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Title: Bacterial microcompartments

Abstract

Bacterial microcompartments (BMCs) are self-assembling organelles that consist of an enzymatic core that is encapsulated by a selectively permeable protein shell. The potential to form BMCs is widespread, found across the Kingdom Bacteria. BMCs have crucial roles in carbon dioxide fixation in autotrophs and the catabolism of organic substrates in heterotrophs. They contribute to the metabolic versatility of bacteria, providing a competitive advantage in specific environmental niches. Although BMCs were first visualized more than sixty years ago, it is mainly in the last decade that progress has been made in understanding their metabolic diversity and the structural basis of their assembly and function. This progress has not only heightened our understanding of their role in microbial metabolism but it is also beginning to enable their use in a variety of applications in synthetic biology. In this Review, we focus on recent insights into the structure, assembly, diversity and function of BMCs.

Authors:
 [1];  [2];  [3];  [4];  [1]
  1. Michigan State Univ., East Lansing, MI (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
  2. Michigan State Univ., East Lansing, MI (United States)
  3. Max Planck Institute for Terrestrial Microbiology, Marburg (Germany)
  4. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Publication Date:
Research Org.:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States); Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI Identifier:
1485085
Alternate Identifier(s):
OSTI ID: 1687379
Grant/Contract Number:  
AC02-05CH11231; FG02-91ER20021
Resource Type:
Accepted Manuscript
Journal Name:
Nature Reviews Microbiology
Additional Journal Information:
Journal Volume: 16; Journal Issue: 5; Journal ID: ISSN 1740-1526
Publisher:
Springer Nature
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Kerfeld, Cheryl A., Aussignargues, Clement, Zarzycki, Jan, Cai, Fei, and Sutter, Markus. Bacterial microcompartments. United States: N. p., 2018. Web. doi:10.1038/nrmicro.2018.10.
Kerfeld, Cheryl A., Aussignargues, Clement, Zarzycki, Jan, Cai, Fei, & Sutter, Markus. Bacterial microcompartments. United States. https://doi.org/10.1038/nrmicro.2018.10
Kerfeld, Cheryl A., Aussignargues, Clement, Zarzycki, Jan, Cai, Fei, and Sutter, Markus. Mon . "Bacterial microcompartments". United States. https://doi.org/10.1038/nrmicro.2018.10. https://www.osti.gov/servlets/purl/1485085.
@article{osti_1485085,
title = {Bacterial microcompartments},
author = {Kerfeld, Cheryl A. and Aussignargues, Clement and Zarzycki, Jan and Cai, Fei and Sutter, Markus},
abstractNote = {Bacterial microcompartments (BMCs) are self-assembling organelles that consist of an enzymatic core that is encapsulated by a selectively permeable protein shell. The potential to form BMCs is widespread, found across the Kingdom Bacteria. BMCs have crucial roles in carbon dioxide fixation in autotrophs and the catabolism of organic substrates in heterotrophs. They contribute to the metabolic versatility of bacteria, providing a competitive advantage in specific environmental niches. Although BMCs were first visualized more than sixty years ago, it is mainly in the last decade that progress has been made in understanding their metabolic diversity and the structural basis of their assembly and function. This progress has not only heightened our understanding of their role in microbial metabolism but it is also beginning to enable their use in a variety of applications in synthetic biology. In this Review, we focus on recent insights into the structure, assembly, diversity and function of BMCs.},
doi = {10.1038/nrmicro.2018.10},
journal = {Nature Reviews Microbiology},
number = 5,
volume = 16,
place = {United States},
year = {Mon Mar 05 00:00:00 EST 2018},
month = {Mon Mar 05 00:00:00 EST 2018}
}

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Figures / Tables:

Figure 1 Figure 1: Core biochemistry of carboxysomes and metabolosomes and superloci organization A) Schematic of the bacterial microcompartment (BMC) shell and encapsulated enzymes and associated flow of substrates/products. α-carboxysomes and β-carboxysomes both encapsulate carbonic anhydrase (CA) and Form 1 RuBisCO to fix CO2 as part of the Calvin-Benson-Bassham Cycle (CBB). Themore » shell prevents loss of CO2 to the cytoplasm. B) Metabolosomes have more diverse initial substrates compared to carboxysomes, but they typically share a common core biochemistry that is based on a signature enzyme, an aldehyde dehydrogenase (AldDH), an alcohol dehydrogenase (AlcDH) and a phosphotransacylase (PTAC). The signature enzyme generates the aldehyde which is then converted to a product alcohol by the AlcDH. This reaction uses CoA and NAD+ which are recycled in a separate reaction branch that uses AldDH and PTAC to produce a phosphorylated product (R-P). This product is then dephosphorylated by an acetyl kinase (AK) in a reaction that generates ATP. C) Schematic of a typical gene composition in a superlocus encoding a BMC. In addition to genes encoding shell and core proteins, BMC superloci encode proteins for supporting and ancillary functions, like transporters for the signature substrate. 3-PGA, 3-phosphoglycerate; RuBP, ribulose 1,5-bisphosphate;.« less

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Figures/Tables have been extracted from DOE-funded journal article accepted manuscripts.