Evidence map›Paper›PMID 14769934›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Identification of plastid envelope proteins required for import of protochlorophyllide oxidoreductase A into the chloroplast of barley.

Steffen Reinbothe, Françoise Quigley, John Gray, Andreas Schemenewitz, Christiane Reinbothe

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

  1. Review
  2. Article
  3. A Protochlorophyllide (Pchlide)Frontiers in plant science · 2019
    Article
  4. Roles and maturation of iron-sulfur proteins in plastids.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Three proteins mediate import of transit sequence-less precursors into the inner envelope of chloroplasts in Arabidopsis thaliana.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  11. Review
  12. Article
  13. A search for factors influencing etioplast-chloroplast transition.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  14. Article
  15. Article
  16. Review
  17. Three thioredoxin targets in the inner envelope membrane of chloroplasts function in protein import and chlorophyll metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  18. A substrate-independent, 14:3:3 protein-mediated plastid import pathway of NADPH:protochlorophyllide oxidoreductase A.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  19. Review
  20. A plant porphyria related to defects in plastid import of protochlorophyllide oxidoreductase A.Proceedings of the National Academy of Sciences of the United States of America · 2007
    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

5 authors.

Steffen ReinbotheUniversité Joseph Fourier et Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5575, BP53, F-38041 Grenoble Cedex 9, France. steffen.reinbothe@ujf-grenoble.fr
Françoise Quigley
John Gray
Andreas Schemenewitz
Christiane Reinbothe

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chloroplasts synthesize an abundance of different tetrapyrrole compounds. Among them are chlorophyll and its precursor protochlorophyllide (Pchlide), which accumulate in light- and dark-grown plants, respectively. Pchlide is converted to chlorophyllide by virtue of the NADPH:Pchlide oxidoreductase (POR), which, in angiosperms, is the only known light-dependent enzyme of the chlorophyll biosynthetic pathway. In etiolated barley plants, two closely related POR proteins exist termed PORA and PORB, which are nuclear gene products. Here we identified plastid envelope proteins that interact with the cytosolic PORA precursor (pPORA) during its posttranslational chloroplast import. We demonstrate that pPORA interacts with several previously unreported components. Among them is a Pchlide a oxygenase, which provides Pchlide b as import substrate for pPORA, and a tyrosine aminotransferase thought to be involved in the synthesis of photoprotective vitamin E. Two other constituents were found to be orthologs of the GTP-binding proteins Toc33/34 and of the outer plastid envelope protein Oep16.

Indexed as

Amino Acid SequenceChloroplastsHordeumIntracellular MembranesMacromolecular SubstancesMembrane Transport ProteinsMolecular Sequence DataOxidoreductases Acting on CH-CH Group DonorsOxygenasesPhotochemistryPlant ProteinsPlastidsProtein BindingProtein TransportProtochlorophyllideTocopherolsMacromolecular SubstancesMembrane Transport ProteinsOxidoreductases Acting on CH-CH Group DonorsOxygenasesPlant ProteinsProtochlorophyllideprotochlorophyllide reductaseTocopherolsTyrosine Transaminase

Identifiers

PMID14769934
PMCPMC380236

What OpenQuestion holds

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Registered trials

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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.