Heterologous Assembly of Pleomorphic Bacterial Microcompartment Shell Architectures Spanning the Nano‐ to Microscale
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- MSU‐DOE Plant Research Laboratory Michigan State University East Lansing MI 48824 USA, Department of Biochemistry and Molecular Biology Michigan State University East Lansing MI 48824 USA
- MSU‐DOE Plant Research Laboratory Michigan State University East Lansing MI 48824 USA, Environmental Genomics and Systems Biology and Molecular Biophysics and Integrative Bioimaging Divisions Lawrence Berkeley National Laboratory Berkeley CA 94720 USA
- California Institute for Quantitative Biosciences (QB3) University of California, Berkeley Berkeley CA 94720 USA, Molecular Biophysics and Integrative Bioimaging Division Lawrence Berkeley National Laboratory Berkeley CA 94720 USA
- California Institute for Quantitative Biosciences (QB3) University of California, Berkeley Berkeley CA 94720 USA, Molecular Biophysics and Integrative Bioimaging Division Lawrence Berkeley National Laboratory Berkeley CA 94720 USA, Howard Hughes Medical Institute University of California, Berkeley Berkeley CA 94720 USA, Department of Molecular and Cell Biology University of California, Berkeley Berkeley CA 94720 USA
- MSU‐DOE Plant Research Laboratory Michigan State University East Lansing MI 48824 USA, Department of Biochemistry and Molecular Biology Michigan State University East Lansing MI 48824 USA, Environmental Genomics and Systems Biology and Molecular Biophysics and Integrative Bioimaging Divisions Lawrence Berkeley National Laboratory Berkeley CA 94720 USA
Abstract Many bacteria use protein‐based organelles known as bacterial microcompartments (BMCs) to organize and sequester sequential enzymatic reactions. Regardless of their specialized metabolic function, all BMCs are delimited by a shell made of multiple structurally redundant, yet functionally diverse, hexameric (BMC‐H), pseudohexameric/trimeric (BMC‐T), or pentameric (BMC‐P) shell protein paralogs. When expressed without their native cargo, shell proteins have been shown to self‐assemble into 2D sheets, open‐ended nanotubes, and closed shells of ≈40 nm diameter that are being developed as scaffolds and nanocontainers for applications in biotechnology. Here, by leveraging a strategy for affinity‐based purification, it is demonstrated that a wide range of empty synthetic shells, many differing in end‐cap structures, can be derived from a glycyl radical enzyme‐associated microcompartment. The range of pleomorphic shells observed, which span ≈2 orders of magnitude in size from ≈25 nm to ≈1.8 µm, reveal the remarkable plasticity of BMC‐based biomaterials. In addition, new capped nanotube and nanocone morphologies are observed that are consistent with a multicomponent geometric model in which architectural principles are shared among asymmetric carbon, viral protein, and BMC‐based structures.
- Sponsoring Organization:
- USDOE
- Grant/Contract Number:
- NONE; SC0023395
- OSTI ID:
- 1971387
- Alternate ID(s):
- OSTI ID: 1971389; OSTI ID: 2234102
- Journal Information:
- Advanced Materials, Journal Name: Advanced Materials Journal Issue: 23 Vol. 35; ISSN 0935-9648
- Publisher:
- Wiley Blackwell (John Wiley & Sons)Copyright Statement
- Country of Publication:
- Germany
- Language:
- English
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