Cation permeability in CorA family of proteins

Abstract CorA proteins belong to 2-TM-GxN family of membrane proteins, and play a major role in Mg2+ transport in prokaryotes and eukaryotic mitochondria. The selection of substrate is believed to occur via the signature motif GxN, however there is no consensus how strict this selection within the f...

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Autores principales:	Artem Stetsenko, Albert Guskov
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/107fc948f5d841d7ab6a3b013551f932
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spelling	oai:doaj.org-article:107fc948f5d841d7ab6a3b013551f9322021-12-02T15:23:40ZCation permeability in CorA family of proteins10.1038/s41598-020-57869-z2045-2322https://doaj.org/article/107fc948f5d841d7ab6a3b013551f9322020-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-57869-zhttps://doaj.org/toc/2045-2322Abstract CorA proteins belong to 2-TM-GxN family of membrane proteins, and play a major role in Mg2+ transport in prokaryotes and eukaryotic mitochondria. The selection of substrate is believed to occur via the signature motif GxN, however there is no consensus how strict this selection within the family. To answer this question, we employed fluorescence-based transport assays on three different family members, namely CorA from bacterium Thermotoga maritima, CorA from the archeon Methanocaldococcus jannaschii and ZntB from bacterium Escherichia coli, reconstituted into proteoliposomes. Our results show that all three proteins readily transport Mg2+, Co2+, Ni2+ and Zn2+, but not Al3+. Despite the similarity in cation specificity, ZntB differs from the CorA proteins, as in the former transport is stimulated by a proton gradient, but in the latter by the membrane potential, confirming the hypothesis that CorA and ZntB proteins diverged to different transport mechanisms within the same protein scaffold.Artem StetsenkoAlbert GuskovNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 10, Iss 1, Pp 1-9 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Artem Stetsenko Albert Guskov Cation permeability in CorA family of proteins
description	Abstract CorA proteins belong to 2-TM-GxN family of membrane proteins, and play a major role in Mg2+ transport in prokaryotes and eukaryotic mitochondria. The selection of substrate is believed to occur via the signature motif GxN, however there is no consensus how strict this selection within the family. To answer this question, we employed fluorescence-based transport assays on three different family members, namely CorA from bacterium Thermotoga maritima, CorA from the archeon Methanocaldococcus jannaschii and ZntB from bacterium Escherichia coli, reconstituted into proteoliposomes. Our results show that all three proteins readily transport Mg2+, Co2+, Ni2+ and Zn2+, but not Al3+. Despite the similarity in cation specificity, ZntB differs from the CorA proteins, as in the former transport is stimulated by a proton gradient, but in the latter by the membrane potential, confirming the hypothesis that CorA and ZntB proteins diverged to different transport mechanisms within the same protein scaffold.
format	article
author	Artem Stetsenko Albert Guskov
author_facet	Artem Stetsenko Albert Guskov
author_sort	Artem Stetsenko
title	Cation permeability in CorA family of proteins
title_short	Cation permeability in CorA family of proteins
title_full	Cation permeability in CorA family of proteins
title_fullStr	Cation permeability in CorA family of proteins
title_full_unstemmed	Cation permeability in CorA family of proteins
title_sort	cation permeability in cora family of proteins
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/107fc948f5d841d7ab6a3b013551f932
work_keys_str_mv	AT artemstetsenko cationpermeabilityincorafamilyofproteins AT albertguskov cationpermeabilityincorafamilyofproteins
_version_	1718387246668709888

Cation permeability in CorA family of proteins

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