Natural variation in arsenate tolerance identifies an arsenate reductase in Arabidopsis thaliana

作者：Sanchez Bermejo Eduardo; Castrillo Gabriel; del Llano Barbara; Navarro Cristina; Zarco Fernandez Sonia; Jorge Martinez Herrera Dannys; Leo del Puerto Yolanda; Munoz Riansares; Camara Carmen; Paz Ares Javier; Alonso Blanco Carlos; Leyva Antonio^*

来源：Nature Communications, 2014, 5(1): 4617.

DOI：10.1038/ncomms5617

The enormous amount of environmental arsenic was a major factor in determining the biochemistry of incipient life forms early in the Earth%26apos;s history. The most abundant chemical form in the reducing atmosphere was arsenite, which forced organisms to evolve strategies to manage this chemical species. Following the great oxygenation event, arsenite oxidized to arsenate and the action of arsenate reductases became a central survival requirement. The identity of a biologically relevant arsenate reductase in plants nonetheless continues to be debated. Here we identify a quantitative trait locus that encodes a novel arsenate reductase critical for arsenic tolerance in plants. Functional analyses indicate that several non-additive polymorphisms affect protein structure and account for the natural variation in arsenate reductase activity in Arabidopsis thaliana accessions. This study shows that arsenate reductases are an essential component for natural plant variation in As(V) tolerance.

• 出版日期2014-8