Evidence map›Paper›PMID 16328785›Full record

ReviewPhotosynthesis research2005

The role of 5'-adenylylsulfate reductase in controlling sulfate reduction in plants.

Melinda N Martin, Mitchell C Tarczynski, Bo Shen, Thomas Leustek

Abstract readReview
PubMed Publisher
In one paragraph

Review in Photosynthesis research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

35 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Co-overexpression ofFrontiers in plant science · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Redox and Thiols in Archaea.Antioxidants (Basel, Switzerland) · 2020
    Review
  9. Article
  10. C-terminal Redox Domain ofAntioxidants (Basel, Switzerland) · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Engineering sulfur storage in maize seed proteins without apparent yield loss.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 2 institutions in 1 country.

Melinda N MartinDepartment of Plant Biology and Pathology, Biotechnology Center for Agriculture and the Environment, Rutgers University, New Brunswick, NJ 08901-8520, USA.
Mitchell C Tarczynski
Bo Shen
Thomas Leustek
DuPont (United States) · USRutgers, The State University of New Jersey · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cysteine is the first organic product of sulfate assimilation and as such is the precursor of all molecules containing reduced sulfur including methionine, glutathione, and their many metabolites. In plants, 5'-adenylylsulfate (APS) reductase is hypothesized to be a key regulatory point in sulfate assimilation and reduction. APS reductase catalyzes the two-electron reduction of APS to sulfite using glutathione as an electron donor. This paper reviews the experimental basis for this hypothesis. In addition, the results of an experiment designed to test the hypothesis by bypassing the endogenous APS reductase and its regulatory mechanisms are described. Two different bacterial assimilatory reductases were expressed in transgenic Zea mays, the thioredoxin-dependent APS reductase from Pseudomonas aeruginosa and the thioredoxin-dependent 3'-phosphoadenylylsulfate reductase from Escherichia coli. Each of them was placed under transcriptional control of the ubiquitin promoter and the protein products were targeted to chloroplasts. The leaves of transgenic Z. mays lines showed significant accumulation of reduced organic thiol compounds including cysteine, gamma-glutamylcysteine, and glutathione; and reduced inorganic forms of sulfur including sulfite and thiosulfate. Both bacterial enzymes appeared to be equally capable of deregulating the assimilative sulfate reduction pathway. The reduced sulfur compounds accumulated to such high levels that the transgenic plants showed evidence of toxicity. The results provide additional evidence that APS reductase is a major control point for sulfate reduction in Z. mays.

Indexed as

AnimalsGene Expression Regulation, EnzymologicGene Expression Regulation, PlantOxidation-ReductionOxidoreductases Acting on Sulfur Group DonorsPlant DevelopmentPlantsSulfatesadenylylsulfate reductaseOxidoreductases Acting on Sulfur Group DonorsSulfates

Identifiers

PMID16328785
OpenAlexW2079756048

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.