Structural insights into the main S-layer unit of Deinococcus radiodurans reveal a massive protein complex with porin-like features

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F20%3A10411546" target="_blank" >RIV/00216208:11110/20:10411546 - isvavai.cz</a>

Result on the web

<a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=svs~xSoUPl" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=svs~xSoUPl</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/jbc.RA119.012174" target="_blank" >10.1074/jbc.RA119.012174</a>

Result language

angličtina

Original language name

Structural insights into the main S-layer unit of Deinococcus radiodurans reveal a massive protein complex with porin-like features

Original language description

In the extremophile bacterium Deinococcus radiodurans, the outermost surface layer is tightly connected with the rest of the cell wall. This integrated organization provides a compact structure that shields the bacterium against environmental stresses. The fundamental unit of this surface layer (S-layer) is the S-layer deinoxanthin-binding complex (SDBC), which binds the carotenoid deinoxanthin and provides both, thermostability and UV radiation resistance. However, the structural organization of the SDBC awaits elucidation. Here, we report the isolation of the SDBC with a gentle procedure consisting of lysozyme treatment and solubilization with the nonionic detergent n-dodecyl-?-d-maltoside, which preserved both hydrophilic and hydrophobic components of the SDBC and allows the retention of several minor subunits. As observed by low-resolution single-particle analysis, we show that the complex possesses a porin-like structural organization, but is larger than other known porins. We also noted that the main SDBC component, the protein DR_2577, shares regions of similarity with known porins. Moreover, results from electrophysiological assays with membrane-reconstituted SDBC disclosed that it is a nonselective channel that has some peculiar gating properties, but also exhibits behavior typically observed in pore-forming proteins, such as porins and ionic transporters. The functional properties of this system and its porin-like organization provide information critical for understanding ion permeability through the outer cell surface of S-layer?carrying bacterial species.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10601 - Cell biology

Project

<a href="/en/project/GJ18-25144Y" target="_blank" >GJ18-25144Y: Structural exploration of the ATP-dependent human mitochondrial Lon protease for drug design and further understanding of its mechanism of action</a><br>

Continuities

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

Publication year

2020

Confidentiality

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

Name of the periodical

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

—

Volume of the periodical

295

Issue of the periodical within the volume

13

Country of publishing house

US - UNITED STATES

Number of pages

13

Pages from-to

4224-4236

UT code for WoS article

000523442500012

EID of the result in the Scopus database

2-s2.0-85082561012