Evidence map›Paper›PMID 7628445›Full record

ArticleThe EMBO journal1995

Conservative sorting of F0-ATPase subunit 9: export from matrix requires delta pH across inner membrane and matrix ATP.

E E Rojo, R A Stuart, W Neupert

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 78 citations in OpenAlex.

  1. A dynamic displacement mechanism drives protein import into mitochondria.bioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Mitochondrial membrane potential.Analytical biochemistry · 2018
    Review
  7. Plant Mitochondrial Inner Membrane Protein Insertion.International journal of molecular sciences · 2018
    Review
  8. Article
  9. Article
  10. Article
  11. Delivery of drugs and macromolecules to mitochondria.Advanced drug delivery reviews · 2007
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Oxa1p, an essential component of the N-tail protein export machinery in mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 1998
    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

3 authors at 1 institution in 1 country.

E E RojoInstitut für Physiologische Chemie der Universität München, Germany.
R A Stuart
W Neupert
Ludwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In an attempt to understand the mechanisms of sorting of mitochondrial inner membrane proteins, we have analyzed the import of subunit 9 of the mitochondrial F1F0-ATPase (Su9) from Neurospora crassa, an integral inner membrane protein. A chimeric protein was used consisting of the presequence and the first transmembrane domain of Su9 fused to mouse dihydrofolate reductase (preSu9(1-112)-DHFR). This protein attains the correct topology across the inner membrane (Nout-Cin) following import. The transmembrane domain becomes first completely imported into the matrix, where after processing of the presequence, it mediates membrane insertion and export of the N-terminal tail. Import and export steps can be experimentally dissected into two distinct events. Translocation of the N-terminal hydrophilic tail out of the matrix was blocked when the presequence was not processed, indicating an important role of the sequences and charges flanking the hydrophobic domain. Furthermore, export was supported by a delta pH and required matrix ATP hydrolysis. Thus the hydrophobic transmembrane domain operates as a membrane insertion signal and not as a stop-transfer signal. Our findings suggest that several aspects of this sorting process have been conserved from their prokaryotic ancestors.

Indexed as

Adenosine TriphosphateAmino Acid SequenceAnimalsBiological Transport, ActiveHSP70 Heat-Shock ProteinsHydrogen-Ion ConcentrationHydrolysisIntracellular MembranesMembrane ProteinsMiceMitochondriaMolecular Sequence DataNeurospora crassaProtein PrecursorsProtein Sorting SignalsProton-Translocating ATPasesAdenosine TriphosphateHSP70 Heat-Shock ProteinsMembrane ProteinsProtein PrecursorsProtein Sorting SignalsProton-Translocating ATPasesRecombinant Fusion ProteinsTetrahydrofolate Dehydrogenase

Identifiers

PMID7628445
PMCPMC394411
OpenAlexW27628436

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.