Evidence map›Paper›PMID 17122363›Full record

ArticleMolecular biology of the cell2007

The Tim9p/10p and Tim8p/13p complexes bind to specific sites on Tim23p during mitochondrial protein import.

Alison J Davis, Nathan N Alder, Robert E Jensen, Arthur E Johnson

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2007. 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
–field-weighted citation impact
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.

  1. From the cytosol to the inner membrane: biogenesis of the mitochondrial carrier family.Protein science : a publication of the Protein Society · 2026
    Review
  2. Review
  3. Review
  4. How do Chaperones Bind (Partly) Unfolded Client Proteins?Frontiers in molecular biosciences · 2021
    Review
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  6. Review
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  20. Mechanisms of protein sorting in mitochondria.Cold Spring Harbor perspectives in biology · 2012
    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

4 authors.

Alison J DavisDepartment of Molecular and Cellular Medicine, Texas A&M University System Health Science Center, College Station, TX 77843-1114, USA.
Nathan N Alder
Robert E Jensen
Arthur E Johnson

Funding

THE INTERACTION OF AA-TRNA WITH EF-TU AND RIBOSOMESR01GM026494 · NIGMS · UNIVERSITY OF OKLAHOMA NORMAN · PI JOHNSON, ARTHUR E · 1985 to 2011
$3.7M
MITOCHONDRIAL DYNAMICS-MORPHOLOGY/DIVISION/SEGREGATIONR01GM054021 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI JENSEN, ROBERT E · 1996 to 2008
$2.7M
Protein Translocation and Integration at MitochondriaR01GM064580 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI JOHNSON, ARTHUR E · 2002 to 2005
$1.4M
NIGMS NIH HHS GM26494NIGMS NIH HHS GM54021NIGMS NIH HHS GM64580NIGMS NIH HHS R01 GM026494NIGMS NIH HHS R01 GM054021NIGMS NIH HHS R01 GM064580
6 · The paper itself

Abstract

The import of polytopic membrane proteins into the mitochondrial inner membrane (IM) is facilitated by Tim9p/Tim10p and Tim8p/Tim13p protein complexes in the intermembrane space (IMS). These complexes are proposed to act as chaperones by transporting the hydrophobic IM proteins through the aqueous IMS and preventing their aggregation. To examine the nature of this interaction, Tim23p molecules containing a single photoreactive cross-linking probe were imported into mitochondria in the absence of an IM potential where they associated with small Tim complexes in the IMS. On photolysis and immunoprecipitation, a probe located at a particular Tim23p site (27 different locations were examined) was found to react covalently with, in most cases, only one of the small Tim proteins. Tim8p, Tim9p, Tim10p, and Tim13p were therefore positioned adjacent to specific sites in the Tim23p substrate before its integration into the IM. This specificity of binding to Tim23p strongly suggests that small Tim proteins do not function solely as general chaperones by minimizing the exposure of nonpolar Tim23p surfaces to the aqueous medium, but may also align a folded Tim23p substrate in the proper orientation for delivery and integration into the IM at the TIM22 translocon.

Indexed as

Binding SitesMembrane ProteinsMembrane Transport ProteinsMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMultiprotein ComplexesProtein ConformationProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityMembrane ProteinsMembrane Transport ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMultiprotein ComplexesSaccharomyces cerevisiae ProteinsTIM10 protein, S cerevisiaeTIM13 protein, S cerevisiaeTIM23 protein, S cerevisiaeTim8 protein, S cerevisiaeTim9 protein, S cerevisiae

Identifiers

PMID17122363
PMCPMC1783793

What OpenQuestion holds

Textmetadata
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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.