Evidence map›Paper›PMID 10648604›Full record

ArticleMolecular and cellular biology2000

Tim18p, a new subunit of the TIM22 complex that mediates insertion of imported proteins into the yeast mitochondrial inner membrane.

C M Koehler, M P Murphy, N A Bally, D Leuenberger, W Oppliger, L Dolfini, T Junne, G Schatz, E Or

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

29 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Altered Mitochondrial Protein Homeostasis and Proteinopathies.Frontiers in molecular neuroscience · 2022
    Review
  5. Targeting and Insertion of Membrane Proteins in Mitochondria.Frontiers in cell and developmental biology · 2021
    Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. The Expanding Landscape of Moonlighting Proteins in Yeasts.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  12. Article
  13. Article
  14. Mechanisms of protein sorting in mitochondria.Cold Spring Harbor perspectives in biology · 2012
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  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

9 authors at 1 institution in 1 country.

C M KoehlerBiozentrum, University of Basel, CH-4056 Basel, Switzerland.
M P Murphy
N A Bally
D Leuenberger
W Oppliger
L Dolfini
T Junne
G Schatz
E Or
University of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Import of carrier proteins from the cytoplasm into the mitochondrial inner membrane of yeast is mediated by a distinct system consisting of two soluble 70-kDa protein complexes in the intermembrane space and a 300-kDa complex in the inner membrane, the TIM22 complex. The TIM22 complex contains the peripheral subunits Tim9p, Tim10p, and Tim12p and the integral membrane subunits Tim22p and Tim54p. We identify here an additional subunit, an 18-kDa integral membrane protein termed Tim18p. This protein is made as a 21.9-kDa precursor which is imported into mitochondria and processed to its mature form. When mitochondria are gently solubilized, Tim18p comigrates with the other subunits of the TIM22 complex on nondenaturing gels and is coimmunoprecipitated with Tim54p and Tim12p. Tim18p does not cofractionate with the TIM23 complex upon immunoprecipitation or nondenaturing gel electrophoresis. Deletion of Tim18p decreases the growth rate of yeast cells by a factor of two and is synthetically lethal with temperature-sensitive mutations in Tim9p or Tim10p. It also impairs the import of several precursor proteins into isolated mitochondria, and lowers the apparent mass of the TIM22 complex. We suggest that Tim18p functions in the assembly and stabilization of the TIM22 complex but does not directly participate in protein insertion into the inner membrane.

Indexed as

AntiportersMembrane Transport ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceBase SequenceBiological Transport, ActiveCarrier ProteinsDNA, FungalFungal ProteinsGene DeletionGenes, FungalIntracellular MembranesMacromolecular SubstancesMembrane ProteinsMitochondriaMitochondrial Membrane Transport ProteinsAntiportersCarrier ProteinsDNA, FungalFungal ProteinsMacromolecular SubstancesMembrane ProteinsMembrane Transport ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsSaccharomyces cerevisiae ProteinsTim18 protein, S cerevisiaeTIM22 protein, S cerevisiae

Identifiers

PMID10648604
PMCPMC85242
OpenAlexW2094356666

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.