ArticlePlant physiology2008
Functional characterization of an unusual phytochelatin synthase, LjPCS3, of Lotus japonicus.
Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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.
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.
Who cites it
11 citing papers in PubMed, 40 citations in OpenAlex.
- Ancient duplication and functional differentiation of phytochelatin synthases is conserved in plant genomes.Horticulture research · 2025Article
- Heterologous Expression of the Phytochelatin SynthaseInternational journal of environmental research and public health · 2022Article
- Ancestral function of the phytochelatin synthase C-terminal domain in inhibition of heavy metal-mediated enzyme overactivation.Journal of experimental botany · 2020Article
- Evolution and functional differentiation of recently diverged phytochelatin synthase genes from Arundo donax L.Journal of experimental botany · 2019Article
- Differences of Cd uptake and expression of OAS and IRT genes in two varieties of ryegrasses.Environmental science and pollution research international · 2019Article
- Identification of alternatively spliced transcripts of rice phytochelatin synthase 2 gene OsPCS2 involved in mitigation of cadmium and arsenic stresses.Plant molecular biology · 2017Article
- Transcriptome Profiling of Louisiana iris Root and Identification of Genes Involved in Lead-Stress Response.International journal of molecular sciences · 2015Article
- Arsenite elicits anomalous sulfur starvation responses in barley.Plant physiology · 2013Article
- Effect of magnetic nanoparticles on tobacco BY-2 cell suspension culture.International journal of environmental research and public health · 2012Article
- Characterization of the phytochelatin synthase of Schistosoma mansoni.PLoS neglected tropical diseases · 2011Article
- Characterization of the Sesbania rostrata phytochelatin synthase gene: alternative splicing and function of four isoforms.International journal of molecular sciences · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In plants and many other organisms, phytochelatin synthase (PCS) catalyzes the synthesis of phytochelatins from glutathione in the presence of certain metals and metalloids. We have used budding yeast (Saccharomyces cerevisiae) as a heterologous system to characterize two PCS proteins, LjPCS1 and LjPCS3, of the model legume Lotus japonicus. Initial experiments revealed that the metal tolerance of yeast cells in vivo depends on the concentrations of divalent cations in the growth medium. Detailed in vivo (intact cells) and in vitro (broken cells) assays of PCS activity were performed with yeast expressing the plant enzymes, and values of phytochelatin production for each metal tested were normalized with respect to those of cadmium to correct for the lower expression level of LjPCS3. Our results showed that lead was the best activator of LjPCS1 in the in vitro assay, whereas, for both assays, arsenic, iron, and aluminum were better activators of LjPCS3 and mercury was similarly active with the two enzymes. Most interestingly, zinc was a powerful activator, especially of LjPCS3, when assayed in vivo, whereas copper and silver were the strongest activators in the in vitro assay. We conclude that the in vivo and in vitro assays are useful and complementary to assess the response of LjPCS1 and LjPCS3 to a wide range of metals and that the differences in the C-terminal domains of the two proteins are responsible for their distinct expression levels or stabilities in heterologous systems and patterns of metal activation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.