Natural variation in arsenate tolerance identifies an arsenate reductase in Arabidopsis thaliana
2014; Nature Portfolio; Volume: 5; Issue: 1 Linguagem: Inglês
10.1038/ncomms5617
ISSN2041-1723
AutoresEduardo Sánchez-Bermejo, Gabriel Castrillo, Bárbara del Llano, Cristina Navarro, S. Zarco-Fernández, Dannys Jorge Martínez-Herrera, Yolanda Leo del Puerto, Riansares Muñoz, Carmen Cámara, Javier Paz‐Ares, Carlos Alonso‐Blanco, Antonio Leyva,
Tópico(s)Photosynthetic Processes and Mechanisms
ResumoThe enormous amount of environmental arsenic was a major factor in determining the biochemistry of incipient life forms early in the Earth’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. Arsenic tolerance in plants is critical for their adaptation to some soils and has therefore played an important role in plant distribution. Here, the authors identify a quantitative trait locus encoding an arsenate reductase enzyme that confers arsenic tolerance in plants.
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