Evidence map›Paper›PMID 25331882›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Compartmentalization of the protein repair machinery in photosynthetic membranes.

Sujith Puthiyaveetil, Onie Tsabari, Troy Lowry, Steven Lenhert, Robert R Lewis, Ziv Reich, Helmut Kirchhoff

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.6field-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

52 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Defining the heterogeneous composition of Arabidopsis thylakoid membrane.The Plant journal : for cell and molecular biology · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Protein assemblies in theFrontiers in plant science · 2024
    Article
  18. Article
  19. Structure ofeLife · 2023
    Article
  20. 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

7 authors at 3 institutions in 2 countries.

Sujith PuthiyaveetilInstitute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340;
Onie TsabariDepartment of Biological Chemistry, Weizmann Institute of Science, 76100 Rehovot, Israel;
Troy LowryDepartment of Biological Science, Florida State University, Tallahassee, FL 32306-4370; and.
Steven LenhertDepartment of Biological Science, Florida State University, Tallahassee, FL 32306-4370; and.
Robert R LewisSchool of Electrical Engineering and Computer Science, Washington State University, Richland, WA 99354.
Ziv ReichDepartment of Biological Chemistry, Weizmann Institute of Science, 76100 Rehovot, Israel;
Helmut KirchhoffInstitute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340; kirchhh@wsu.edu.
Washington State University · USFlorida State University · USWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A crucial component of protein homeostasis in cells is the repair of damaged proteins. The repair of oxygen-evolving photosystem II (PS II) supercomplexes in plant chloroplasts is a prime example of a very efficient repair process that evolved in response to the high vulnerability of PS II to photooxidative damage, exacerbated by high-light (HL) stress. Significant progress in recent years has unraveled individual components and steps that constitute the PS II repair machinery, which is embedded in the thylakoid membrane system inside chloroplasts. However, an open question is how a certain order of these repair steps is established and how unwanted back-reactions that jeopardize the repair efficiency are avoided. Here, we report that spatial separation of key enzymes involved in PS II repair is realized by subcompartmentalization of the thylakoid membrane, accomplished by the formation of stacked grana membranes. The spatial segregation of kinases, phosphatases, proteases, and ribosomes ensures a certain order of events with minimal mutual interference. The margins of the grana turn out to be the site of protein degradation, well separated from active PS II in grana core and de novo protein synthesis in unstacked stroma lamellae. Furthermore, HL induces a partial conversion of stacked grana core to grana margin, which leads to a controlled access of proteases to PS II. Our study suggests that the origin of grana in evolution ensures high repair efficiency, which is essential for PS II homeostasis.

Indexed as

Evolution, MolecularProteolysisArabidopsisPhotosystem II Protein ComplexThylakoidsPhotosystem II Protein Complexgrana marginphotoinhibitionphotosynthesisPS II repair cyclethylakoid membrane

Identifiers

PMID25331882
PMCPMC4226077
OpenAlexW2103018690

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.