Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00118308" target="_blank" >RIV/00216224:14740/20:00118308 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.nature.com/articles/s41467-019-14205-y.pdf" target="_blank" >https://www.nature.com/articles/s41467-019-14205-y.pdf</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41467-019-14205-y" target="_blank" >10.1038/s41467-019-14205-y</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LM2015043" target="_blank" >LM2015043: Česká infrastruktura pro integrativní strukturní biologii</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Nature Communications

ISSN

2041-1723

e-ISSN

—

Svazek periodika

11

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

13

Strana od-do

388

Kód UT WoS článku

000512537400009

EID výsledku v databázi Scopus

2-s2.0-85078311746