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

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.
 [1] ;  [1] ;  [1] ;  [2] ;  [3]
  1. Michigan State Univ., East Lansing, MI (United States)
  2. Univ. of California, Berkeley, CA (United States)
  3. 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:
Grant/Contract Number:
Accepted Manuscript
Journal Name:
Communicative & Integrative Biology
Additional Journal Information:
Journal Volume: 8; Journal Issue: 3; Journal ID: ISSN 1942-0889
Research Org:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
bacterial microcompartments; BMC assembly; carboxysomes; encapsulation peptides; metabolosomes; protein-protein interaction; synthetic biology
OSTI Identifier: