A PIP1 aquaporin contributes to hydrostatic pressure-induced water transport in both the root and rosette of Arabidopsis.
Aquaporins are channel proteins that facilitate the transport of water across plant cell membranes. In this work, we used a combination of pharmacological and reverse genetic approaches to investigate the overall significance of aquaporins for tissue water conductivity in Arabidopsis (Arabidopsis thaliana). We addressed the function in roots and leaves of AtPIP1;2, one of the most abundantly expressed isoforms of the plasma membrane intrinsic protein family. At variance with the water transport phenotype previously described in AtPIP2;2 knockout mutants, disruption of AtPIP1;2 reduced by 20% to 30% the root hydrostatic hydraulic conductivity but did not modify osmotic root water transport. These results document qualitatively distinct functions of different PIP isoforms in root water uptake. The hydraulic conductivity of excised rosettes (K(ros)) was measured by a novel pressure chamber technique. Exposure of Arabidopsis plants to darkness increased K(ros) by up to 90%. Mercury and azide, two aquaporin inhibitors with distinct modes of action, were able to induce similar inhibition of K(ros) by approximately 13% and approximately 25% in rosettes from plants grown in the light or under prolonged (11-18 h) darkness, respectively. Prolonged darkness enhanced the transcript abundance of several PIP genes, including AtPIP1;2. Mutant analysis showed that, under prolonged darkness conditions, AtPIP1;2 can contribute to up to approximately 20% of K(ros) and to the osmotic water permeability of isolated mesophyll protoplasts. Therefore, AtPIP1;2 can account for a significant portion of aquaporin-mediated leaf water transport. The overall work shows that AtPIP1;2 represents a key component of whole-plant hydraulics.
Postaire
Olivier
O
Biochimie et Physiologie Moléculaire des Plantes, Institut de Biologie Intégrative des Plantes, UMR 5004 CNRS/UMR 0386 INRA/Montpellier SupAgro/Université Montpellier 2, F-34060 Montpellier cedex 1, France.
Tournaire-Roux
Colette
C
Grondin
Alexandre
A
Boursiac
Yann
Y
Morillon
Raphaël
R
Schäffner
Anton R
AR
Maurel
Christophe
C
D020346:Aquaporins / Q000235:genetics / Q000378:metabolism*; D017360:Arabidopsis / Q000235:genetics / Q000502:physiology*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D001386:Azides / Q000494:pharmacology; D004269:DNA, Bacterial / Q000235:genetics; D018744:DNA, Plant / Q000235:genetics; D003624:Darkness; D018506:Gene Expression Regulation, Plant; D005816:Genetic Complementation Test; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D008628:Mercury / Q000494:pharmacology; D016254:Mutagenesis, Insertional; D009154:Mutation; D009995:Osmosis; D018515:Plant Leaves / Q000502:physiology*; D018517:Plant Roots / Q000502:physiology*; D030821:Plants, Genetically Modified / Q000235:genetics / Q000502:physiology; D014867:Water / Q000378:metabolism*
D020346:Aquaporins; D029681:Arabidopsis Proteins; D001386:Azides; D004269:DNA, Bacterial; D018744:DNA, Plant; D008565:Membrane Proteins; D008628:Mercury; D014867:Water; C085550:At2g45960 protein, Arabidopsis; C036483:T-DNA