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Structure-Function Relationships of NHX Antiporters of Arabidopsis thaliana.

AuthorsRombolá-Caldentey, B.; Cubero, Beatriz ; Schmöckel S.M.; Quintero, Francisco J. ; Pardo, José M.
Issue Date7-Jul-2019
PublisherAmerican Society of Plant Biologists
CitationStructure-Function Relationships of NHX Antiporters of Arabidopsis thaliana (Póster) 2019
AbstractThe K+,Na+/H+ exchangers NHX of Arabidopsis thaliana mediate the accumulation of K+ into the vacuole of cells, thereby increasing the osmotic potential, water uptake and the turgor pressure necessary for cell expansion and growth, as well as for regulation of vacuolar pH. They are part of the Cation Proton Antiporter superfamily (CPA), a highly conserved group of transmembrane proteins that exchange cations for protons in opposite directions to locally modulate pH, as well as electrical and cation balances. Using a phylogenetic approach, we aimed to get a better insight of the NHX1 protein structure, function and regulation. As a result of our studies we could generate new topological and ternary models of NHX1. By conservation analyses we could identify essential structural domains and amino acid residues putatively involved in ion transport, cation coordination, and pH sensing of the protein. Pointmutation alleles of these relevant residues were generated, and their impact on the biochemical activity and pH dependence of NHX1 by functionality tests in yeast was studied. Of special interest are the results obtained from allele mutants generated by emulating the motifs of electrogenic CPA proteins in order to transform the electroneutral nature of NHX1 into electrogenic. Overall, our results demonstrate that AtNHX1 conserves the structural features characteristic of microbial and mammalian members of the CPA superfamily.
DescriptionPóster presentado en el 18th International Workshop on Plant Membrane Biology, July 7-12, 2019, Glasgow, UK
Appears in Collections:(IBVF) Comunicaciones congresos
(IRNAS) Comunicaciones congresos
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