Porin from Marine Bacterium Marinomonas primoryensis KMM 3633 T : Isolation, Physico-Chemical Properties, and Functional Activity

Marinomonas primoryensis KMM 3633 T , extreme living marine bacterium was isolated from a sample of coastal sea ice in the Amursky Bay near Vladivostok, Russia. The goal of our investigation is to study outer membrane channels determining cell permeability. Porin from M. primoryensis KMM 3633 T (MpO...

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Bibliographic Details
Published in:Molecules
Main Authors: Olga D. Novikova, Valentina A. Khomenko, Natalia Yu. Kim, Galina N. Likhatskaya, Lyudmila A. Romanenko, Ekaterina I. Aksenova, Marina S. Kunda, Natalia N. Ryzhova, Olga Yu. Portnyagina, Tamara F. Solov’eva, Olga L. Voronina
Format: Article in Journal/Newspaper
Language:English
Published: MDPI AG 2020
Subjects:
marine bacteria
whole genome sequence
porin
amino acids composition
bilayer lipid membrane
pore-forming activity
Organic chemistry
QD241-441
Sea ice
Online Access:https://doi.org/10.3390/molecules25143131
https://doaj.org/article/9aea5a212efb43bf934e0a5ca1ccf5e8
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Summary:Marinomonas primoryensis KMM 3633 T , extreme living marine bacterium was isolated from a sample of coastal sea ice in the Amursky Bay near Vladivostok, Russia. The goal of our investigation is to study outer membrane channels determining cell permeability. Porin from M. primoryensis KMM 3633 T (MpOmp) has been isolated and characterized. Amino acid analysis and whole genome sequencing were the sources of amino acid data of porin, identified as Porin_4 according to the conservative domain searching. The amino acid composition of MpOmp distinguished by high content of acidic amino acids and low content of sulfur-containing amino acids, but there are no tryptophan residues in its molecule. The native MpOmp existed as a trimer. The reconstitution of MpOmp into black lipid membranes demonstrated its ability to form ion channels whose conductivity depends on the electrolyte concentration. The spatial structure of MpOmp had features typical for the classical gram-negative porins. However, the oligomeric structure of isolated MpOmp was distinguished by very low stability: heat-modified monomer was already observed at 30 °C. The data obtained suggest the stabilizing role of lipids in the natural membrane of marine bacteria in the formation of the oligomeric structure of porin.

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