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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...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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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. |
format | Online Article Text |
id | pubmed-7397200 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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