Evidence map›Paper›PMID 15356344›Full record

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

Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen.

Gayathri Gopalan, Zengyong He, Yves Balmer, Patrick Romano, Rajeev Gupta, Annie Héroux, Bob B Buchanan, Kunchithapadam Swaminathan, Sheng Luan

Open access · greenAbstract 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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.2field-weighted citation impact, top 8% 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, 101 citations in OpenAlex.

  1. Classification of Protein Disulfide Bonds.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  2. Structural features of chloroplast trigger factor determined at 2.6 Å resolution.Acta crystallographica. Section D, Structural biology · 2022
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Chloroplast immunophilins.Protoplasma · 2016
    Review
  10. Article
  11. Article
  12. Thioredoxin-dependent regulatory networks in chloroplasts under fluctuating light conditions.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014
    Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
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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

9 authors at 3 institutions in 2 countries.

Gayathri GopalanDepartment of Biological Sciences, National University of Singapore, Singapore 119260.
Zengyong He
Yves Balmer
Patrick Romano
Rajeev Gupta
Annie Héroux
Bob B Buchanan
Kunchithapadam Swaminathan
Sheng Luan
University of California, Berkeley · USBrookhaven National Laboratory · USInstitute of Molecular and Cell Biology · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Change in redox status has long been known to link light to the posttranslational regulation of chloroplast enzymes. So far, studies have been conducted primarily with thioredoxin-linked members of the stroma that function in a broad array of biosynthetic and degradatory processes. Consequently, little is known about the role of redox in regulating the growing number of enzymes found to occur in the lumen, the site of oxygen evolution in thylakoid membranes. To help fill this gap, we have studied AtFKBP13, an FKBP-type immunophilin earlier shown to interact with a redox-active protein of the lumen, and found the enzyme to contain a pair of disulfide bonds in x-ray structural studies. These disulfides, which in protein mutagenesis experiments were shown to be essential for the associated peptidyl-prolyl isomerase activity, are unique to chloroplast FKBPs and are absent in animal and yeast counterparts. Both disulfide bonds were redox-active and were reduced by thioredoxin from either chloroplast or bacterial sources in a reaction that led to loss of enzyme activity. The results suggest a previously unrecognized paradigm for redox regulation in chloroplasts in which activation by light is achieved in concert with oxygen evolution by the oxidation of sulfhydryl groups (conversion of SH to S-S). Such a mechanism, occurring in the thylakoid lumen, is in direct contrast to regulation of enzymes in the stroma, where reduction of disulfides targeted by thioredoxin (S-S converted to SH) leads to an increase in activity in the light.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsChloroplastsCloning, MolecularCrystallography, X-RayDisulfidesEscherichia coliModels, MolecularNADPOxidation-ReductionPlant ProteinsProtein ConformationRecombinant ProteinsTacrolimusTacrolimus Binding ProteinsArabidopsis ProteinsDisulfidesFKBP-13NADPPlant ProteinsRecombinant ProteinsTacrolimusTacrolimus Binding ProteinsThioredoxins

Identifiers

PMID15356344
PMCPMC518858
OpenAlexW1984294720

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.