Evidence map›Paper›PMID 9405363›Full record

ArticleThe EMBO journal1997

The chloroplastic protein import machinery contains a Rieske-type iron-sulfur cluster and a mononuclear iron-binding protein.

A Caliebe, R Grimm, G Kaiser, J Lübeck, J Soll, L Heins

Abstract readComparative Study
In one paragraph

Article in The EMBO journal, 1997. 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
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

51 citing papers in PubMed, 186 citations in OpenAlex.

  1. Review
  2. Article
  3. Coexpressed subunits of dual genetic origin define a conserved supercomplex mediating essential protein import into chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  4. Article
  5. Article
  6. A Protochlorophyllide (Pchlide)Frontiers in plant science · 2019
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Three proteins mediate import of transit sequence-less precursors into the inner envelope of chloroplasts in Arabidopsis thaliana.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Three thioredoxin targets in the inner envelope membrane of chloroplasts function in protein import and chlorophyll metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  20. 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 1 institution in 1 country.

A CaliebeBotanisches Institut, Christian-Albrechts-Universität, Am Botanischen Garten 1-9, D-24118 Kiel, Germany.
R Grimm
G Kaiser
J Lübeck
J Soll
L Heins
Christian-Albrechts-Universität zu Kiel · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transport of precursor proteins across the chloroplastic envelope membranes requires the interaction of protein translocons localized in both the outer and inner envelope membranes. Analysis by blue native gel electrophoresis revealed that the translocon of the inner envelope membranes consisted of at least six proteins with molecular weights of 36, 45, 52, 60, 100 and 110 kDa, respectively. Tic110 and ClpC, identified as components of the protein import apparatus of the inner envelope membrane, were prominent constituents of this complex. The amino acid sequence of the 52 kDa protein, deduced from the cDNA, contains a predicted Rieske-type iron-sulfur cluster and a mononuclear iron-binding site. Diethylpyrocarbonate, a Rieske-type protein-modifying reagent, inhibits the translocation of precursor protein across the inner envelope membrane, whereas binding of the precursor to the outer envelope membrane is still possible. In another independent experimental approach, the 52 kDa protein could be co-purified with a trapped precursor protein in association with the chloroplast protein translocon subunits Toc86, Toc75, Toc34 and Tic110. Together, these results strongly suggest that the 52 kDa protein, named Tic55 due to its calculated molecular weight, is a member of the chloroplastic inner envelope protein translocon.

Indexed as

Electron Transport Complex IIIAmino Acid SequenceBinding SitesCarrier ProteinsChloroplastsCloning, MolecularDiethyl PyrocarbonateIntracellular MembranesIron-Binding ProteinsIron-Sulfur ProteinsMembrane ProteinsMolecular Sequence DataMolecular WeightPisum sativumProtein PrecursorsRecombinant ProteinsCarrier ProteinsDiethyl PyrocarbonateElectron Transport Complex IIIIron-Binding ProteinsIron-Sulfur ProteinsMembrane ProteinsProtein PrecursorsRecombinant ProteinsRieske iron-sulfur proteinTransferrin-Binding Proteins

Identifiers

PMID9405363
PMCPMC1170334
OpenAlexW2043433011

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.