Evidence map›Paper›PMID 26212107›Full record

ArticleScientific reports2015

Directionality of substrate translocation of the hemolysin A Type I secretion system.

Michael H H Lenders, Stefanie Weidtkamp-Peters, Diana Kleinschrodt, Karl-Erich Jaeger, Sander H J Smits, Lutz Schmitt

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. A molecular toolkit for heterologous protein secretion acrossbioRxiv : the preprint server for biology · 2023
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  7. Microorganisms · 2022
    Review
  8. Article
  9. Article
  10. Functional Analysis of Hypothetical Proteins ofBioinformatics and biology insights · 2022
    Article
  11. Cloning and Functional Characterization of PutativeJournal of microbiology and biotechnology · 2020
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Secretion of recombinant proteins fromEngineering in life sciences · 2018
    Review
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Michael H H LendersInstitute of Biochemistry, Heinrich-Heine-Universitaet, D-40225 Duesseldorf, Germany.
Stefanie Weidtkamp-PetersCenter for Advanced Imaging (CAi), Heinrich-Heine-Universitaet, D-40225 Duesseldorf, Germany.
Diana KleinschrodtProtein Production Facility, Heinrich-Heine-Universitaet, 40225 Duesseldorf, Germany.
Karl-Erich Jaeger1] Institute of Molecular Enzyme Technology, Heinrich-Heine-Universitaet and Institute of Bio- and Geosciences IBG-1: Biotechnology, Forschungszentrum Juelich GmbH, D-52426 Juelich, Germany [2] Center of Excellence on Plant Sciences (CEPLAS), Heinrich-Heine-Universitaet, D-40225 Duesseldorf, Germany.
Sander H J SmitsInstitute of Biochemistry, Heinrich-Heine-Universitaet, D-40225 Duesseldorf, Germany.
Lutz Schmitt1] Institute of Biochemistry, Heinrich-Heine-Universitaet, D-40225 Duesseldorf, Germany [2] Center of Excellence on Plant Sciences (CEPLAS), Heinrich-Heine-Universitaet, D-40225 Duesseldorf, Germany.
Heinrich Heine University Düsseldorf · DEForschungszentrum Jülich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type 1 secretion systems (T1SS) of Gram-negative bacteria are responsible for the secretion of various proteases, lipases, S-layer proteins or toxins into the extracellular space. The paradigm of these systems is the hemolysin A (HlyA) T1SS of Escherichia coli. This multiple membrane protein complex is able to secrete the toxin HlyA in one step across both E. coli membranes. Common to all secreted T1SS substrates is a C-terminal secretion sequence being necessary as well as sufficient for secretion. However, it is not known whether transport occurs directionally, i.e. the N- or the C-terminus of T1SS substrates is secreted first. We have addressed this question by constructing HlyA fusions with the rapidly folding eGFP resulting in a stalled T1SS. Differential labeling and subsequent fluorescence microscopic detection of C- and N-terminal parts of the fusions allowed us to demonstrate vectorial transport of HlyA through the T1SS with the C-terminus appearing first outside the bacterial cells.

Indexed as

Escherichia coliEscherichia coli ProteinsHemolysin ProteinsProtein Translocation SystemsProtein TransportEscherichia coli ProteinsHemolysin ProteinsHlya protein, E coliProtein Translocation Systems

Identifiers

PMID26212107
PMCPMC4648471
OpenAlexW942112336

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.