ALMT-independent guard cell R-type anion currents

Abstract

ABSTRACTPlant transpiration is controlled by stomata, with S- and R-type anion channels playing key roles in guard cell action. Arabidopsis mutants lacking the ALMT12/QUAC1 R-type anion channel function in guard cells show only a partial reduction in R-type channel currents. To identify the molecular nature of the remaining R-type anion channel population, patch clamp studies were performed. This R-type current fraction in thealmt12mutant exhibited the same voltage dependence, susceptibility to ATP block and lacked a chloride permeability as the wildtype. Therefore, we asked whether the R-type anion currents in the ALMT12/QUAC1-free mutant are caused by additional ALMT isoforms. In wildtype guard cellsALMT12, ALMT13andALMT14transcripts were detected, whereas only ALMT13 was found expressed in thealmt12mutant. Substantial R-type anion currents still remained active in thealmt12/13andalmt12/14double mutants as well as thealmt12/13/14triple mutant. This situation, supported by transpiration measurements, suggests that, with the exception of ALMT12, channel species other than ALMTs carry the guard cell R-type anion currents.