INWARD RECTIFIER POTASSIUM CHANNELS IN PLANTS DIFFER FROM THEIR ANIMAL COUNTERPARTS IN RESPONSE TO VOLTAGE AND CHANNEL MODULATORS

We have investigated the electrophysiological basis of potassium inwar d rectification of the KAT1 gene product from Arabidopsis thaliana exp ressed in Xenopus oocytes and of functionally related Kf channels in t he plasmamembrane of guard and root cells from Vicia faba and Zen mays . The whole-cell currents passed by these channels activate, following steps to membrane potentials more negative than -100 mV, with half ac tivation times of tens of milliseconds. This voltage dependence was un affected by the removal of cytoplasmic magnesium. Consequently, unlike inward rectifier channels of animals, inward rectification of plant p otassium channels is an intrinsic property of the channel protein itse lf. We also found that the activation kinetics of KAT1 were modulated by external pH. Decreasing the pH in the range 8.5 to 4.5 hastened act ivation and shifted the steady state activation curve by 19 mV per pH unit. This indicates that the activity of these K+ channels and the ac tivity of the plasma membrane H+-ATPase may not only be coordinated by membrane potential but also by pH. The instantaneous current-voltage relationship, on the other hand, did not depend on pH, indicating that H+ do not block the channel. In addition to sensitivity towards proto ns, the channels showed a high affinity voltage dependent block in the presence of cesium, but were less sensitive to barium. Recordings fro m membrane patches of KAT1 injected oocytes in symmetric, Mg2+-free, 1 00 mM-K+, solutions allowed measurements of the current-voltage relati on of single open KAT1 channels with a unitary conductance of 5 pS. We conclude that the inward rectification of the currents mediated by th e KAT1 gene product, or the related endogenous channels of plant cells , results from voltage-modulated structural changes within the channel proteins. The voltage-sensing or the gating-structures appear to inte ract with a titratable acidic residue exposed to the extracellular med ium.