Evidence map›Paper›PMID 16766666›Full record

ArticlePlant physiology2006

A novel arsenate reductase from the arsenic hyperaccumulating fern Pteris vittata.

Danielle R Ellis, Luke Gumaelius, Emily Indriolo, Ingrid J Pickering, Jo Ann Banks, David E Salt

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
10.4field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

55 citing papers in PubMed, 225 citations in OpenAlex.

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  4. Frontiers in plant science · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 2 countries.

Danielle R EllisDepartment of Botany and Plant Pathology , Purdue University, West Lafayette, Indiana 47907, USA.
Luke Gumaelius
Emily Indriolo
Ingrid J Pickering
Jo Ann Banks
David E Salt
Purdue University West Lafayette · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pteris vittata sporophytes hyperaccumulate arsenic to 1% to 2% of their dry weight. Like the sporophyte, the gametophyte was found to reduce arsenate [As(V)] to arsenite [As(III)] and store arsenic as free As(III). Here, we report the isolation of an arsenate reductase gene (PvACR2) from gametophytes that can suppress the arsenate sensitivity and arsenic hyperaccumulation phenotypes of yeast (Saccharomyces cerevisiae) lacking the arsenate reductase gene ScACR2. Recombinant PvACR2 protein has in vitro arsenate reductase activity similar to ScACR2. While PvACR2 and ScACR2 have sequence similarities to the CDC25 protein tyrosine phosphatases, they lack phosphatase activity. In contrast, Arath;CDC25, an Arabidopsis (Arabidopsis thaliana) homolog of PvACR2 was found to have both arsenate reductase and phosphatase activities. To our knowledge, PvACR2 is the first reported plant arsenate reductase that lacks phosphatase activity. CDC25 protein tyrosine phosphatases and arsenate reductases have a conserved HCX5R motif that defines the active site. PvACR2 is unique in that the arginine of this motif, previously shown to be essential for phosphatase and reductase activity, is replaced with a serine. Steady-state levels of PvACR2 expression in gametophytes were found to be similar in the absence and presence of arsenate, while total arsenate reductase activity in P. vittata gametophytes was found to be constitutive and unaffected by arsenate, consistent with other known metal hyperaccumulation mechanisms in plants. The unusual active site of PvACR2 and the arsenate reductase activities of cell-free extracts correlate with the ability of P. vittata to hyperaccumulate arsenite, suggesting that PvACR2 may play an important role in this process.

Indexed as

Amino Acid MotifsAmino Acid SequenceArabidopsis ProteinsArsenate ReductasesArsenatesArsenicArsenite Transporting ATPasescdc25 PhosphatasesCloning, MolecularGene DeletionGenetic Complementation TestIon PumpsMolecular Sequence DataMultienzyme ComplexesPhenotypePhylogenyArabidopsis ProteinsARR2 protein, S cerevisiaeArsenate ReductasesArsenatesArsenicarsenic acidArsenite Transporting ATPasescdc25 PhosphatasesIon PumpsMultienzyme ComplexesPlant ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID16766666
PMCPMC1533930
OpenAlexW2126078589

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.