Evidence map›Paper›PMID 11171977›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae.

C Voisine, Y C Cheng, M Ohlson, B Schilke, K Hoff, H Beinert, J Marszalek, E A Craig

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

56 citing papers in PubMed, 130 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Sulfur Administration in Fe-S Cluster Homeostasis.Antioxidants (Basel, Switzerland) · 2021
    Review
  9. Review
  10. Fe-S Protein Synthesis in Green Algae Mitochondria.Plants (Basel, Switzerland) · 2021
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Molecular chaperones involved in mitochondrial iron-sulfur protein biogenesis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  17. Article
  18. Iron-sulfur cluster biogenesis and trafficking in mitochondria.The Journal of biological chemistry · 2017
    Review
  19. Article
  20. Review
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

8 authors at 3 institutions in 2 countries.

C VoisineDepartment of Biomolecular Chemistry, University of Wisconsin, Madison, WI 53706, USA.
Y C Cheng
M Ohlson
B Schilke
K Hoff
H Beinert
J Marszalek
E A Craig
University of California, Irvine · USUniversity of Gdańsk · PLUniversity of Wisconsin–Madison · US

Funding

TRANSCRIPTIONALLY REGULATED GENESR01GM027870 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CRAIG, ELIZABETH A · 1985 to 2017
$5.8M
NIGMS NIH HHS GM27870NIGMS NIH HHS R01 GM027870
6 · The paper itself

Abstract

A minor Hsp70 chaperone of the mitochondrial matrix of Saccharomyces cerevisiae, Ssq1, is involved in the formation or repair of Fe/S clusters and/or mitochondrial iron metabolism. Here, we report evidence that Jac1, a J-type chaperone of the mitochondrial matrix, is the partner of Ssq1 in this process. Reduced activity of Jac1 results in a decrease in activity of Fe/S containing mitochondrial proteins and an accumulation of iron in mitochondria. Fe/S enzyme activities remain low in both jac1 and ssq1 mutant mitochondria even if normal mitochondrial iron levels are maintained. Therefore, the low activities observed are not solely due to oxidative damage caused by excess iron. Rather, these molecular chaperones likely play a direct role in the normal assembly process of Fe/S clusters.

Indexed as

Saccharomyces cerevisiae ProteinsAconitate HydrataseAnimalsBinding SitesFungal ProteinsHSP70 Heat-Shock ProteinsIronMitochondriaMitochondrial ProteinsMolecular ChaperonesMutagenesis, Site-DirectedRabbitsSaccharomyces cerevisiaeSuccinate DehydrogenaseAconitate HydrataseFungal ProteinsHSP70 Heat-Shock ProteinsIronISU1 protein, S cerevisiaeJAC1 protein, S cerevisiaeMitochondrial ProteinsMolecular ChaperonesNFU1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSSQ1 protein, S cerevisiaeSuccinate Dehydrogenase

Identifiers

PMID11171977
PMCPMC29283
OpenAlexW2093363808

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.