Deletion of the N‐terminal domain of the yeast vacuolar (Na+, K+)/H+ antiporter Vnx1p improves salt tolerance in yeast and transgenic Arabidopsis. Issue 1 (14th January 2020)

• Record Type: Journal Article
• Authors: Cagnac, Olivier; Baghour, Mourad; Jaime‐Pérez, Noelia; Aranda‐Sicilia, M. Nieves; Sánchez‐Romero, M. Elena; Rodríguez‐Rosales, M. Pilar; Venema, Kees
• Is Part Of: Yeast. Volume 37:Issue 1(2020:Jan.)
• Page Start: 173
• Page End: 185
• Publication Date: 2020-01-14
• Subjects: (Na+, K+)/H+ antiporters -- Arabidopsis -- ion transport -- salt tolerance -- vacuoles -- yeast; Yeast -- Periodicals; Yeasts -- Periodicals; Yeasts -- genetics -- Periodicals; Electronic journals; 547
• DOI: 10.1002/yea.3450
• Languages: English
• ISSNs: 0749-503X

Abstract

Abstract: 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.