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Deletion of the N‐terminal domain of the yeast vacuolar (Na + ,K + )/H + antiporter Vnx1p improves salt tolerance in yeast and transgenic Arabidopsis
Author(s) -
Cagnac Olivier,
Baghour Mourad,
JaimePérez Noelia,
ArandaSicilia M. Nieves,
SánchezRomero M. Elena,
RodríguezRosales M. Pilar,
Venema Kees
Publication year - 2020
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.3450
Subject(s) - antiporters , antiporter , yeast , arabidopsis , biology , sodium–hydrogen antiporter , cytosol , salinity , salt (chemistry) , vacuole , saccharomyces cerevisiae , biochemistry , microbiology and biotechnology , gene , biophysics , sodium , cytoplasm , chemistry , enzyme , membrane , mutant , ecology , organic chemistry
Cation/proton antiporters play a major role in the control of cytosolic ion concentrations in prokaryotes and eukaryotes organisms. In yeast, we previously demonstrated that Vnx1p is a vacuolar monovalent cation/H + exchanger showing Na + /H + and K + /H + antiporter activity. We have also shown that disruption of VNX1 results in an almost complete abolishment of vacuolar Na + /H + exchange, but yeast cells overexpressing the complete protein do not show improved salinity tolerance. In this study, we have identified an autoinhibitory N‐terminal domain and have engineered a constitutively activated version of Vnx1p, by removing this domain. Contrary to the wild type protein, the activated protein has a pronounced effect on yeast salt tolerance and vacuolar pH. Expression of this truncated VNX1 gene also improves Arabidopsis salt tolerance and increases Na + and K + accumulation of salt grown plants thus suggesting a biotechnological potential of activated Vnx1p to improve salt tolerance of crop plants.