Deletion of the N-terminal domain of the yeast vacuolar (Na+ ,K+ )/H+ antiporter Vnx1p improves salt tolerance in yeast and transgenic Arabidopsis.

Olivier Cagnac, Mourad Baghour, Noelia Jaime-Pérez, M Nieves Aranda-Sicilia, M Elena Sánchez-Romero, M Pilar Rodríguez-Rosales, Kees Venema

Yeast (Chichester, England) 2020 Jan

filter terms:

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. © 2019 John Wiley & Sons, Ltd.

Citation

Olivier Cagnac, Mourad Baghour, Noelia Jaime-Pérez, M Nieves Aranda-Sicilia, M Elena Sánchez-Romero, M Pilar Rodríguez-Rosales, Kees Venema. Deletion of the N-terminal domain of the yeast vacuolar (Na+ ,K+ )/H+ antiporter Vnx1p improves salt tolerance in yeast and transgenic Arabidopsis. Yeast (Chichester, England). 2020 Jan;37(1):173-185