Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles

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Publikace nespadá pod Lékařskou fakultu, ale pod Středoevropský technologický institut. Oficiální stránka publikace je na webu muni.cz.

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KALNINS G. CESLE E.E. JANSONS J. LIEPINS J. FILIMONĚNKO Anatolij TARS K.

Rok publikování 2020
Druh Článek v odborném periodiku
Časopis / Zdroj Nature Communications
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www https://www.nature.com/articles/s41467-019-14205-y.pdf
Doi http://dx.doi.org/10.1038/s41467-019-14205-y
Klíčová slova SHELL PROTEINS; CARBOXYSOME; ORGANELLES; 1 2-PROPANEDIOL; METABOLITE; INSIGHTS; VISUALIZATION; DEGRADATION; SEQUENCES; SOFTWARE
Popis 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 angstrom resolution, and demonstrate variability among the minor shell forms.
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