles that encase a specific metabolic pathway within a semi-permeable protein shell. Short encapsulation peptides can direct cargo proteins to the lumen of the compartments. However, the fusion of such peptides to non-native proteins does not guarantee encapsulation and often causes aggregation. Here, we report an approach for targeting recombinant proteins to BMCs that utilizes specific de novo coiled-coil protein-protein interactions. Attachment of one coiled-coil module to PduA (a component of the BMC shell) allows targeting of a fluorescent protein fused to a cognate coiled-coil partner. This interaction takes place on the outer surface of the BMC. The redesign of PduA to generate an N-terminus on the luminal side of the BMC results in intact compartments to which proteins can still be targeted via the designed coiled-coil system. This study provides a strategy to display proteins on the surface or within the lumen of the BMCs.
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Registered trials
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