Evidence map›Paper›PMID 23053543›Full record

ArticlePlanta2013

The first α-helical domain of the vesicle-inducing protein in plastids 1 promotes oligomerization and lipid binding.

Stephanie Otters, Paula Braun, Johanna Hubner, Gerhardt Wanner, Ute C Vothknecht, Fatima Chigri

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

32 citing papers in PubMed, 59 citations in OpenAlex.

  1. Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins.The Plant journal : for cell and molecular biology · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. DistinctiveFrontiers in plant science · 2022
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Phosphoinositides regulate chloroplast processes.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Article
  16. Article
  17. Review
  18. Chloroplast vesicle transport.Photosynthesis research · 2018
    Review
  19. Article
  20. MgThe Journal of biological chemistry · 2018
    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

6 authors at 4 institutions in 1 country.

Stephanie OttersDepartment of Biology I, Botany, LMU Munich, Großhaderner Strasse 2-4, Planegg-Martinsried, Munich, Germany.
Paula Braun
Johanna Hubner
Gerhardt Wanner
Ute C Vothknecht
Fatima Chigri
Urologische Klinik München · DECenter for Integrated Protein Science Munich · DELudwig-Maximilians-Universität München · DEMunich University of Applied Sciences · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The vesicle-inducing protein in plastids 1 (Vipp1) is an essential component for thylakoid biogenesis in cyanobacteria and chloroplasts. Vipp1 proteins share significant structural similarity with their evolutionary ancestor PspA (bacterial phage shock protein A), namely a predominantly α-helical structure, the formation of oligomeric high molecular weight complexes (HMW-Cs) and a tight association with membranes. Here, we elucidated domains of Vipp1 from Arabidopsis thaliana involved in homo-oligomerization as well as association with chloroplast inner envelope membranes. We could show that the 21 N-terminal amino acids of Vipp1, which form the first α-helix of the protein, are essential for assembly of the 2 MDa HMW-C but are not needed for formation of smaller subcomplexes. Interestingly, removal of this domain also interferes with association of the Vipp1 protein to the inner envelope. Fourier transform infrared spectroscopy of recombinant Vipp1 further indicates that Escherichia coli lipids bind tightly enough that they can be co-purified with the protein. This feature also depends on the presence of the first helix, which strongly supports an interaction of lipids with the Vipp1 HMW-C but not with smaller subcomplexes. Therefore, Vipp1 oligomerization appears to be a prerequisite for its membrane association. Our results further highlight structural differences between Vipp1 and PspA, which might be important in regard to their different function in thylakoid biogenesis and bacterial stress response, respectively.

Indexed as

ArabidopsisArabidopsis ProteinsBacterial ProteinsChloroplast ProteinsChromatography, GelCloning, MolecularEscherichia coliHeat-Shock ProteinsIntracellular MembranesMembrane LipidsMembrane ProteinsMolecular WeightMultiprotein ComplexesPlastidsProtein BindingProtein Structure, SecondaryArabidopsis ProteinsBacterial ProteinsChloroplast ProteinsHeat-Shock ProteinsMembrane LipidsMembrane ProteinsMultiprotein Complexesphage shock protein, BacteriaRecombinant ProteinsVIPP1 protein, Arabidopsis

Identifiers

PMID23053543
OpenAlexW2024956866

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.