Self-Assembly Stability and Variability of Bacterial Microcompartment Shell Proteins in Response to the Environmental Change



Faulkner, Matthew, Zhao, Long-Sheng, Barrett, Steve ORCID: 0000-0003-2960-3334 and Liu, Lu-Ning ORCID: 0000-0002-8884-4819
(2019) Self-Assembly Stability and Variability of Bacterial Microcompartment Shell Proteins in Response to the Environmental Change. NANOSCALE RESEARCH LETTERS, 14 (1). 54-.

This is the latest version of this item.

Access the full-text of this item by clicking on the Open Access link.
[img] Text
2019_3 5815 dynamics_NRL.pdf - Published version

Download (3MB)

Abstract

Bacterial microcompartments (BMCs) are proteinaceous self-assembling organelles that are widespread among the prokaryotic kingdom. By segmenting key metabolic enzymes and pathways using a polyhedral shell, BMCs play essential roles in carbon assimilation, pathogenesis, and microbial ecology. The BMC shell is composed of multiple protein homologs that self-assemble to form the defined architecture. There is tremendous interest in engineering BMCs to develop new nanobioreactors and molecular scaffolds. Here, we report the quantitative characterization of the formation and self-assembly dynamics of BMC shell proteins under varying pH and salt conditions using high-speed atomic force microscopy (HS-AFM). We show that 400-mM salt concentration is prone to result in larger single-layered shell patches formed by shell hexamers, and a higher dynamic rate of hexamer self-assembly was observed at neutral pH. We also visualize the variability of shell proteins from hexameric assemblies to fiber-like arrays. This study advances our knowledge about the stability and variability of BMC protein self-assemblies in response to microenvironmental changes, which will inform rational design and construction of synthetic BMC structures with the capacity of remodeling their self-assembly and structural robustness. It also offers a powerful toolbox for quantitatively assessing the self-assembly and formation of BMC-based nanostructures in biotechnology applications.

Item Type: Article
Uncontrolled Keywords: Bacterial microcompartment, Protein dynamics, Self-assembly, High-speed atomic force microscopy, Synthetic engineering
Depositing User: Symplectic Admin
Date Deposited: 12 Feb 2019 12:45
Last Modified: 19 Jan 2023 01:03
DOI: 10.1186/s11671-019-2884-3
Open Access URL: https://doi.org/10.1186/s11671-019-2884-3
Related URLs:
URI: https://livrepository.liverpool.ac.uk/id/eprint/3032728

Available Versions of this Item