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@article{1748082,
author = {Kalnins, G. and Cesle, E.E. and Jansons, J. and Liepins, J. and Filimoněnko, Anatolij and Tars, K.},
article_location = {London},
article_number = {1},
doi = {http://dx.doi.org/10.1038/s41467-019-14205-y},
keywords = {SHELL PROTEINS; CARBOXYSOME; ORGANELLES; 1 2-PROPANEDIOL; METABOLITE; INSIGHTS; VISUALIZATION; DEGRADATION; SEQUENCES; SOFTWARE},
language = {eng},
issn = {2041-1723},
journal = {Nature Communications},
title = {Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles},
url = {https://www.nature.com/articles/s41467-019-14205-y.pdf},
volume = {11},
year = {2020}
}
TY - JOUR
ID - 1748082
AU - Kalnins, G. - Cesle, E.E. - Jansons, J. - Liepins, J. - Filimoněnko, Anatolij - Tars, K.
PY - 2020
TI - Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles
JF - Nature Communications
VL - 11
IS - 1
SP - 388
EP - 388
PB - Nature Publishing Group
SN - 20411723
KW - SHELL PROTEINS
KW - CARBOXYSOME
KW - ORGANELLES
KW - 1 2-PROPANEDIOL
KW - METABOLITE
KW - INSIGHTS
KW - VISUALIZATION
KW - DEGRADATION
KW - SEQUENCES
KW - SOFTWARE
UR - https://www.nature.com/articles/s41467-019-14205-y.pdf
N2 - 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.
ER -
KALNINS, G., E.E. CESLE, J. JANSONS, J. LIEPINS, Anatolij FILIMONĚNKO a K. TARS. Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles. \textit{Nature Communications}. London: Nature Publishing Group, 2020, roč.~11, č.~1, s.~388-400. ISSN~2041-1723. Dostupné z: https://dx.doi.org/10.1038/s41467-019-14205-y.
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