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Commun Integr Biol. 2015 Jun 23;8(3):e1039755. doi: 10.1080/19420889.2015.1039755. eCollection 2015 May-Jun.

Bacterial microcompartment assembly: The key role of encapsulation peptides.

Author information

1
DOE Plant Research Laboratory; Michigan State University ; East Lansing, MI USA.
2
Department of Plant and Microbial Biology; University of California, Berkeley ; Berkeley, CA USA.
3
DOE Plant Research Laboratory; Michigan State University ; East Lansing, MI USA ; Department of Plant and Microbial Biology; University of California, Berkeley ; Berkeley, CA USA ; Physical Biosciences Division; Lawrence Berkeley National Laboratory ; Berkeley, CA USA ; Berkeley Synthetic Biology Institute ; Berkeley, CA USA.

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. Here, 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.

KEYWORDS:

BMC assembly; bacterial microcompartments; carboxysomes; encapsulation peptides; metabolosomes; protein-protein interaction; synthetic biology

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