Nematocida displodere mechanosensitive ion channel of small conductance 2 assembles into a unique 6-channel super-structure in vitro.

Autor: Berg A; Department of Molecular Biology, The Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå Centre for Microbial Research, Science for Life Laboratory, Umeå University, Umeå, Västerbotten, Sweden.; Department of Medical Biochemistry and Biophysics, Wallenberg Centre for Molecular Medicine, Umeå University, Umeå, Västerbotten, Sweden., Berntsson RP; Department of Medical Biochemistry and Biophysics, Wallenberg Centre for Molecular Medicine, Umeå University, Umeå, Västerbotten, Sweden.; Wallenberg Centre for Molecular Medicine & Umeå Centre for Microbial Research, Umeå University, Umeå, Sweden., Barandun J; Department of Molecular Biology, The Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå Centre for Microbial Research, Science for Life Laboratory, Umeå University, Umeå, Västerbotten, Sweden.
Jazyk: angličtina
Zdroj: PloS one [PLoS One] 2024 Jul 22; Vol. 19 (7), pp. e0301951. Date of Electronic Publication: 2024 Jul 22 (Print Publication: 2024).
DOI: 10.1371/journal.pone.0301951
Abstrakt: Mechanosensitive ion channels play an essential role in reacting to environmental signals and sustaining cell integrity by facilitating ion flux across membranes. For obligate intracellular pathogens like microsporidia, adapting to changes in the host environment is crucial for survival and propagation. Despite representing a eukaryote of extreme genome reduction, microsporidia have expanded the gene family of mechanosensitive ion channels of small conductance (mscS) through repeated gene duplication and horizontal gene transfer. All microsporidian genomes characterized to date contain mscS genes of both eukaryotic and bacterial origin. Here, we investigated the cryo-electron microscopy structure of the bacterially derived mechanosensitive ion channel of small conductance 2 (MscS2) from Nematocida displodere, an intracellular pathogen of Caenorhabditis elegans. MscS2 is the most compact MscS-like channel known and assembles into a unique superstructure in vitro with six heptameric MscS2 channels. Individual MscS2 channels are oriented in a heterogeneous manner to one another, resembling an asymmetric, flexible six-way cross joint. Finally, we show that microsporidian MscS2 still forms a heptameric membrane channel, however the extreme compaction suggests a potential new function of this MscS-like protein.
Competing Interests: The authors have declared that no competing interests exist.
(Copyright: © 2024 Berg et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.)
Databáze: MEDLINE
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