ArticleScientific reports2015
The arsenic hyperaccumulating Pteris vittata expresses two arsenate reductases.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 41 citations in OpenAlex.
- Omics advancements towards exploring arsenic toxicity and tolerance in plants: a review.Planta · 2025Review
- Review
- Synchrotron micro-X-ray fluorescence imaging of arsenic in frozen-hydrated sections of a root of Pteris vittata.Metallomics : integrated biometal science · 2021Article
- Arsenic redox transformations and cycling in the rhizosphere ofEnvironmental and experimental botany · 2020Article
- A review on global metal accumulators-mechanism, enhancement, commercial application, and research trend.Environmental science and pollution research international · 2019Review
- Speciation and uptake of antimony and arsenic by two populations of Pteris vittata L. and Holcus lanatus L. from co-contaminated soil.Environmental science and pollution research international · 2018Article
- The first complete chloroplast genome ofMitochondrial DNA. Part B, Resources · 2018Article
- An Endophytic Bacterial Consortium modulates multiple strategies to improve Arsenic Phytoremediation Efficacy in Solanum nigrum.Scientific reports · 2018Article
- Root transcripts associated with arsenic accumulation in hyperaccumulator Pteris vittata.Journal of biosciences · 2018Article
- Evidence for exocellular Arsenic in Fronds of Pteris vittata.Scientific reports · 2017Article
- Isolation and identification of flavonoids components fromSpringerPlus · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymatic reduction of arsenate to arsenite is the first known step in arsenate metabolism in all organisms. Although the presence of one mRNA arsenate reductase (PvACR2) has been characterized in gametophytes of P. vittata, no arsenate reductase protein has been directly observed in this arsenic hyperaccumulating fern, yet. In order to assess the possible presence of arsenate reductase in P. vittata, two recombinant proteins, ACR2-His6 and Trx-His6-S-Pv2.5-8 were prepared in Escherichia coli, purified and used to produce polyclonal antibodies. The presence of these two enzymes was evaluated by qRT-PCR, immunoblotting and direct MS analysis. Enzymatic activity was detected in crude extracts. For the first time we detected and identified two arsenate reductase proteins (PvACR2 and Pv2.5-8) in sporophytes and gametophytes of P. vittata. Despite an increase of the mRNA levels for both proteins in roots, no difference was observed at the protein level after arsenic treatment. Overall, our data demonstrate the constitutive protein expression of PvACR2 and Pv2.5-8 in P. vittata tissues and propose their specific role in the complex metabolic network of arsenic reduction.
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