: Plants can survive in soils of low micromolar potassium (K+) concentrations. Root K+ intake is accomplished by the K+ channel AKT1 and KUP/HAK/KT type high-affinity K+ transporters. Arabidopsis HAK5 mutants impaired in low K+ acquisition have been identified already more than two decades ago, the molecular mechanism, however, is still a matter of debate also because of lack of direct measurements of HAK5-mediated K+ currents. When we expressed AtHAK5 in Xenopus oocytes together with CBL1/CIPK23, no inward currents were elicited in sufficient K+ media. Under low K+ and inward-directed proton motive force (PMF), the inward K+ current increased indicating that HAK5 energetically couples the uphill transport of K+ to the downhill flux of H+. At extracellular K+ concentrations above 25 μM, the initial rise in current was followed by a concentration-graded inactivation. When we replaced Tyr450 in AtHAK5 to Ala the K+ affinity strongly decreased, indicating that AtHAK5 position Y450 holds a key for K+ sensing and transport. When the soil K+ concentration drops toward the range that thermodynamically cannot be covered by AKT1, the AtHAK5 K+/H+ symporter progressively takes over K+ nutrition. Therefore, optimizing K+ use efficiency of crops, HAK5 could be key for low K+ tolerant agriculture.
Arabidopsis HAK5 under low K+ availability operates as PMF powered high-affinity K+ transporter
Armando Carpaneto;
2024-01-01
Abstract
: Plants can survive in soils of low micromolar potassium (K+) concentrations. Root K+ intake is accomplished by the K+ channel AKT1 and KUP/HAK/KT type high-affinity K+ transporters. Arabidopsis HAK5 mutants impaired in low K+ acquisition have been identified already more than two decades ago, the molecular mechanism, however, is still a matter of debate also because of lack of direct measurements of HAK5-mediated K+ currents. When we expressed AtHAK5 in Xenopus oocytes together with CBL1/CIPK23, no inward currents were elicited in sufficient K+ media. Under low K+ and inward-directed proton motive force (PMF), the inward K+ current increased indicating that HAK5 energetically couples the uphill transport of K+ to the downhill flux of H+. At extracellular K+ concentrations above 25 μM, the initial rise in current was followed by a concentration-graded inactivation. When we replaced Tyr450 in AtHAK5 to Ala the K+ affinity strongly decreased, indicating that AtHAK5 position Y450 holds a key for K+ sensing and transport. When the soil K+ concentration drops toward the range that thermodynamically cannot be covered by AKT1, the AtHAK5 K+/H+ symporter progressively takes over K+ nutrition. Therefore, optimizing K+ use efficiency of crops, HAK5 could be key for low K+ tolerant agriculture.
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