Evidence map›Paper›PMID 10357811›Full record

ArticleThe EMBO journal1999

Competition between Sec- and TAT-dependent protein translocation in Escherichia coli.

S Cristóbal, J W de Gier, H Nielsen, G von Heijne

Abstract readComparative Study
In one paragraph

Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
10.0field-weighted citation impact, top 1% 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

94 citing papers in PubMed, 274 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Twin-arginine transport complex plays an essential role inbioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
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  8. SignalP: The Evolution of a Web Server.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  9. Protein Sorting Prediction.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. The biogenesis of β-lactamase enzymes.Microbiology (Reading, England) · 2022
    Review
  14. Review
  15. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Review

34 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

S CristóbalDepartment of Biochemistry, Stockholm University, S-106 91 Stockholm, Sweden.
J W de Gier
H Nielsen
G von Heijne
Stockholm University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recently, a new protein translocation pathway, the twin-arginine translocation (TAT) pathway, has been identified in both bacteria and chloroplasts. To study the possible competition between the TAT- and the well-characterized Sec translocon-dependent pathways in Escherichia coli, we have fused the TorA TAT-targeting signal peptide to the Sec-dependent inner membrane protein leader peptidase (Lep). We find that the soluble, periplasmic P2 domain from Lep is re-routed by the TorA signal peptide into the TAT pathway. In contrast, the full-length TorA-Lep fusion protein is not re-routed into the TAT pathway, suggesting that Sec-targeting signals in Lep can override TAT-targeting information in the TorA signal peptide. We also show that the TorA signal peptide can be converted into a Sec-targeting signal peptide by increasing the hydrophobicity of its h-region. Thus, beyond the twin-arginine motif, the overall hydrophobicity of the signal peptide plays an important role in TAT versus Sec targeting. This is consistent with statistical data showing that TAT-targeting signal peptides in general have less hydrophobic h-regions than Sec-targeting signal peptides.

Indexed as

Amino Acid SequenceArginineBacterial ProteinsBiological TransportEndopeptidase KEscherichia coliGlycineKineticsLeucineMolecular Sequence DataMutationPeptide FragmentsPeriplasmProtein ConformationProtein Processing, Post-TranslationalProtein Sorting SignalsArginineBacterial ProteinsEndopeptidase KGlycineLeucinePeptide FragmentsProtein Sorting SignalsRecombinant Fusion Proteins

Identifiers

PMID10357811
PMCPMC1171380
OpenAlexW2005211587

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.