Journal
BIOMACROMOLECULES
Volume 17, Issue 8, Pages 2522-2529Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biomac.6b00469
Keywords
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Funding
- Project Proteins At Work, a program of The Netherlands Proteomics Centre - The Netherlands Organization for Scientific Research (NWO) as part of the National Roadmap Large-Scale Research Facilities of The Netherlands [184.032.201]
- VIDI Grant from the NWO
- Project-ruimte Grant from Fundamenteel Onderzoek der Materie (FOM)
- NanoNextNL
- National Science Foundation [DMR-1505662]
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Prokaryotes mostly lack membranous compartments that are typical of eukaryotic cells, but instead, they have various protein-based organelles. These include bacterial microcompartments like the carboxysome and the virus-like nanocompartment encapsulin. Encapsulins have an adaptable mechanism for enzyme packaging, which makes it an attractive platform to carry a foreign protein cargo. Here we investigate the assembly pathways and mechanical properties of the cargo-free and cargo-loaded nanocompartments, using a combination of native mass spectrometry, atomic force microscopy and multiscale computational molecular modeling. We show that encapsulin dimers assemble into rigid single-enzyme bacterial containers. Moreover, we demonstrate that cargo encapsulation has a mechanical impact on the shell. The structural similarity of encapsulins to virus capsids is reflected in their mechanical properties. With these robust mechanical properties encapsulins provide a suitable platform for the development of nanotechnological applications.
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