Evidence map›Paper›PMID 21483722›Full record

ArticlePLoS biology2011

A chaperonin subunit with unique structures is essential for folding of a specific substrate.

Lianwei Peng, Yoichiro Fukao, Fumiyoshi Myouga, Reiko Motohashi, Kazuo Shinozaki, Toshiharu Shikanai

RetractedOpen access · goldAbstract readRetracted Publication
In one paragraph

Article in PLoS biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

34 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. OsCpn60β1 is Essential for Chloroplast Development in Rice (International journal of molecular sciences · 2020
    Article
  10. Article
  11. Low-Temperature Adaptation of the Snow AlgaFrontiers in microbiology · 2020
    Article
  12. Rubisco Assembly in the Chloroplast.Frontiers in molecular biosciences · 2018
    Review
  13. Reconstitution of Pure Chaperonin Hetero-Oligomer PreparationsFrontiers in molecular biosciences · 2018
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Lianwei PengDepartment of Botany, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto, Japan.
Yoichiro Fukao
Fumiyoshi Myouga
Reiko Motohashi
Kazuo Shinozaki
Toshiharu Shikanai
Kyoto University · JPNara Institute of Science and Technology · JPUniversity of Shizuoka · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type I chaperonins are large, double-ring complexes present in bacteria (GroEL), mitochondria (Hsp60), and chloroplasts (Cpn60), which are involved in mediating the folding of newly synthesized, translocated, or stress-denatured proteins. In Escherichia coli, GroEL comprises 14 identical subunits and has been exquisitely optimized to fold its broad range of substrates. However, multiple Cpn60 subunits with different expression profiles have evolved in chloroplasts. Here, we show that, in Arabidopsis thaliana, the minor subunit Cpn60β4 forms a heterooligomeric Cpn60 complex with Cpn60α1 and Cpn60β1-β3 and is specifically required for the folding of NdhH, a subunit of the chloroplast NADH dehydrogenase-like complex (NDH). Other Cpn60β subunits cannot complement the function of Cpn60β4. Furthermore, the unique C-terminus of Cpn60β4 is required for the full activity of the unique Cpn60 complex containing Cpn60β4 for folding of NdhH. Our findings suggest that this unusual kind of subunit enables the Cpn60 complex to assist the folding of some particular substrates, whereas other dominant Cpn60 subunits maintain a housekeeping chaperonin function by facilitating the folding of other obligate substrates.

Indexed as

Protein FoldingAmino Acid SequenceArabidopsisChaperonin 60ChloroplastsChromatography, AffinityGene Expression Regulation, PlantMolecular Sequence DataMutationReverse Transcriptase Polymerase Chain ReactionChaperonin 60

Identifiers

PMID21483722
PMCPMC3071376
OpenAlexW2013278943

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.