Evidence map›Paper›PMID 24946091›Full record

ArticleMolecular microbiology2014

Comparative analysis of the secretion capability of early and late flagellar type III secretion substrates.

Hanna M Singer, Marc Erhardt, Kelly T Hughes

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  15. Review
  16. Article
  17. RNA Localization in Bacteria.Microbiology spectrum · 2018
    Review
  18. Flagella-mediated secretion of a novelCommunications biology · 2018
    Article
  19. Article
  20. Article
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

3 authors at 2 institutions in 3 countries.

Hanna M SingerMicrobiologie, Département de Médecine, Université de Fribourg, Fribourg, Switzerland.
Marc Erhardt
Kelly T Hughes
University of Fribourg · CHUniversity of Utah · US

Funding

Coupling gene regulation to flagellar morphogenesisR01GM056141 · NIGMS · UNIVERSITY OF WASHINGTON · PI HUGHES, KELLY T · 1998 to 2023
$8.3M
NIGMS NIH HHS GM056141NIGMS NIH HHS R01 GM056141
6 · The paper itself

Abstract

A remarkable feature of the flagellar-specific type III secretion system (T3SS) is the selective recognition of a few substrate proteins among the many thousand cytoplasmic proteins. Secretion substrates are divided into two specificity classes: early substrates secreted for hook-basal body (HBB) construction and late substrates secreted after HBB completion. Secretion was reported to require a disordered N-terminal secretion signal, mRNA secretion signals within the 5'-untranslated region (5'-UTR) and for late substrates, piloting proteins known as the T3S chaperones. Here, we utilized translational β-lactamase fusions to probe the secretion efficacy of the N-terminal secretion signal of fourteen secreted flagellar substrates in Salmonella enterica. We observed a surprising variety in secretion capability between flagellar proteins of the same secretory class. The peptide secretion signals of the early-type substrates FlgD, FlgF, FlgE and the late-type substrate FlgL were analysed in detail. Analysing the role of the 5'-UTR in secretion of flgB and flgE revealed that the native 5'-UTR substantially enhanced protein translation and secretion. Based on our data, we propose a multicomponent signal that drives secretion via the flagellar T3SS. Both mRNA and peptide signals are recognized by the export apparatus and together with substrate-specific chaperones allowing for targeted secretion of flagellar substrates.

Indexed as

ArabinoseBacterial ProteinsBacterial Secretion Systemsbeta-LactamasesBiological TransportFlagellaMolecular ChaperonesProtein BiosynthesisRecombinant Fusion ProteinsSalmonella typhimuriumSubstrate SpecificityArabinoseBacterial ProteinsBacterial Secretion Systemsbeta-LactamasesMolecular ChaperonesRecombinant Fusion Proteins

Identifiers

PMID24946091
PMCPMC5076378
OpenAlexW1900806339

What OpenQuestion holds

Textmetadata
LicenceTDM
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.