Evidence map›Paper›PMID 32936292›Full record

ArticleJournal of experimental botany2020

Ancestral function of the phytochelatin synthase C-terminal domain in inhibition of heavy metal-mediated enzyme overactivation.

Mingai Li, Enrico Barbaro, Erika Bellini, Alessandro Saba, Luigi Sanità di Toppi, Claudio Varotto

Open access · bronzeAbstract read
In one paragraph

Article in Journal of experimental botany, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 35 citations in OpenAlex.

  1. Silicon-mediated alleviation of mercury toxicity requires coordinated regulation of antioxidant defense, metal homeostasis, and nodule function in mung bean.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
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  8. A synthetic biology approach for the treatment of pollutants with microalgae.Frontiers in bioengineering and biotechnology · 2024
    Review
  9. A Novel Isoprene Synthase from the Monocot TreeInternational journal of molecular sciences · 2023
    Article
  10. Review
  11. Phytochelatins: Sulfur-Containing Metal(loid)-Chelating Ligands in Plants.International journal of molecular sciences · 2023
    Review
  12. Heterologous Expression of the Phytochelatin SynthaseInternational journal of environmental research and public health · 2022
    Article
  13. Review
  14. Article
  15. Review
  16. Overexpression ofFrontiers in plant science · 2021
    Article
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 2 institutions in 1 country.

Mingai LiDepartment of Biodiversity and Molecular Ecology, Research and Innovation Centre, Fondazione Edmund Mach, San Michele all'Adige, Trento, Italy.
Enrico BarbaroDepartment of Biodiversity and Molecular Ecology, Research and Innovation Centre, Fondazione Edmund Mach, San Michele all'Adige, Trento, Italy.
Erika BelliniDipartimento di Biologia, Università di Pisa, Pisa, Italy.
Alessandro SabaDipartimento di Patologia Chirurgica, Medica, Molecolare e dell'Area Critica, Università di Pisa, Pisa, Italy.
Luigi Sanità di ToppiDipartimento di Biologia, Università di Pisa, Pisa, Italy.
Claudio VarottoDepartment of Biodiversity and Molecular Ecology, Research and Innovation Centre, Fondazione Edmund Mach, San Michele all'Adige, Trento, Italy.
Fondazione Edmund Mach · ITUniversity of Pisa · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phytochelatin synthases (PCSs) play essential roles in detoxification of a broad range of heavy metals in plants and other organisms. Until now, however, no PCS gene from liverworts, the earliest branch of land plants and possibly the first one to acquire a PCS with a C-terminal domain, has been characterized. In this study, we isolated and functionally characterized the first PCS gene from a liverwort, Marchantia polymorpha (MpPCS). MpPCS is constitutively expressed in all organs examined, with stronger expression in thallus midrib. The gene expression is repressed by Cd2+ and Zn2+. The ability of MpPCS to increase heavy metal resistance in yeast and to complement cad1-3 (the null mutant of the Arabidopsis ortholog AtPCS1) proves its function as the only PCS from M. polymorpha. Site-directed mutagenesis of the most conserved cysteines of the C-terminus of the enzyme further uncovered that two twin-cysteine motifs repress, to different extents, enzyme activation by heavy metal exposure. These results highlight an ancestral function of the PCS elusive C-terminus as a regulatory domain inhibiting enzyme overactivation by essential and non-essential heavy metals. The latter finding may be relevant for obtaining crops with decreased root to shoot mobility of cadmium, thus preventing its accumulation in the food chain.

Indexed as

AminoacyltransferasesArabidopsisArabidopsis ProteinsCadmiumPhytochelatinsAminoacyltransferasesArabidopsis ProteinsCadmiumglutathione gamma-glutamylcysteinyltransferasePhytochelatinsCadmiumC-terminal domainMarchantia polymorphaoveractivationphytochelatinphytochelatin synthasesite-directed mutagenesistwin-cysteine motifzinc

Identifiers

PMID32936292
PMCPMC7586750
OpenAlexW3087599935

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.