Evidence map›Paper›PMID 9822596›Full record

ArticleThe EMBO journal1998

C- to N-terminal translocation of preproteins into mitochondria.

H Fölsch, B Gaume, M Brunner, W Neupert, R A Stuart

Abstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

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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

5 authors.

H FölschInstitut für Physiologische Chemie, Goethestrasse 33, 80336 München, Germany.
B Gaume
M Brunner
W Neupert
R A Stuart

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear-encoded mitochondrial matrix proteins in most cases contain N-terminal targeting signals and are imported in a linear N- to C-terminal (N-->C) fashion. We asked whether import can also occur in a C- to N-terminal direction (C-->N). We placed targeting signals at the C-terminus of passenger proteins. Import did occur in this 'backwards' fashion. It paralleled that of the 'normal' N-->C mechanism in terms of efficiency, rate, energetic requirements and ability to mediate unfolding and refolding during and following import of protein containing a folded domain. Furthermore, this reaction was mediated by the TIM17-23 machinery. The import pathway taken by certain inner-membrane proteins contains elements of such a C-->N translocation pathway, as they are targeted to mitochondria by internal targeting signals. These internal targeting signals appear to form loop structures together with neighbouring transmembrane segments, and penetrate the inner membrane in a membrane-potential-dependent manner. The dimeric TIM17-23 complex, together with mt-Hsp70, acts on both sides of the loop structure to facilitate their translocation into the matrix. On one side of the loop import occurs in the common N-->C direction, whereas the translocation of the other side involves the novel C-->N import direction. We conclude therefore that the mitochondrial import machinery displays no preference for the directionality of the import process.

Indexed as

Base SequenceBiological TransportDNA PrimersElectron Transport Complex IVHSP70 Heat-Shock ProteinsMitochondriaProtein PrecursorsProtein Sorting SignalsSaccharomyces cerevisiaeTetrahydrofolate DehydrogenaseDNA PrimersElectron Transport Complex IVHSP70 Heat-Shock ProteinsProtein PrecursorsProtein Sorting SignalsTetrahydrofolate Dehydrogenase

Identifiers

PMID9822596
PMCPMC1170998

What OpenQuestion holds

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Registered trials

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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.