Evidence map›Paper›PMID 18071923›Full record

ArticlePhotosynthesis research2008

Proteomic analysis of highly purified prolamellar bodies reveals their significance in chloroplast development.

Lisa A Blomqvist, Margareta Ryberg, Christer Sundqvist

Abstract read
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In one paragraph

Article in Photosynthesis research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

33 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
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  7. Bean and Pea Plastoglobules Change in Response to Chilling Stress.International journal of molecular sciences · 2021
    Article
  8. Curvature thylakoid 1 proteins modulate prolamellar body morphology and promote organized thylakoid biogenesis inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
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  12. Review
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  14. Spatial Nano-Morphology of the Prolamellar Body in EtiolatedFrontiers in cell and developmental biology · 2020
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. 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

3 authors at 1 institution in 1 country.

Lisa A BlomqvistDepartment of Plant and Environmental Sciences, Göteborg University, P.O. Box 461, 405 30 Göteborg, Sweden. Lisa.Blomqvist@dpes.gu.se
Margareta Ryberg
Christer Sundqvist
University of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The prolamellar body (PLB) proteome of dark-grown wheat leaves was characterized. PLBs are formed not only in etioplasts but also in chloroplasts in young developing leaves during the night, yet their function is not fully understood. Highly purified PLBs were prepared from 7-day-old dark-grown leaves and identified by their spectral properties as revealed by low-temperature fluorescence spectroscopy. The PLB preparation had no contamination of extra-plastidal proteins, and only two envelope proteins were found. The PLB proteome was analysed by a combination of 1-D SDS-PAGE and nano-LC FTICR MS. The identification of chlorophyll synthase in the PLB fraction is the first time this enzyme protein was found in extracts of dark-grown plants. This finding is in agreement with its previous localization to PLBs using activity studies. NADPH:protochlorophyllide oxidoreductase A (PORA), which catalyses the reduction of protochlorophyllide to chlorophyllide, dominates the proteome of PLBs. Besides the identification of the PORA protein, the PORB protein was identified for the first time in dark-grown wheat. Altogether 64 unique proteins, representing pigment biosynthesis, photosynthetic light reaction, Calvin cycle proteins, chaperones and protein synthesis, were identified. The in number of proteins' largest group was the one involved in photosynthetic light reactions. This fact strengthens the assumption that the PLB membranes are precursors to the thylakoids and used for the formation of the photosynthetic membranes during greening. The present work is important to enhance our understanding of the significance of PLBs in chloroplast development.

Indexed as

ChlorophyllChloroplastsComputational BiologyMass SpectrometryOxidoreductases Acting on CH-CH Group DonorsPlant ProteinsProteomicsTriticumChlorophyllOxidoreductases Acting on CH-CH Group DonorsPlant Proteinsprotochlorophyllide reductase

Identifiers

PMID18071923
OpenAlexW2050807912

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.