Evidence map›Paper›PMID 19520850›Full record

ArticleThe Journal of biological chemistry2009

Selective binding of glutathione conjugates of fatty acid derivatives by plant glutathione transferases.

David P Dixon, Robert Edwards

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

48 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Overlooked and misunderstood: can glutathione conjugates be clues to understanding plant glutathione transferases?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  6. Review
  7. ΔiScience · 2024
    Article
  8. Article
  9. Article
  10. Proteomic Analysis of Proteins Related to Defense Responses inInternational journal of molecular sciences · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Is there a role for tau glutathione transferases in tetrapyrrole metabolism and retrograde signalling in plants?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Article
  20. Photosynthetic signalling during high light stress and recovery: targets and dynamics.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    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

2 authors at 1 institution in 1 country.

David P DixonCentre for Bioactive Chemistry, School of Biological and Biomedical Sciences, Durham University, South Road, Durham DH1 3LE, United Kingdom.
Robert Edwards
Durham University · GB

Funding

Biotechnology and Biological Sciences Research Council BBC51227X1Biotechnology and Biological Sciences Research Council BB/G001766/1
6 · The paper itself

Abstract

Proteomic studies with Arabidopsis thaliana have revealed that the plant-specific Tau (U) class glutathione transferases (GSTs) are selectively retained by S-hexylglutathione affinity supports. Overexpression of members of the Arabidopsis GST superfamily in Escherichia coli showed that 25 of the complement of 28 GSTUs caused the aberrant accumulation of acylated glutathione thioesters in vivo, a perturbation that was not observed with other GST classes. Each GSTU caused a specific group of fatty acyl derivatives to accumulate, which varied in chain length (C(6) to C(18)), additional oxygen content (0 or 1), and desaturation (0 or 1). Thioesters bound tightly to recombinant GSTs (K(d) approximately 1 microm), explaining their accumulation. Transient expression of GSTUs in Nicotiana benthamiana followed by recovery by Strep-tag affinity chromatography allowed the respective plant ligands to be extracted and characterized. Again, each GST showed a distinct profile of recovered metabolites, notably glutathionylated oxophytodienoic acid and related oxygenated fatty acids. Similarly, the expression of the major Tau protein GSTU19 in the endogenous host Arabidopsis led to the selective binding of the glutathionylated oxophytodienoic acid-glutathione conjugate, with the enzyme able to catalyze the conjugation reaction. Additional ligands identified in planta included other fatty acid derivatives including divinyl ethers and glutathionylated chlorogenic acid. The strong and specific retention of various oxygenated fatty acids by each GSTU and the conservation in binding observed in the different hosts suggest that these proteins have selective roles in binding and conjugating these unstable metabolites in vivo.

Indexed as

ArabidopsisChlorogenic AcidChromatography, AffinityElectrophoresis, Gel, Two-DimensionalFatty AcidsGlutathioneGlutathione TransferaseKineticsLigandsModels, BiologicalNicotianaOxygenPlantsProtein BindingProteomicsChlorogenic AcidFatty AcidsGlutathioneGlutathione TransferaseLigandsOxygen

Identifiers

PMID19520850
PMCPMC2755848
OpenAlexW2005266375

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.