Evidence map›Paper›PMID 19720832›Full record

ArticleThe Journal of biological chemistry2009

Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55.

Adi Naamati, Neta Regev-Rudzki, Shlomi Galperin, Roland Lill, Ophry Pines

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 86 citations in OpenAlex.

  1. Review
  2. Pulling back the mitochondria's iron curtain.npj metabolic health and disease · 2025
    Review
  3. Review
  4. Mitochondria function in cytoplasmic FeS protein biogenesis.Biochimica et biophysica acta. Molecular cell research · 2024
    Review
  5. Article
  6. Article
  7. The Journey of Mitochondrial Protein Import and the Roadmap to Follow.International journal of molecular sciences · 2023
    Review
  8. The identification of two M20B family peptidases required for full virulence inFrontiers in cellular and infection microbiology · 2023
    Article
  9. Review
  10. Review
  11. Article
  12. Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. A single mNature communications · 2021
    Article
  14. Fe-S Protein Synthesis in Green Algae Mitochondria.Plants (Basel, Switzerland) · 2021
    Review
  15. Review
  16. Article
  17. Using synthetic biology to overcome barriers to stable expression of nitrogenase in eukaryotic organelles.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Proteolytic Control of Lipid Metabolism.ACS chemical biology · 2019
    Review
  19. 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

5 authors at 2 institutions in 2 countries.

Adi NaamatiDepartment of Microbiology and Molecular Genetics, IMRIC, Faculty of Medicine, Hebrew University, Jerusalem 91120, Israel.
Neta Regev-Rudzki
Shlomi Galperin
Roland Lill
Ophry Pines
Hebrew University of Jerusalem · ILPhilipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, each subcellular compartment harbors a specific group of proteins that must accomplish specific tasks. Nfs1 is a highly conserved mitochondrial cysteine desulfurase that participates in iron-sulfur cluster assembly as a sulfur donor. Previous genetic studies, in Saccharomyces cerevisiae, have suggested that this protein distributes between the mitochondria and the nucleus with biochemically undetectable amounts in the nucleus (termed "eclipsed distribution"). Here, we provide direct evidence for Nfs1 nuclear localization (in addition to mitochondria) using both alpha-complementation and subcellular fractionation. We also demonstrate that mitochondrial and nuclear Nfs1 are derived from a single translation product. Our data suggest that the Nfs1 distribution mechanism involves at least partial entry of the Nfs1 precursor into mitochondria, and then retrieval of a minor subpopulation (probably by reverse translocation) into the cytosol and then the nucleus. To further elucidate the mechanism of Nfs1 distribution we determined the N-terminal mitochondrial sequence of Nfs1 by Edman degradation. This led to the discovery of a novel mitochondrial processing enzyme, Icp55. This enzyme removes three amino acids from the N terminus of Nfs1 after cleavage by mitochondrial processing peptidase. Intriguingly, Icp55 protease (like its substrate Nfs1) appears to be dual distributed between the nucleus and mitochondria.

Indexed as

Active Transport, Cell NucleusAminopeptidasesCytosolMitochondriaMitochondrial ProteinsProtein TransportSaccharomyces cerevisiae ProteinsSulfurtransferasesAminopeptidasesIcp55 protein, S cerevisiaeMitochondrial ProteinsNFS1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSulfurtransferases

Identifiers

PMID19720832
PMCPMC2781575
OpenAlexW2017392747

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.