Evidence map›Paper›PMID 8642611›Full record

ArticleJournal of molecular evolution1996

Intron position as an evolutionary marker of thioredoxins and thioredoxin domains.

M Sahrawy, V Hecht, J Lopez-Jaramillo, A Chueca, Y Chartier, Y Meyer

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Journal of molecular evolution, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Thioredoxins in Arabidopsis and other plants.Photosynthesis research · 2005
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Identification and characterization of a mitochondrial thioredoxin system in plants.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  18. Evolutionary relationships among self-incompatibility RNases.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  19. Article
  20. Nuclear-encoded proteins target to the plastid in Toxoplasma gondii and Plasmodium falciparum.Proceedings of the National Academy of Sciences of the United States of America · 1998
    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 2 countries.

M SahrawyDepartment of Plant Biochemistry, Consejo Superior de Investigaciones, Granada, Spain.
V Hecht
J Lopez-Jaramillo
A Chueca
Y Chartier
Y Meyer
Université de Perpignan · FREstación Experimental del Zaidín · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In contrast to prokaryotes, which typically possess one thioredoxin gene per genome, three different thioredoxin types have been described in higher plants. All are encoded by nuclear genes, but thioredoxins m and f are chloroplastic while thioredoxins h have no transit peptide and are probably cytoplasmic. We have cloned and sequenced Arabidopsis thaliana genomic fragments encoding the five previously described thioredoxins h, as well as a sixth gene encoding a new thioredoxin h. In spite of the high divergence of the sequences, five of them possess two introns at positions identical to the previously sequenced tobacco thioredoxin h gene, while a single one has only the first intron. The recently published sequence of Chlamydomonas thioredoxin h shows three introns, two at the same positions as in higher plants. This strongly suggests a common origin for all cytoplasmic thioredoxins of plants and green algae. In addition, we have cloned and sequenced pea DNA genomic fragments encoding thioredoxins m and f. The thioredoxin m sequence shows only one intron between the regions encoding the transit peptide and the mature protein, supporting the prokaryotic origin of this sequence and suggesting that its association with the transit peptide has been facilitated by exon shuffling. In contrast, the thioredoxin f sequence shows two introns, one at the same position as an intron in various plant and animal thioredoxins and the second at the same position as an intron in thioredoxin domains of disulfide isomerases. This strongly supports the hypothesis of a eukaryotic origin for chloroplastic thioredoxin f.

Indexed as

Biological EvolutionAmino Acid SequenceArabidopsisBase SequenceChloroplast ThioredoxinsGenetic MarkersGenome, PlantIntronsIsomerasesMolecular Sequence DataPisum sativumPlantsProtein Disulfide-IsomerasesSequence Homology, Amino AcidThioredoxinsChloroplast ThioredoxinsGenetic MarkersIsomerasesProtein Disulfide-IsomerasesThioredoxins

Identifiers

PMID8642611
OpenAlexW2064911759

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.