Evidence map›Paper›PMID 20959450›Full record

ArticleThe Journal of biological chemistry2010

YidC is involved in the biogenesis of the secreted autotransporter hemoglobin protease.

Wouter S P Jong, Corinne M ten Hagen-Jongman, Eelco Ruijter, Romano V A Orru, Pierre Genevaux, Joen Luirink

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Overproduction of β-barrel outer membrane proteins inExtracellular vesicles and circulating nucleic acids · 2025
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  14. Review
  15. Article
  16. 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

6 authors at 2 institutions in 2 countries.

Wouter S P JongSection of Molecular Microbiology, Department of Molecular Cell Biology, VU University, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands.
Corinne M ten Hagen-Jongman
Eelco Ruijter
Romano V A Orru
Pierre Genevaux
Joen Luirink
Vrije Universiteit Amsterdam · NLLaboratoire de Microbiologie et Génétique Moléculaires · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autotransporters (ATs) constitute an important family of virulence factors secreted by Gram-negative bacteria. Following their translocation across the inner membrane (IM), ATs temporarily reside in the periplasmic space after which they are secreted into the extracellular environment. Previous studies have shown that the AT hemoglobin protease (Hbp) of Escherichia coli requires a functional signal recognition particle pathway and Sec translocon for optimal targeting to and translocation across the IM. Here, we analyzed the mode of IM translocation of Hbp in more detail. Using site-directed photocross-linking, we found that the Hbp signal peptide is adjacent to YidC early during biogenesis. Notably, YidC is in part associated with the Sec translocon but has until now primarily been implicated in the biogenesis of IM proteins. In vivo, YidC appeared critical for the biogenesis of the ATs Hbp and EspC. For Hbp, depletion of YidC resulted in the formation of secretion-incompetent intermediates that were sensitive to degradation by the periplasmic protease DegP, indicating that YidC activity affects Hbp biogenesis at a late stage, after translocation across the IM. This is the first demonstration of a role for YidC in the biogenesis of an extracellular protein. We propose that YidC is required for maintenance of the translocation-competent state of certain ATs in the periplasm. The large periplasmic domain of YidC is not critical for this novel functionality as it can be deleted without affecting Hbp biogenesis.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsCell MembraneEndopeptidasesEscherichia coliEscherichia coli ProteinsHeat-Shock ProteinsMembrane Transport ProteinsPeriplasmPeriplasmic ProteinsProtein Sorting SignalsProtein Structure, TertiarySecA ProteinsSEC Translocation ChannelsSerine EndopeptidasesAdenosine TriphosphatasesBacterial ProteinsDegP proteaseEndopeptidasesEscherichia coli ProteinsHeat-Shock Proteinshemoglobin protease HbpMembrane Transport ProteinsPeriplasmic ProteinsProtein Sorting SignalsSecA ProteinsSEC Translocation ChannelsSerine EndopeptidasesYIDC protein, E coli

Identifiers

PMID20959450
PMCPMC3000949
OpenAlexW2128562787

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.