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XB-ART-54316
Cell Mol Life Sci 2018 Mar 01;756:1133-1144. doi: 10.1007/s00018-017-2716-5.
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Structural variations in wheat HKT1;5 underpin differences in Na+ transport capacity.

Xu B , Waters S , Byrt CS , Plett D , Tyerman SD , Tester M , Munns R , Hrmova M , Gilliham M .


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An important trait associated with the salt tolerance of wheat is the exclusion of sodium ions (Na+) from the shoot. We have previously shown that the sodium transporters TmHKT1;5-A and TaHKT1;5-D, from Triticum monoccocum (Tm) and Triticum aestivum (Ta), are encoded by genes underlying the major shoot Na+-exclusion loci Nax1 and Kna1, respectively. Here, using heterologous expression, we show that the affinity (K m) for the Na+ transport of TmHKT1;5-A, at 2.66 mM, is higher than that of TaHKT1;5-D at 7.50 mM. Through 3D structural modelling, we identify residues D471/a gap and D474/G473 that contribute to this property. We identify four additional mutations in amino acid residues that inhibit the transport activity of TmHKT1;5-A, which are predicted to be the result of an occlusion of the pore. We propose that the underlying transport properties of TmHKT1;5-A and TaHKT1;5-D contribute to their unique ability to improve Na+ exclusion in wheat that leads to an improved salinity tolerance in the field.

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References [+] :
Ali, A Single Amino-Acid Substitution in the Sodium Transporter HKT1 Associated with Plant Salt Tolerance. 2016, Pubmed, Xenbase