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Biotechnological Advances in Bacterial Microcompartment Technology

2018; Elsevier BV; Volume: 37; Issue: 3 Linguagem: Inglês

10.1016/j.tibtech.2018.08.006

0167-9430

Matthew J. Lee, David J. Palmer, Martin J. Warren,

Microbial Fuel Cells and Bioremediation

Bacterial microcompartments (BMCs) are widespread proteinaceous organelles consisting of a semipermeable protein shell and an encapsulated enzymatic pathway. BMCs can be divided into the anabolic carboxysomes and the catabolic metabolosomes. Targeting to organelles is facilitated by short, amphipathic, alpha helical encapsulation peptides. Heterologous enzymatic pathways can be encapsulated within empty organelles, resulting in enhanced productivity. A BMC-H-based cytoscaffold is able to significantly enhance biofuel production through enzyme colocation. Bacterial microcompartments (BMCs) represent proteinaceous macromolecular nanobioreactors that are found in a broad range of bacteria, and which are associated with either anabolic or catabolic processes. They consist of a semipermeable outer shell that packages a central metabolic enzyme or pathway, providing both enhanced flux and protection against toxic intermediates. Recombinant production of BMCs has led to their repurposing with the incorporation of altogether new pathways. Deconstructing BMCs into their component parts has shown that some individual shell proteins self-associate into filaments that can be further modified into a cytoplasmic scaffold, or cytoscaffold, to which enzymes/proteins can be targeted. BMCs therefore represent a modular system that is highly suited for engineering biological systems for useful purposes. Bacterial microcompartments (BMCs) represent proteinaceous macromolecular nanobioreactors that are found in a broad range of bacteria, and which are associated with either anabolic or catabolic processes. They consist of a semipermeable outer shell that packages a central metabolic enzyme or pathway, providing both enhanced flux and protection against toxic intermediates. Recombinant production of BMCs has led to their repurposing with the incorporation of altogether new pathways. Deconstructing BMCs into their component parts has shown that some individual shell proteins self-associate into filaments that can be further modified into a cytoplasmic scaffold, or cytoscaffold, to which enzymes/proteins can be targeted. BMCs therefore represent a modular system that is highly suited for engineering biological systems for useful purposes. proteinaceous organelles ∼100 nm in diameter found in ∼20% of bacterial species that encase either anabolic or catabolic processes. a component of the BMC shell containing a single Pfam 00936 domain; six BMC-H proteins come together to form a homohexameric tile that forms part of the BMC shell. a component of the BMC shell containing a single Pfam 03319 domain; five BMC-P proteins come together to form a homopentameric tile that forms the vertices of the BMC. a component of the BMC shell containing two fused Pfam 00936 domains; three BMC-T proteins come together to form a homotrimeric tile that forms part of the BMC shell. bacterial organelles containing the enzymes carbonic anhydrase to generate a high local concentration of CO2 and ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) to catalyse the carboxylation of ribulose 1,5-bisphosphate, the first step in carbon fixation. short (∼18 amino acid) peptides that form amphipathic alpha helices natively found on the N or C terminus of encapsulated proteins that target such proteins to the lumen of BMCs. catabolic BMCs that encase a metabolic pathway in which a signature enzyme converts a metabolite into an aldehyde that is subsequently converted into an acid and alcohol. a metabolosome enzyme that is specific to the first substrate to product conversion.