Evidence map›Paper›PMID 22209765›Full record

ArticleThe Plant cell2011

Lumen Thiol Oxidoreductase1, a disulfide bond-forming catalyst, is required for the assembly of photosystem II in Arabidopsis.

Mohamed Karamoko, Sara Cline, Kevin Redding, Natividad Ruiz, Patrice P Hamel

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

47 citing papers in PubMed, 95 citations in OpenAlex.

  1. Giant viruses encode vitamin K-based redox modules for lipid modification.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Review
  4. On the non-oxygenic origins of thylakoids.Communications biology · 2025
    Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. The Cryptic Plastid ofmSphere · 2020
    Article
  20. Photosynthetic characterization of transgenicPlant signaling & behavior · 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

5 authors at 2 institutions in 1 country.

Mohamed KaramokoDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210, USA.
Sara Cline
Kevin Redding
Natividad Ruiz
Patrice P Hamel
The Ohio State University · USArizona State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here, we identify Arabidopsis thaliana Lumen Thiol Oxidoreductase1 (LTO1) as a disulfide bond-forming enzyme in the thylakoid lumen. Using topological reporters in bacteria, we deduced a lumenal location for the redox active domains of the protein. LTO1 can partially substitute for the proteins catalyzing disulfide bond formation in the bacterial periplasm, which is topologically equivalent to the plastid lumen. An insertional mutation within the LTO1 promoter is associated with a severe photoautotrophic growth defect. Measurements of the photosynthetic activity indicate that the lto1 mutant displays a limitation in the electron flow from photosystem II (PSII). In accordance with these measurements, we noted a severe depletion of the structural subunits of PSII but no change in the accumulation of the cytochrome b(6)f complex or photosystem I. In a yeast two-hybrid assay, the thioredoxin-like domain of LTO1 interacts with PsbO, a lumenal PSII subunit known to be disulfide bonded, and a recombinant form of the molecule can introduce a disulfide bond in PsbO in vitro. The documentation of a sulfhydryl-oxidizing activity in the thylakoid lumen further underscores the importance of catalyzed thiol-disulfide chemistry for the biogenesis of the thylakoid compartment.

Indexed as

ArabidopsisArabidopsis ProteinsBacterial ProteinsBase SequenceCloning, MolecularCytochromes fDisulfidesDNA, PlantEnzyme ActivationEscherichia coliGenetic Complementation TestGenetic VectorsMolecular Sequence DataOxidation-ReductionPhotosynthesisPhotosystem II Protein ComplexArabidopsis ProteinsBacterial ProteinsCytochromes fDisulfidesDNA, Plantlumen thiol oxidoreductase 1, Arabidopsisphotosystem II manganese-stabilizing proteinPhotosystem II Protein ComplexThylakoid Membrane ProteinsVitamin K Epoxide Reductases

Identifiers

PMID22209765
PMCPMC3269877
OpenAlexW2171732491

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.