ArticleNature communications2025
A blueprint for biomolecular condensation driven by bacterial microcompartment encapsulation peptides.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed.
- Unlocking the bacterial condensome: from "dark matter" to design.Molecular biology of the cell · 2026Article
- Peptide-Ligand Cooperative Interplay Drives Gold Nanoparticle Encapsulation by Protein Cages.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Employing Nanotechnology to Enhance Ethanol Production in Two Synechococcus elongatus Strains.Chembiochem : a European journal of chemical biology · 2026Article
- Many paths, similar destinations: viruses and bacterial microcompartments form polyhedra inside cells.Journal of virology · 2026Review
- A molecular basis for stoichiometric enzyme encapsulation in the vitamin B2 biosynthesis compartment.Nature communications · 2026Article
- Review
- Molecular Modeling and Molecular Dynamics Simulation of a Packed and Intact Bacterial Microcompartment.The journal of physical chemistry. B · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Bacterial microcompartments are protein organelles with diverse metabolic capabilities. Their functional diversity is determined by an enzymatic core that is sequestered within a structurally conserved protein shell architecture. Segregation of protein cargo into the bacterial microcompartment is enabled by encapsulation peptides, which are short helical domains fused to core proteins through a disordered linker. Here, we investigate how encapsulation peptides drive multicomponent cargo assembly into biomolecular condensates. In vitro experiments supported by molecular dynamics simulations demonstrate the importance of both conserved hydrophobic packing and electrostatic interactions in stabilizing trimeric encapsulation peptide bundles. Topological rearrangements of encapsulation peptide domains can drive programmable liquid- or gel-like partitioning in vitro and in vivo. This partitioning is found to be encapsulation peptide-specific, modular, and can co-assemble at least three fluorescent reporters. In summary, we describe the molecular features necessary to drive biomolecular condensation using a widespread peptide tag. This work can serve as a blueprint for implementing encapsulation peptide biotechnology across diverse applications.
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Registered trials
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