Evidence map›Paper›PMID 16489135›Full record

ArticlePlant physiology2006

A reassessment of substrate specificity and activation of phytochelatin synthases from model plants by physiologically relevant metals.

Jorge Loscos, Loreto Naya, Javier Ramos, Maria R Clemente, Manuel A Matamoros, Manuel Becana

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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Phytochelatins: Sulfur-Containing Metal(loid)-Chelating Ligands in Plants.International journal of molecular sciences · 2023
    Review
  5. Article
  6. Article
  7. Heterologous Expression of the Phytochelatin SynthaseInternational journal of environmental research and public health · 2022
    Article
  8. Article
  9. Review
  10. Article
  11. Effect of magnetic nanoparticles on tobacco BY-2 cell suspension culture.International journal of environmental research and public health · 2012
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. 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.

Jorge LoscosDepartamento de Nutrición Vegetal, Estación Experimental de Aula Dei, Consejo Superior de Investigaciones Científicas, 50080 Zaragoza, Spain.
Loreto Naya
Javier Ramos
Maria R Clemente
Manuel A Matamoros
Manuel Becana
Consejo Superior de Investigaciones Científicas · ESEstación Experimental de Aula Dei · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phytochelatin synthases (PCS) catalyze phytochelatin (PC) synthesis from glutathione (GSH) in the presence of certain metals. The resulting PC-metal complexes are transported into the vacuole, avoiding toxic effects on metabolism. Legumes have the unique capacity to partially or completely replace GSH by homoglutathione (hGSH) and PCs by homophytochelatins (hPCs). However, the synthesis of hPCs has received little attention. A search for PCS genes in the model legume Lotus (Lotus japonicus) resulted in the isolation of a cDNA clone encoding a protein (LjPCS1) highly homologous to a previously reported homophytochelatin synthase (hPCS) of Glycine max (GmhPCS1). Recombinant LjPCS1 and Arabidopsis (Arabidopsis thaliana) PCS1 (AtPCS1) were affinity purified and their polyhistidine-tags removed. AtPCS1 catalyzed hPC synthesis from hGSH alone at even higher rates than did LjPCS1, indicating that GmhPCS1 is not a genuine hPCS and that a low ratio of hPC to PC synthesis is an inherent feature of PCS1 enzymes. For both enzymes, hGSH is a good acceptor, but a poor donor, of gamma-glutamylcysteine units. Purified AtPCS1 and LjPCS1 were activated (in decreasing order) by Cd2+, Zn2+, Cu2+, and Fe3+, but not by Co2+ or Ni2+, in the presence of 5 mm GSH and 50 microm metal ions. Activation of both enzymes by Fe3+ was proven by the complete inhibition of PC synthesis by the iron-specific chelator desferrioxamine. Plants of Arabidopsis and Lotus accumulated (h)PCs only in response to a large excess of Cu2+ and Zn2+, but to a much lower extent than did with Cd2+, indicating that (h)PC synthesis does not significantly contribute in vivo to copper, zinc, and iron detoxification.

Indexed as

AminoacyltransferasesArabidopsisArabidopsis ProteinsEnzyme ActivationGlycine maxLotusMetals, HeavyPhylogenyPlant ProteinsRecombinant ProteinsSequence Analysis, ProteinSubstrate SpecificityAminoacyltransferasesArabidopsis ProteinsAT5G44070 protein, Arabidopsisglutathione gamma-glutamylcysteinyltransferaseMetals, HeavyPlant ProteinsRecombinant Proteins

Identifiers

PMID16489135
PMCPMC1435825
OpenAlexW2156608307

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.