Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles

Bacterial microcompartments (BMCs) are prokaryotic organelles consisting of a protein shell and an encapsulated enzymatic core. BMCs are involved in several biochemical processes, such as choline, glycerol and ethanolamine degradation and carbon fixation. Since non-native enzymes can also be encapsu...

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Vydáno v:	Nature communications Ročník 11; číslo 1; s. 388 - 13
Hlavní autoři:	Kalnins, Gints, Cesle, Eva-Emilija, Jansons, Juris, Liepins, Janis, Filimonenko, Anatolij, Tars, Kaspars
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	London Nature Publishing Group UK 20.01.2020 Nature Publishing Group Nature Portfolio
Témata:	101/28 45/77 631/326/41/2536 631/326/88 631/535/1258/1259 82/16 82/83 Bacteria Bacterial Proteins - genetics Bacterial Proteins - metabolism Biodegradation Carbon fixation Choline Choline - metabolism Cryoelectron Microscopy Encapsulation Enzymes Ethanolamine Gene expression Genetic Loci Glycerol Humanities and Social Sciences Icosahedral phase Klebsiella Klebsiella pneumoniae Klebsiella pneumoniae - cytology Klebsiella pneumoniae - enzymology Klebsiella pneumoniae - genetics Klebsiella pneumoniae - ultrastructure Lyases - genetics Lyases - metabolism multidisciplinary Organelles Organelles - enzymology Organelles - ultrastructure Proteins Recombinant Proteins - genetics Recombinant Proteins - metabolism Science Science (multidisciplinary) Synthetic Biology
ISSN:	2041-1723, 2041-1723
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Shrnutí:	Bacterial microcompartments (BMCs) are prokaryotic organelles consisting of a protein shell and an encapsulated enzymatic core. BMCs are involved in several biochemical processes, such as choline, glycerol and ethanolamine degradation and carbon fixation. Since non-native enzymes can also be encapsulated in BMCs, an improved understanding of BMC shell assembly and encapsulation processes could be useful for synthetic biology applications. Here we report the isolation and recombinant expression of BMC structural genes from the Klebsiella pneumoniae GRM2 locus, the investigation of mechanisms behind encapsulation of the core enzymes, and the characterization of shell particles by cryo-EM. We conclude that the enzymatic core is encapsulated in a hierarchical manner and that the CutC choline lyase may play a secondary role as an adaptor protein. We also present a cryo-EM structure of a pT = 4 quasi-symmetric icosahedral shell particle at 3.3 Å resolution, and demonstrate variability among the minor shell forms. Bacterial microcompartments (BMCs) consist of a protein shell and an encapsulated enzymatic core. Here, Kalnins et al. study a BMC from Klebsiella pneumoniae , show that the enzymatic core is encapsulated in a hierarchical manner, and solve the cryo-EM structure of a pT = 4 quasi-symmetric icosahedral shell particle.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ISSN:	2041-1723 2041-1723
DOI:	10.1038/s41467-019-14205-y