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Quantification of Cytosolic vs. Vacuolar Salmonella in Primary Macrophages by Differential Permeabilization
Published on: July 28, 2015
Prokaryotic Organelles: Bacterial Microcompartments in E. coli and Salmonella
Katie L Stewart1, Andrew M Stewart1, Thomas A Bobik1
1The Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA 50011.
Abstract:
Bacterial microcompartments (MCPs) are proteinaceous organelles consisting of a metabolic pathway encapsulated within a selectively permeable protein shell. Hundreds of species of bacteria produce MCPs of at least nine different types, and MCP metabolism is associated with enteric pathogenesis, cancer, and heart disease. This review focuses chiefly on the four types of catabolic MCPs (metabolosomes) found in Escherichia coli and Salmonella: the propanediol utilization (pdu), ethanolamine utilization (eut), choline utilization (cut), and glycyl radical propanediol (grp) MCPs. Although the great majority of work done on catabolic MCPs has been carried out with Salmonella and E. coli, research outside the group is mentioned where necessary for a comprehensive understanding. Salient characteristics found across MCPs are discussed, including enzymatic reactions and shell composition, with particular attention paid to key differences between classes of MCPs. We also highlight relevant research on the dynamic processes of MCP assembly, protein targeting, and the mechanisms that underlie selective permeability. Lastly, we discuss emerging biotechnology applications based on MCP principles and point out challenges, unanswered questions, and future directions.
Insights
Bacterial microcompartments (MCPs) are protein shells enclosing metabolic pathways. This review details four types of catabolic MCPs in E. coli and Salmonella, exploring their structure, function, and biotechnological potential.
Area of Science:
- Microbiology
- Biochemistry
- Structural Biology
Background:
- Bacterial microcompartments (MCPs) are protein-bound organelles found in hundreds of bacterial species.
- MCPs encapsulate metabolic pathways, influencing processes linked to pathogenesis and disease.
- At least nine distinct types of MCPs exist, with four catabolic types (metabolosomes) studied in E. coli and Salmonella.
Purpose of the Study:
- To review the structure, function, and assembly of catabolic MCPs in E. coli and Salmonella.
- To highlight key differences and shared characteristics among propanediol utilization (pdu), ethanolamine utilization (eut), choline utilization (cut), and glycyl radical propanediol (grp) MCPs.
- To discuss emerging applications and future research directions for MCPs.
Main Methods:
- Review of existing literature on bacterial microcompartments.
- Analysis of enzymatic reactions and protein shell composition.
- Discussion of MCP assembly, protein targeting, and selective permeability mechanisms.
Main Results:
- Detailed examination of four catabolic MCPs: pdu, eut, cut, and grp.
- Comparison of enzymatic activities and shell structures across different MCP classes.
- Overview of dynamic processes including assembly and protein localization.
Conclusions:
- MCPs represent a diverse class of bacterial organelles with significant roles in metabolism.
- Understanding MCPs offers insights into pathogenesis and potential biotechnological applications.
- Further research is needed to fully elucidate MCP assembly, permeability, and diverse functions.
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