Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles

KALNINS, G., E.E. CESLE, J. JANSONS, J. LIEPINS, Anatolij FILIMONĚNKO and K. TARS. Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles. Nature Communications. London: Nature Publishing Group, 2020, vol. 11, No 1, p. 388-400. ISSN 2041-1723. Available from: https://dx.doi.org/10.1038/s41467-019-14205-y.

Basic information

• Original name: Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles
• Authors: KALNINS, G., E.E. CESLE, J. JANSONS, J. LIEPINS, Anatolij FILIMONĚNKO (203 Czech Republic, guarantor, belonging to the institution) and K. TARS.
• Edition: Nature Communications, London, Nature Publishing Group, 2020, 2041-1723.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10608 Biochemistry and molecular biology
• Country of publisher: United Kingdom of Great Britain and Northern Ireland
• Confidentiality degree: is not subject to a state or trade secret
• WWW: URL
• Impact factor: Impact factor: 14.919
• RIV identification code: RIV/00216224:14740/20:00118308
• Organization unit: Central European Institute of Technology
• Doi: http://dx.doi.org/10.1038/s41467-019-14205-y
• UT WoS: 000512537400009
• Keywords in English: SHELL PROTEINS; CARBOXYSOME; ORGANELLES; 1 2-PROPANEDIOL; METABOLITE; INSIGHTS; VISUALIZATION; DEGRADATION; SEQUENCES; SOFTWARE
• Tags: CF CRYO, rivok

Abstract

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.

Links

• LM2015043, research and development project: Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)

Investor: Ministry of Education, Youth and Sports of the CR