Bacterial microcompartment assembly: The key role of encapsulation peptides
Abstract
Bacterial microcompartments (BMCs) are proteinaceous organelles used by a broad range of bacteria to segregate and optimize metabolic reactions. Their functions are diverse, and can be divided into anabolic (carboxysome) and catabolic (metabolosomes) processes, depending on their cargo enzymes. The assembly pathway for the β-carboxysome has been characterized, revealing that biogenesis proceeds from the inside out. The enzymes coalesce into a procarboxysome, followed by encapsulation in a protein shell that is recruited to the procarboxysome by a short (~17 amino acids) extension on the C-terminus of one of the encapsulated proteins. A similar extension is also found on the N- or C-termini of a subset of metabolosome core enzymes. These encapsulation peptides (EPs) are characterized by a primary structure predicted to form an amphipathic α-helix that interacts with shell proteins. In this study, we review the features, function and widespread occurrence of EPs among metabolosomes, and propose an expanded role for EPs in the assembly of diverse BMCs.
- Authors:
-
- Michigan State Univ., East Lansing, MI (United States)
- Univ. of California, Berkeley, CA (United States)
- Michigan State Univ., East Lansing, MI (United States); Univ. of California, Berkeley, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Berkeley Synthetic Biology Inst., Berkeley, CA (United States)
- Publication Date:
- Research Org.:
- Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory; Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division
- OSTI Identifier:
- 1714351
- Alternate Identifier(s):
- OSTI ID: 1220568
- Grant/Contract Number:
- FG02-91ER20021
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Communicative & Integrative Biology
- Additional Journal Information:
- Journal Volume: 8; Journal Issue: 3; Journal ID: ISSN 1942-0889
- Publisher:
- Taylor & Francis
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; bacterial microcompartments; BMC assembly; carboxysomes; encapsulation peptides; metabolosomes; protein-protein interaction; synthetic biology
Citation Formats
Aussignargues, Clément, Paasch, Bradley C., Gonzalez-Esquer, Raul, Erbilgin, Onur, and Kerfeld, Cheryl A. Bacterial microcompartment assembly: The key role of encapsulation peptides. United States: N. p., 2015.
Web. doi:10.1080/19420889.2015.1039755.
Aussignargues, Clément, Paasch, Bradley C., Gonzalez-Esquer, Raul, Erbilgin, Onur, & Kerfeld, Cheryl A. Bacterial microcompartment assembly: The key role of encapsulation peptides. United States. https://doi.org/10.1080/19420889.2015.1039755
Aussignargues, Clément, Paasch, Bradley C., Gonzalez-Esquer, Raul, Erbilgin, Onur, and Kerfeld, Cheryl A. Tue .
"Bacterial microcompartment assembly: The key role of encapsulation peptides". United States. https://doi.org/10.1080/19420889.2015.1039755. https://www.osti.gov/servlets/purl/1714351.
@article{osti_1714351,
title = {Bacterial microcompartment assembly: The key role of encapsulation peptides},
author = {Aussignargues, Clément and Paasch, Bradley C. and Gonzalez-Esquer, Raul and Erbilgin, Onur and Kerfeld, Cheryl A.},
abstractNote = {Bacterial microcompartments (BMCs) are proteinaceous organelles used by a broad range of bacteria to segregate and optimize metabolic reactions. Their functions are diverse, and can be divided into anabolic (carboxysome) and catabolic (metabolosomes) processes, depending on their cargo enzymes. The assembly pathway for the β-carboxysome has been characterized, revealing that biogenesis proceeds from the inside out. The enzymes coalesce into a procarboxysome, followed by encapsulation in a protein shell that is recruited to the procarboxysome by a short (~17 amino acids) extension on the C-terminus of one of the encapsulated proteins. A similar extension is also found on the N- or C-termini of a subset of metabolosome core enzymes. These encapsulation peptides (EPs) are characterized by a primary structure predicted to form an amphipathic α-helix that interacts with shell proteins. In this study, we review the features, function and widespread occurrence of EPs among metabolosomes, and propose an expanded role for EPs in the assembly of diverse BMCs.},
doi = {10.1080/19420889.2015.1039755},
journal = {Communicative & Integrative Biology},
number = 3,
volume = 8,
place = {United States},
year = {Tue Jun 23 00:00:00 EDT 2015},
month = {Tue Jun 23 00:00:00 EDT 2015}
}
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