High affinity Na+ transport by wheat HKT1;5 is blocked by K

Plant Direct. 2020 Oct 21;4(10):e00275. doi: 10.1002/pld3.275. eCollection 2020 Oct.


The wheat sodium transporters TmHKT1;5-A and TaHKT1;5-D are encoded by genes underlying the major shoot Na+ exclusion loci Nax2 and Kna1 from Triticum monococcum (Tm) and Triticum aestivum (Ta), respectively. In contrast to HKT2 transporters that have been shown to exhibit high affinity K+-dependent Na+ transport, HKT1 proteins have, with one exception, only been shown to catalyze low affinity Na+ transport and no K+ transport. Here, using heterologous expression in Xenopus laevis oocytes we uncover a novel property of HKT1 proteins, that both TmHKT1;5-A and TaHKT1;5-D encode dual (high and low) affinity Na+-transporters with the high-affinity component being abolished when external K+ is in excess of external Na+. Three-dimensional structural modeling suggested that, compared to Na+, K+ is bound more tightly in the selectivity filter region by means of additional van der Waals forces, which is likely to explain the K+ block at the molecular level. The low-affinity component for Na+ transport of TmHKT1;5-A had a lower K m than that of TaHKT1;5-D and was less sensitive to external K+. We propose that these properties contribute towards the improvements in shoot Na+-exclusion and crop plant salt tolerance following the introgression of TmHKT1;5-A into diverse wheat backgrounds.

Keywords: KtrB; dual affinity; high‐affinity K transporters; membrane transport; salinity; sodium exclusion.