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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) (Mp...

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Autores principales: Novikova, Olga D., Khomenko, Valentina A., Kim, Natalia Yu., Likhatskaya, Galina N., Romanenko, Lyudmila A., Aksenova, Ekaterina I., Kunda, Marina S., Ryzhova, Natalia N., Portnyagina, Olga Yu., Solov’eva, Tamara F., Voronina, Olga L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7397200/
https://www.ncbi.nlm.nih.gov/pubmed/32650591
http://dx.doi.org/10.3390/molecules25143131
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author Novikova, Olga D.
Khomenko, Valentina A.
Kim, Natalia Yu.
Likhatskaya, Galina N.
Romanenko, Lyudmila A.
Aksenova, Ekaterina I.
Kunda, Marina S.
Ryzhova, Natalia N.
Portnyagina, Olga Yu.
Solov’eva, Tamara F.
Voronina, Olga L.
author_facet Novikova, Olga D.
Khomenko, Valentina A.
Kim, Natalia Yu.
Likhatskaya, Galina N.
Romanenko, Lyudmila A.
Aksenova, Ekaterina I.
Kunda, Marina S.
Ryzhova, Natalia N.
Portnyagina, Olga Yu.
Solov’eva, Tamara F.
Voronina, Olga L.
author_sort Novikova, Olga D.
collection PubMed
description 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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spelling pubmed-73972002020-08-16 Porin from Marine Bacterium Marinomonas primoryensis KMM 3633(T): Isolation, Physico-Chemical Properties, and Functional Activity Novikova, Olga D. Khomenko, Valentina A. Kim, Natalia Yu. Likhatskaya, Galina N. Romanenko, Lyudmila A. Aksenova, Ekaterina I. Kunda, Marina S. Ryzhova, Natalia N. Portnyagina, Olga Yu. Solov’eva, Tamara F. Voronina, Olga L. Molecules Article 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. MDPI 2020-07-08 /pmc/articles/PMC7397200/ /pubmed/32650591 http://dx.doi.org/10.3390/molecules25143131 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Novikova, Olga D.
Khomenko, Valentina A.
Kim, Natalia Yu.
Likhatskaya, Galina N.
Romanenko, Lyudmila A.
Aksenova, Ekaterina I.
Kunda, Marina S.
Ryzhova, Natalia N.
Portnyagina, Olga Yu.
Solov’eva, Tamara F.
Voronina, Olga L.
Porin from Marine Bacterium Marinomonas primoryensis KMM 3633(T): Isolation, Physico-Chemical Properties, and Functional Activity
title Porin from Marine Bacterium Marinomonas primoryensis KMM 3633(T): Isolation, Physico-Chemical Properties, and Functional Activity
title_full Porin from Marine Bacterium Marinomonas primoryensis KMM 3633(T): Isolation, Physico-Chemical Properties, and Functional Activity
title_fullStr Porin from Marine Bacterium Marinomonas primoryensis KMM 3633(T): Isolation, Physico-Chemical Properties, and Functional Activity
title_full_unstemmed Porin from Marine Bacterium Marinomonas primoryensis KMM 3633(T): Isolation, Physico-Chemical Properties, and Functional Activity
title_short Porin from Marine Bacterium Marinomonas primoryensis KMM 3633(T): Isolation, Physico-Chemical Properties, and Functional Activity
title_sort porin from marine bacterium marinomonas primoryensis kmm 3633(t): isolation, physico-chemical properties, and functional activity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7397200/
https://www.ncbi.nlm.nih.gov/pubmed/32650591
http://dx.doi.org/10.3390/molecules25143131
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