Evidence map›Paper›PMID 22801422›Full record

ArticleThe Journal of biological chemistry2012

Revisiting the supramolecular organization of photosystem II in Chlamydomonas reinhardtii.

Ryutaro Tokutsu, Nobuyasu Kato, Khanh Huy Bui, Takashi Ishikawa, Jun Minagawa

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

  1. Article
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  9. Structure ofeLife · 2023
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  10. Article
  11. State transition is quiet around pyrenoid and LHCII phosphorylation is not essential for thylakoid deformation inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Article
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  15. Article
  16. 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

5 authors.

Ryutaro TokutsuDivision of Environmental Photobiology, National Institute for Basic Biology, Okazaki 444-8585, Japan.
Nobuyasu Kato
Khanh Huy Bui
Takashi Ishikawa
Jun Minagawa

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosystem II (PSII) is a multiprotein complex that splits water and initiates electron transfer in photosynthesis. The central part of PSII, the PSII core, is surrounded by light-harvesting complex II proteins (LHCIIs). In higher plants, two or three LHCII trimers are seen on each side of the PSII core whereas only one is seen in the corresponding positions in Chlamydomonas reinhardtii, probably due to the absence of CP24, a minor monomeric LHCII. Here, we re-examined the supramolecular organization of the C. reinhardtii PSII-LHCII supercomplex by determining the effect of different solubilizing detergents. When we solubilized the thylakoid membranes with n-dodecyl-β-D-maltoside (β-DM) or n-dodecyl-α-D-maltoside (α-DM) and subjected them to gel filtration, we observed a clear difference in molecular mass. The α-DM-solubilized PSII-LHCII supercomplex bound twice more LHCII than the β-DM-solubilized supercomplex and retained higher oxygen-evolving activity. Single-particle image analysis from electron micrographs of the α-DM-solubilized and negatively stained supercomplex revealed that the PSII-LHCII supercomplex had a novel supramolecular organization, with three LHCII trimers attached to each side of the core.

Indexed as

Chlamydomonas reinhardtiiDetergentsGlucosidesPhotosystem II Protein ComplexProtein Structure, QuaternaryThylakoidsDetergentsdodecyl maltosideGlucosidesPhotosystem II Protein Complex

Identifiers

PMID22801422
PMCPMC3438989

What OpenQuestion holds

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Registered trials

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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.