Arabidopsis thaliana vacuolar TPK channels form functional K(+) uptake pathways in Escherichia coli

Very few vacuolar two pore potassium channels (TPKs) have been functionally characterized. In this paper we have used complementation of K(+) uptake deficient Escherichia coli mutant LB2003 to analyze the functional properties of Arabidopsis thaliana TPK family members. The four isoforms of AtTPKs w...

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Autores principales: Isayenkov, Stanislav, Maathuis, Frans J M
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2013
Materias:
Research Paper
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3909031/
https://www.ncbi.nlm.nih.gov/pubmed/23656881
http://dx.doi.org/10.4161/psb.24665
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author Isayenkov, Stanislav
Maathuis, Frans J M
author_facet Isayenkov, Stanislav
Maathuis, Frans J M
author_sort Isayenkov, Stanislav
collection PubMed
description Very few vacuolar two pore potassium channels (TPKs) have been functionally characterized. In this paper we have used complementation of K(+) uptake deficient Escherichia coli mutant LB2003 to analyze the functional properties of Arabidopsis thaliana TPK family members. The four isoforms of AtTPKs were cloned and expressed in LB2003 E. coli background.The expression of channels in bacteria was analyzed by RT-PCR. Our results show that AtTPK1, AtTPK2 and AtTPK5 are restoring the LB2003 growth on low K(+) media. The analysis of potassium uptake exhibited elevated level of K(+) uptake in the same three types of AtTPKs transformants.
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spelling pubmed-39090312014-02-05 Arabidopsis thaliana vacuolar TPK channels form functional K(+) uptake pathways in Escherichia coli Isayenkov, Stanislav Maathuis, Frans J M Plant Signal Behav Research Paper Very few vacuolar two pore potassium channels (TPKs) have been functionally characterized. In this paper we have used complementation of K(+) uptake deficient Escherichia coli mutant LB2003 to analyze the functional properties of Arabidopsis thaliana TPK family members. The four isoforms of AtTPKs were cloned and expressed in LB2003 E. coli background.The expression of channels in bacteria was analyzed by RT-PCR. Our results show that AtTPK1, AtTPK2 and AtTPK5 are restoring the LB2003 growth on low K(+) media. The analysis of potassium uptake exhibited elevated level of K(+) uptake in the same three types of AtTPKs transformants. Landes Bioscience 2013-07-01 2013-04-22 /pmc/articles/PMC3909031/ /pubmed/23656881 http://dx.doi.org/10.4161/psb.24665 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Research Paper
Isayenkov, Stanislav
Maathuis, Frans J M
Arabidopsis thaliana vacuolar TPK channels form functional K(+) uptake pathways in Escherichia coli
title Arabidopsis thaliana vacuolar TPK channels form functional K(+) uptake pathways in Escherichia coli
title_full Arabidopsis thaliana vacuolar TPK channels form functional K(+) uptake pathways in Escherichia coli
title_fullStr Arabidopsis thaliana vacuolar TPK channels form functional K(+) uptake pathways in Escherichia coli
title_full_unstemmed Arabidopsis thaliana vacuolar TPK channels form functional K(+) uptake pathways in Escherichia coli
title_short Arabidopsis thaliana vacuolar TPK channels form functional K(+) uptake pathways in Escherichia coli
title_sort arabidopsis thaliana vacuolar tpk channels form functional k(+) uptake pathways in escherichia coli
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3909031/
https://www.ncbi.nlm.nih.gov/pubmed/23656881
http://dx.doi.org/10.4161/psb.24665
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AT maathuisfransjm arabidopsisthalianavacuolartpkchannelsformfunctionalkuptakepathwaysinescherichiacoli

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