Evidence map›Paper›PMID 25419702›Full record

ArticlePloS one2014

The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20.

Anna Vitlin Gruber, Gal Zizelski, Abdussalam Azem, Celeste Weiss

Abstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Rubisco Assembly in the Chloroplast.Frontiers in molecular biosciences · 2018
    Review
  6. Reconstitution of Pure Chaperonin Hetero-Oligomer PreparationsFrontiers in molecular biosciences · 2018
    Article
  7. Review
  8. 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

4 authors.

Anna Vitlin GruberDepartment of Biochemistry and Molecular Biology, Tel Aviv University, Tel Aviv, Israel.
Gal ZizelskiDepartment of Biochemistry and Molecular Biology, Tel Aviv University, Tel Aviv, Israel.
Abdussalam AzemDepartment of Biochemistry and Molecular Biology, Tel Aviv University, Tel Aviv, Israel.
Celeste WeissDepartment of Biochemistry and Molecular Biology, Tel Aviv University, Tel Aviv, Israel.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The A. thaliana genome encodes five co-chaperonin homologs, three of which are destined to the chloroplast. Two of the proteins, Cpn10(2) and Cpn20, form functional homo-oligomers in vitro. In the current work, we present data on the structure and function of the third A. thaliana co-chaperonin, which exhibits unique properties. We found that purified recombinant Cpn10(1) forms inactive dimers in solution, in contrast to the active heptamers that are formed by canonical Cpn10s. Additionally, our data demonstrate that Cpn10(1) is capable of assembling into active hetero-oligomers together with Cpn20. This finding was reinforced by the formation of active co-chaperonin species upon mixing an inactive Cpn20 mutant with the inactive Cpn10(1). The present study constitutes the first report of a higher plant Cpn10 subunit that is able to function only upon formation of hetero-oligomers with other co-chaperonins.

Indexed as

Protein MultimerizationArabidopsis ProteinsChaperoninsElectrophoresis, Polyacrylamide GelGroup I ChaperoninsModels, MolecularMutationProtein SubunitsArabidopsis ProteinsChaperoninsCpn10(1) protein, ArabidopsisCpn20 protein, ArabidopsisGroup I ChaperoninsProtein Subunits

Identifiers

PMID25419702
PMCPMC4242682

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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.