Visualization of Bacterial Microcompartment Facet Assembly Using High-Speed Atomic Force Microscopy

Journal Article · Mon Dec 07 00:00:00 EST 2015 · Nano Letters

DOI:https://doi.org/10.1021/acs.nanolett.5b04259· OSTI ID:1229691

Sutter, Markus ^[1]; Faulkner, Matthew; Aussignargues, Clément ^[2]; Paasch, Bradley C. ^[2]; Barrett, Steve; Kerfeld, Cheryl A. ^[3]; Liu, Lu-Ning

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1. MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824, United States, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States
2. MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824, United States
3. MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824, United States, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States, Department of Plant and Microbial Biology, University of California, Berkeley, Berkeley, California 94720, United States, Berkeley Synthetic Biology Institute, Berkeley, California 94720, United States, Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, United States

Bacterial microcompartments (BMCs) are proteinaceous organelles widespread among bacterial phyla. They compartmentalize enzymes within a selectively permeable shell and play important roles in CO₂ fixation, pathogenesis, and microbial ecology. Here, we combine X-ray crystallography and high-speed atomic force microscopy to characterize, at molecular resolution, the structure and dynamics of BMC shell facet assembly. Our results show that preformed hexamers assemble into uniformly oriented shell layers, a single hexamer thick. We also observe the dynamic process of shell facet assembly. Shell hexamers can dissociate from and incorporate into assembled sheets, indicating a flexible intermolecular interaction. Furthermore, we demonstrate that the self-assembly and dynamics of shell proteins are governed by specific contacts at the interfaces of shell proteins. Our study provides novel insights into the formation, interactions, and dynamics of BMC shell facets, which are essential for the design and engineering of self-assembled biological nanoreactors and scaffolds based on BMC architectures.

• Research Organization: Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
• Sponsoring Organization: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Inst. of Health (NIH) (United States); Royal Society (United Kingdom); Biotechnology and Biological Sciences Research Council (BBSRC) (United Kingdom)
• Grant/Contract Number: AC02-05CH11231; 1R01AI114975-01; UF120411; RG130442; BB/M024202/1; BB/M012441/1
• OSTI ID: 1229691
• Alternate ID(s): OSTI ID: 1414741
• Journal Information: Nano Letters, Journal Name: Nano Letters Vol. 16 Journal Issue: 3; ISSN 1530-6984
• Publisher: American Chemical Society
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
bacterial microcompartment
high-speed atomic force microscopy
protein dynamics
protein interaction
self-assembly