Publication

Cation permeability in CorA family of proteins

Stetsenko, A. & Guskov, A., 21-Jan-2020, In : Scientific Reports. 10, 9 p., 840.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Stetsenko, A., & Guskov, A. (2020). Cation permeability in CorA family of proteins. Scientific Reports, 10, [840]. https://doi.org/10.1038/s41598-020-57869-z

Author

Stetsenko, Artem ; Guskov, Albert. / Cation permeability in CorA family of proteins. In: Scientific Reports. 2020 ; Vol. 10.

Harvard

Stetsenko, A & Guskov, A 2020, 'Cation permeability in CorA family of proteins', Scientific Reports, vol. 10, 840. https://doi.org/10.1038/s41598-020-57869-z

Standard

Cation permeability in CorA family of proteins. / Stetsenko, Artem; Guskov, Albert.

In: Scientific Reports, Vol. 10, 840, 21.01.2020.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Stetsenko A, Guskov A. Cation permeability in CorA family of proteins. Scientific Reports. 2020 Jan 21;10. 840. https://doi.org/10.1038/s41598-020-57869-z


BibTeX

@article{9858672b4032426d8a1d5cd210526ff2,
title = "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 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.",
author = "Artem Stetsenko and Albert Guskov",
year = "2020",
month = "1",
day = "21",
doi = "10.1038/s41598-020-57869-z",
language = "English",
volume = "10",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Cation permeability in CorA family of proteins

AU - Stetsenko, Artem

AU - Guskov, Albert

PY - 2020/1/21

Y1 - 2020/1/21

N2 - 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.

AB - 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.

U2 - 10.1038/s41598-020-57869-z

DO - 10.1038/s41598-020-57869-z

M3 - Article

VL - 10

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 840

ER -

ID: 112510423