Evidence map›Paper›PMID 24151298›Full record

ArticleThe Plant cell2013

Cell growth defect factor1/chaperone-like protein of POR1 plays a role in stabilization of light-dependent protochlorophyllide oxidoreductase in Nicotiana benthamiana and Arabidopsis.

Jae-Yong Lee, Ho-Seok Lee, Ji-Young Song, Young Jun Jung, Steffen Reinbothe, Youn-Il Park, Sang Yeol Lee, Hyun-Sook Pai

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

26 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Light dependent protochlorophyllide oxidoreductase: a succinct look.Physiology and molecular biology of plants : an international journal of functional plant biology · 2024
    Review
  5. Article
  6. Article
  7. microPublication biology · 2023
    Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. A Protochlorophyllide (Pchlide)Frontiers in plant science · 2019
    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

8 authors at 4 institutions in 2 countries.

Jae-Yong LeeDepartment of Systems Biology, Yonsei University, Seoul 120-749, Korea.
Ho-Seok Lee
Ji-Young Song
Young Jun Jung
Steffen Reinbothe
Youn-Il Park
Sang Yeol Lee
Hyun-Sook Pai
Yonsei University · KRChungnam National University · KRGyeongsang National University · KRUniversité Joseph Fourier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Angiosperms require light for chlorophyll biosynthesis because one reaction in the pathway, the reduction of protochlorophyllide (Pchlide) to chlorophyllide, is catalyzed by the light-dependent protochlorophyllide oxidoreductase (POR). Here, we report that Cell growth defect factor1 (Cdf1), renamed here as chaperone-like protein of POR1 (CPP1), an essential protein for chloroplast development, plays a role in the regulation of POR stability and function. Cdf1/CPP1 contains a J-like domain and three transmembrane domains, is localized in the thylakoid and envelope membranes, and interacts with POR isoforms in chloroplasts. CPP1 can stabilize POR proteins with its holdase chaperone activity. CPP1 deficiency results in diminished POR protein accumulation and defective chlorophyll synthesis, leading to photobleaching and growth inhibition of plants under light conditions. CPP1 depletion also causes reduced POR accumulation in etioplasts of dark-grown plants and as a result impairs the formation of prolamellar bodies, which subsequently affects chloroplast biogenesis upon illumination. Furthermore, in cyanobacteria, the CPP1 homolog critically regulates POR accumulation and chlorophyll synthesis under high-light conditions, in which the dark-operative Pchlide oxidoreductase is repressed by its oxygen sensitivity. These findings and the ubiquitous presence of CPP1 in oxygenic photosynthetic organisms suggest the conserved nature of CPP1 function in the regulation of POR.

Indexed as

LightArabidopsisArabidopsis ProteinsChlorophyllChloroplast ProteinsChloroplastsGene Expression Regulation, PlantMolecular ChaperonesNicotianaOxidoreductases Acting on CH-CH Group DonorsPlants, Genetically ModifiedProtochlorophyllideRNA InterferenceArabidopsis ProteinsChlorophyllChloroplast ProteinsMolecular ChaperonesOxidoreductases Acting on CH-CH Group DonorsProtochlorophyllideprotochlorophyllide reductase

Identifiers

PMID24151298
PMCPMC3877821
OpenAlexW2043833167

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.