Evidence map›Paper›PMID 39321213›Full record

ArticleThe Plant cell2024

Membrane protein provision controls prothylakoid biogenesis in tobacco etioplasts.

Bingqi Li, Tegan Armarego-Marriott, Łucja Kowalewska, Wolfram Thiele, Alexander Erban, Stephanie Ruf, Joachim Kopka, Mark Aurel Schöttler, Ralph Bock

Abstract read
In one paragraph

Article in The Plant cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. The lumenal domain of Cyt bPhotosynthesis research · 2025
    Article
  3. Article
  4. 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

9 authors.

Bingqi LiMax Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany.ORCID 0000-0003-0863-0544
Tegan Armarego-MarriottMax Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany.ORCID 0000-0002-8745-9468
Łucja KowalewskaFaculty of Biology, Department of Plant Anatomy and Cytology, University of Warsaw, 02-096 Warsaw, Poland.ORCID 0000-0002-4090-6291
Wolfram ThieleMax Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany.ORCID 0000-0001-7846-4540
Alexander ErbanMax Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany.ORCID 0000-0003-1794-588X
Stephanie RufMax Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany.ORCID 0000-0002-9469-5944
Joachim KopkaMax Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany.ORCID 0000-0001-9675-4883
Mark Aurel SchöttlerMax Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany.ORCID 0000-0003-3210-0260
Ralph BockMax Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany.ORCID 0000-0001-7502-6940

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cytochrome b559 heterodimer is a conserved component of photosystem II whose physiological role in photosynthetic electron transfer is enigmatic. A particularly puzzling aspect of cytochrome b559 has been its presence in etiolated seedlings, where photosystem II is absent. Whether or not the cytochrome has a specific function in etioplasts is unknown. Here, we have attempted to address the function of cytochrome b559 by generating transplastomic tobacco (Nicotiana tabacum) plants that overexpress psbE and psbF, the plastid genes encoding the two cytochrome b559 apoproteins. We show that strong overaccumulation of the PsbE apoprotein can be achieved in etioplasts by suitable manipulations of the promoter and the translation signals, while the cytochrome b559 level is only moderately elevated. The surplus PsbE protein causes striking ultrastructural alterations in etioplasts; most notably, it causes a condensed prolamellar body and a massive proliferation of prothylakoids, with multiple membrane layers coiled into spiral-like structures. Analysis of plastid lipids revealed that increased PsbE biosynthesis strongly stimulated plastid lipid biosynthesis, suggesting that membrane protein abundance controls prothylakoid membrane biogenesis. Our data provide evidence for a structural role of PsbE in prolamellar body formation and prothylakoid biogenesis, and indicate that thylakoid membrane protein abundance regulates lipid biosynthesis in etioplasts.

Indexed as

etioplastplastidplastid transformationprolamellar bodyprothylakoidregulation of lipid biosynthesisthylakoid biogenesis

Identifiers

PMID39321213
PMCPMC11638105

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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.