Efficient arsenate reduction in As-hyperaccumulator Pteris vittata are mediated by novel arsenate reductases PvHAC1 and PvHAC2.

Arsenic-hyperaccumulator Pteris vittata is efficient in As absorption, reduction, and translocation. But the molecular mechanisms and locations of arsenate (AsV) reduction in P. vittata are still unclear. Here, we identified two new arsenate reductase genes from P. vittata, PvHAC1 and PvHAC2. Two PvHAC genes encoded a rhodanase-like protein, which were localized in the cytoplasm and nucleus. Both recombinant Escherichia coli strains and transgenic Arabidopsis thaliana lines showed arsenate reductase ability after expressing PvHAC genes. Further, expressing PvHAC2 enhanced As tolerance and reduced As accumulation in A. thaliana shoots under AsV exposure. Based on expression pattern analysis, PvHAC1 and PvHAC2 were predominantly expressed in the rhizomes and fronds of P. vittata. Different from those of HAC homologous genes in non-hyperaccumulators, little PvHAC was expressed in the roots. Besides, PvHAC1 expression was strongly upregulated under AsV exposure but not AsIII. The data suggest that arsenate reductase PvHAC1 in the rhizomes coupled with arsenate reductase PvHAC2 in the fronds of P. vittata played a critical role in As-hyperaccumulation by P. vittata, which helps to further improve its utility in phytoremediation of As-contaminated soils.