Evidence map›Paper›PMID 23818601›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

A thioredoxin-like/β-propeller protein maintains the efficiency of light harvesting in Arabidopsis.

Matthew D Brooks, Emily J Sylak-Glassman, Graham R Fleming, Krishna K Niyogi

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

54 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The cell biology and genome ofMolecular biology of the cell · 2025
    Article
  6. Article
  7. Article
  8. Identification of PsbS binding proteins inFrontiers in plant science · 2025
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. STN7 is not essential for developmental acclimation of Arabidopsis to light intensity.The Plant journal : for cell and molecular biology · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Oxidative regulation of chloroplast enzymes by thioredoxin and thioredoxin-like proteins inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  20. Review
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.

Matthew D BrooksDepartment of Plant and Microbial Biology, Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA.
Emily J Sylak-Glassman
Graham R Fleming
Krishna K Niyogi
Lawrence Berkeley National Laboratory · USHoward Hughes Medical Institute · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

The light-harvesting complexes of plants have evolved the ability to switch between efficient light harvesting and quenching forms to optimize photosynthesis in response to the environment. Several distinct mechanisms, collectively termed "nonphotochemical quenching" (NPQ), provide flexibility in this response. Here we report the isolation and characterization of a mutant, suppressor of quenching 1 (soq1), that has high NPQ even in the absence of photosystem II subunit S (PsbS), a protein that is necessary for the rapidly reversible component of NPQ. The formation of NPQ in soq1 was light intensity-dependent, and it exhibited slow relaxation kinetics and other characteristics that distinguish it from known NPQ components. Treatment with chemical inhibitors or an uncoupler, as well as crosses to mutants known to affect other NPQ components, showed that the NPQ in soq1 does not require a transthylakoid pH gradient, zeaxanthin formation, or the phosphorylation of light-harvesting complexes, and it appears to be unrelated to the photosystem II damage-and-repair cycle. Measurements of pigments and chlorophyll fluorescence lifetimes indicated that the additional NPQ in soq1 is the result of a decrease in chlorophyll excited-state lifetime and not pigment bleaching. The SOQ1 gene was isolated by map-based cloning, and it encodes a previously uncharacterized thylakoid membrane protein with thioredoxin-like and β-propeller domains located in the lumen and a haloacid-dehalogenase domain exposed to the chloroplast stroma. We propose that the role of SOQ1 is to prevent formation of a slowly reversible form of antenna quenching, thereby maintaining the efficiency of light harvesting.

Indexed as

ArabidopsisArabidopsis ProteinsCrosses, GeneticFluorescenceImmunoblottingLight-Harvesting Protein ComplexesModels, BiologicalThioredoxinsThylakoid Membrane ProteinsArabidopsis ProteinsLight-Harvesting Protein Complexessuppressor of quenching 1 protein, ArabidopsisThioredoxinsThylakoid Membrane Proteins

Identifiers

PMID23818601
PMCPMC3718131
OpenAlexW2064616580

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.