期刊
ACS CENTRAL SCIENCE
卷 7, 期 4, 页码 658-670出版社
AMER CHEMICAL SOC
DOI: 10.1021/acscentsci.0c01699
关键词
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资金
- Department of Energy [DE-FG02-08ER46539]
- Army Research Office [W911NF-19-10298]
- National Science Foundation [DGE1842165]
- National Institutes of Health through Northwestern University's Biotechnology Training Program [T32GM008449]
- U.S. Department of Energy (DOE) [DE-FG02-08ER46539] Funding Source: U.S. Department of Energy (DOE)
Bacterial microcompartments compartmentalize enzymes for chemical and energy production, aiding bacterial survival in hostile environments. Mutations can alter protein preferred angles and interaction strengths, modifying assembled morphologies. These findings offer insight into controlled protein assembly and principles for designing microcompartments for various applications.
Bacterial microcompartments compartmentalize the enzymes that aid chemical and energy production in many bacterial species. They are postulated to help bacteria survive in hostile environments. Metabolic engineers are interested in repurposing these organelles for non-native functions. Here, we use computational, theoretical, and experimental approaches to determine mechanisms that effectively control microcompartment self-assembly. We find, via multiscale modeling and mutagenesis studies, the interactions responsible for the binding of hexamer-forming proteins in a model system, the propanediol utilization bacterial microcompartments from Salmonella enterica serovar Typhimurium LT2. We determine how the changes in the microcompartment hexamer protein preferred angles and interaction strengths can modify the assembled morphologies. We demonstrate that such altered strengths and angles are achieved via amino acid mutations. A thermodynamic model provides guidelines to design microcompartments of various morphologies. These findings yield insight in controlled protein assembly and provide principles for assembling microcompartments for biochemical or energy applications as nanoreactors.
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