Bacterial microcompartment assembly: The key role of encapsulation peptides

Aussignargues, Clément; Paasch, Bradley C.; Gonzalez-Esquer, Raul; Erbilgin, Onur; Kerfeld, Cheryl A.

doi:10.1080/19420889.2015.1039755

Title: Bacterial microcompartment assembly: The key role of encapsulation peptides

Journal Article · Tue Jun 23 00:00:00 EDT 2015 · Communicative & Integrative Biology

DOI:https://doi.org/10.1080/19420889.2015.1039755· OSTI ID:1714351

Aussignargues, Clément ^[1]; Paasch, Bradley C. ^[1]; Gonzalez-Esquer, Raul ^[1]; Erbilgin, Onur ^[2]; Kerfeld, Cheryl A. ^[3]

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)

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.

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Research Organization:: Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory; Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division

Grant/Contract Number:: FG02-91ER20021

OSTI ID:: 1714351

Alternate ID(s):: OSTI ID: 1220568

Journal Information:: Communicative & Integrative Biology, Vol. 8, Issue 3; ISSN 1942-0889

Publisher:: Taylor & FrancisCopyright Statement

Country of Publication:: United States

Language:: English

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59 BASIC BIOLOGICAL SCIENCES
bacterial microcompartments
BMC assembly
carboxysomes
encapsulation peptides
metabolosomes
protein-protein interaction
synthetic biology

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