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arsenic/arabidopsis
L'enllaç es desa al porta-retalls
Pàgina 1 des de 101 resultats
Overexpression of phytochelatin synthase in Arabidopsis leads to enhanced arsenic tolerance and cadmium hypersensitivity.
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Phytochelatin synthase (PCS) catalyzes the final step in the biosynthesis of phytochelatins, which are a family of cysteine-rich thiol-reactive peptides believed to play important roles in processing many thiol-reactive toxicants. A modified Arabidopsis thaliana PCS sequence (AtPCS1) was active in
Arsenic Methylation in Arabidopsis thaliana Expressing an Algal Arsenite Methyltransferase Gene Increases Arsenic Phytotoxicity.
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Arsenic (As) contamination in soil can lead to elevated transfer of As to the food chain. One potential mitigation strategy is to genetically engineer plants to enable them to transform inorganic As to methylated and volatile As species. In this study, we genetically engineered two ecotypes of
Phytoremediation of arsenic from the contaminated soil using transgenic tobacco plants expressing ACR2 gene of Arabidopsis thaliana.
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We have cloned, characterized and transformed the AtACR2 gene (arsenic reductase 2) of Arabidopsis thaliana into the genome of tobacco (Nicotiana tabacum, var Sumsun). Our results revealed that the transgenic tobacco plants are more tolerant to arsenic than the wild type ones. These plants can grow
Co-expression of Arabidopsis thaliana phytochelatin synthase and Treponema denticola cysteine desulfhydrase for enhanced arsenic accumulation.
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Arsenic is one of the most hazardous pollutants found in aqueous environments and has been shown to be a carcinogen. Phytochelatins (PCs), which are cysteine-rich and thio-reactive peptides, have high binding affinities for various metals including arsenic. Previously, we demonstrated that
Arsentate Induced CHLOROSIS 1/ TRANSLOCON at the outer envelope membrane of CHLOROPLASTS 132 Protects Chloroplasts from Arsenic Toxicity.
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Arsenic (As) is highly toxic to plants and detoxified primarily through complexation with phytochelatins (PCs) and other thiol compounds. To understand the mechanisms of As toxicity and detoxification beyond PCs, we isolated an arsenate-sensitive mutant of Arabidopsis (Arabidopsis thaliana),
Identification of an arsenic tolerant double mutant with a thiol-mediated component and increased arsenic tolerance in phyA mutants.
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A genetic screen was performed to isolate mutants showing increased arsenic tolerance using an Arabidopsis thaliana population of activation tagged lines. The most arsenic-resistant mutant shows increased arsenate and arsenite tolerance. Genetic analyses of the mutant indicate that the mutant
Cytokinin Determines Thiol-Mediated Arsenic Tolerance and Accumulation.
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The presence of arsenic in soil and water is a constant threat to plant growth in many regions of the world. Phytohormones act in the integration of growth control and stress response, but their role in plant responses to arsenic remains to be elucidated. Here, we show that arsenate [As(V)], the
Hyperaccumulation of arsenic by callus, sporophytes and gametophytes of Pteris vittata cultured in vitro.
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The callus of Pteris vittata was induced from gametophytes generated from spores in vitro, and grew rapidly with periodical medium change. Arsenic tolerance and accumulation of P. vittata callus were compared with those of Arabidopsis thaliana callus. Cell death was not detected in P. vittata callus
The shoot-specific expression of gamma-glutamylcysteine synthetase directs the long-distance transport of thiol-peptides to roots conferring tolerance to mercury and arsenic.
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Thiol-peptides synthesized as intermediates in phytochelatin (PC) biosynthesis confer cellular tolerance to toxic elements like arsenic, mercury, and cadmium, but little is known about their long-distance transport between plant organs. A modified bacterial gamma-glutamylcysteine synthetase (ECS)
Heterologous Expression of Pteris vittata Phosphate Transporter PvPht1;3 Enhances Arsenic Translocation to and Accumulation in Tobacco Shoots.
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Arsenic-hyperaccumulator Pteris vittata is efficient in As accumulation and has been used in phytoremediation of As-contaminated soils. Arsenate (AsV) is the predominant As species in aerobic soils and is taken up by plants via phosphate transporters (Pht) including P. vittata. In this
Dissecting the components controlling root-to-shoot arsenic translocation in Arabidopsis thaliana.
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Arsenic (As) is an important environmental and food-chain toxin. We investigated the key components controlling As accumulation and tolerance in Arabidopsis thaliana. We tested the effects of different combinations of gene knockout, including arsenate reductase (HAC1), γ-glutamyl-cysteine synthetase
Arsenic uptake, translocation and speciation in pho1 and pho2 mutants of Arabidopsis thaliana.
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Arsenate [As (V)] is taken up by phosphate [P (V)] transporters in the plasma membrane of roots cells, but the translocation of As from roots to shoots is not well understood. Two mutants of Arabidopsis thaliana (L.) [(pho1, P deficient) and (pho2, P accumulator)], with defects in the regulation and
Phytotoxicities of inorganic arsenic and dimethylarsinic acid to Arabidopsis thaliana and Pteris vittata.
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The mechanisms by which Pteris vittata (L.) hyperaccumulates arsenic (As) have not been fully elucidated. To investigate how P. vittata tolerates high concentrations of arsenite, we compared the toxicities of various As compounds to P. vittata and Arabidopsis thaliana (L.). The phytotoxicities of As
Arabidopsis thaliana MRP1 (AtABCC1) nucleotide binding domain contributes to arsenic stress tolerance with serine triad phosphorylation.
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Multidrug resistance protein AtMRPs belong to the ATP binding cassette (ABC) transporter super family. ABC proteins are membrane proteins involved in the transport of a broad range of amphipathic organic anions across membranes. MRPs (ABCCs) are one of the highly represented subfamilies of ABC
Enhanced arsenic accumulation by engineered yeast cells expressing Arabidopsis thaliana phytochelatin synthase.
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Phytochelatins (PCs) are naturally occurring peptides with high-binding capabilities for a wide range of heavy metals including arsenic (As). PCs are enzymatically synthesized by phytochelatin synthases and contain a (gamma-Glu-Cys)(n) moiety terminated by a Gly residue that makes them relatively
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