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



Sutter, Markus, Faulkner, Matthew ORCID: 0000-0002-0578-388X, Aussignargues, Clément, Paasch, Bradley C, Barrett, Steve ORCID: 0000-0003-2960-3334, Kerfeld, Cheryl A and Liu, Luning ORCID: 0000-0002-8884-4819
(2016) Visualization of Bacterial Microcompartment Facet Assembly Using High-Speed Atomic Force Microscopy. Nano Letters, 16 (03). 1590 - 1595.

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Abstract

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.

Item Type: Article
Uncontrolled Keywords: Bacterial microcompartment, high-speed atomic force microscopy, protein dynamics, rotein interaction, self-assembly
Subjects: ?? QH301 ??
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Depositing User: Symplectic Admin
Date Deposited: 07 Apr 2016 15:24
Last Modified: 10 May 2021 20:10
DOI: 10.1021/acs.nanolett.5b04259
Related URLs:
URI: https://livrepository.liverpool.ac.uk/id/eprint/3000057

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