Evidence map›Paper›PMID 21969381›Full record

ArticleThe Journal of biological chemistry2011

Direct interaction of mitochondrial targeting presequences with purified components of the TIM23 protein complex.

Milit Marom, Dana Dayan, Keren Demishtein-Zohary, Dejana Mokranjac, Walter Neupert, Abdussalam Azem

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.7field-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

26 citing papers in PubMed, 60 citations in OpenAlex.

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  14. How lipids modulate mitochondrial protein import.Journal of bioenergetics and biomembranes · 2016
    Review
  15. Loss of TIM50 suppresses proliferation and induces apoptosis in breast cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  16. Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015
    Review
  17. Article
  18. Article
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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

6 authors at 3 institutions in 2 countries.

Milit MaromDepartment of Biochemistry and Molecular Biology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
Dana DayanDepartment of Biochemistry and Molecular Biology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
Keren Demishtein-ZoharyDepartment of Biochemistry and Molecular Biology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
Dejana MokranjacInstitute for Physiological Chemistry, University of Munich, Munich 81377, Germany.
Walter NeupertMax Planck Institute of Biochemistry, Martinsried 82152, Germany.
Abdussalam AzemDepartment of Biochemistry and Molecular Biology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel. Electronic address: azema@tauex.tau.ac.il.
Tel Aviv University · ILLudwig-Maximilians-Universität München · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Precursor proteins that are imported from the cytosol into the matrix of mitochondria carry positively charged amphipathic presequences and cross the inner membrane with the help of vital components of the TIM23 complex. It is currently unclear which subunits of the TIM23 complex recognize and directly bind to presequences. Here we analyzed the binding of presequence peptides to purified components of the TIM23 complex. The interaction of three different presequences with purified soluble domains of yeast Tim50 (Tim50IMS), Tim23 (Tim23IMS), and full-length Tim44 was examined. Using chemical cross-linking and surface plasmon resonance we demonstrate, for the first time, the ability of purified Tim50IMS and Tim44 to interact directly with the yeast Hsp60 presequence. We also analyzed their interaction with presequences derived from precursors of yeast mitochondrial 70-kDa heat shock protein (mHsp70) and of bovine cytochrome P450SCC. Moreover, we characterized the nature of the interactions and determined their KDs. On the basis of our results, we suggest a mechanism of translocation where stronger interactions of the presequences on the trans side of the channel support the import of precursor proteins through TIM23 into the matrix.

Indexed as

AnimalsBinding SitesBiophysicsBiotinCattleCholesterol Side-Chain Cleavage EnzymeCross-Linking ReagentsKineticsMembrane Transport ProteinsMitochondriaMitochondrial MembranesMitochondrial Precursor Protein Import Complex ProteinsPeptidesProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeBiotinCholesterol Side-Chain Cleavage EnzymeCross-Linking ReagentsMembrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsPeptidesSaccharomyces cerevisiae ProteinsTIM23 protein, S cerevisiae

Identifiers

PMID21969381
PMCPMC3243567
OpenAlexW2017723064

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.