Natural variation in arsenate tolerance identifies an arsenate reductase in Arabidopsis thaliana
Autor: | S. Zarco-Fernández, Carmen Cámara, Gabriel Castrillo, Antonio Leyva, Carlos Alonso-Blanco, Cristina Navarro, Bárbara del Llano, Riansares Muñoz, Eduardo Sánchez-Bermejo, Dannys Jorge Martinez-Herrera, Javier Paz-Ares, Yolanda Leo del Puerto |
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Rok vydání: | 2014 |
Předmět: |
inorganic chemicals
Models Molecular Arsenate Reductases Arsenites Molecular Sequence Data Quantitative Trait Loci Arabidopsis Molecular Conformation General Physics and Astronomy chemistry.chemical_element Quantitative trait locus General Biochemistry Genetics and Molecular Biology Arsenic chemistry.chemical_compound Gene Expression Regulation Plant Botany Escherichia coli Arabidopsis thaliana Amino Acid Sequence Gene Alleles Genetics Multidisciplinary Polymorphism Genetic integumentary system biology Sequence Homology Amino Acid Arabidopsis Proteins fungi Genetic Complementation Test Arsenate food and beverages Chromosome Mapping General Chemistry biology.organism_classification Enzyme assay Thiosulfate Sulfurtransferase Oxygen Arsenate reductase Phenotype chemistry Mutation biology.protein Adaptation |
Zdroj: | Nature communications. 5 |
ISSN: | 2041-1723 |
Popis: | The 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. |
Databáze: | OpenAIRE |
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