Evidence map›Paper›PMID 21357482›Full record

ArticleJournal of bacteriology2011

A C-terminal region of Yersinia pestis YscD binds the outer membrane secretin YscC.

Julia A Ross, Gregory V Plano

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

17 citing papers in PubMed, 36 citations in OpenAlex.

  1. Probing Protein Topology and Conformation by Limited Proteolysis.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  2. Article
  3. Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016
    Review
  9. Review
  10. Review
  11. Article
  12. Regulation of the Yersinia type III secretion system: traffic control.Frontiers in cellular and infection microbiology · 2013
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. 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

2 authors at 1 institution in 1 country.

Julia A RossDepartment of Microbiology and Immunology, University of Miami Miller School of Medicine, Miami, FL 33101, USA.
Gregory V Plano
University of Miami · US

Funding

Structure of the Yersinia pestis type III export complexR01AI050552 · NIAID · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI PLANO, GREGORY V · 2001 to 2004
$903k
NIAID NIH HHS AI050552NIAID NIH HHS R01 AI050552
6 · The paper itself

Abstract

YscD is an essential component of the plasmid pCD1-encoded type III secretion system (T3SS) of Yersinia pestis. YscD has a single transmembrane (TM) domain that connects a small N-terminal cytoplasmic region (residues 1 to 121) to a larger periplasmic region (residues 143 to 419). Deletion analyses established that both the N-terminal cytoplasmic region and the C-terminal periplasmic region are required for YscD function. Smaller targeted deletions demonstrated that a predicted cytoplasmic forkhead-associated (FHA) domain is also required to assemble a functional T3SS; in contrast, a predicted periplasmic phospholipid binding (BON) domain and a putative periplasmic "ring-building motif" domain of YscD could be deleted with no significant effect on the T3S process. Although deletion of the putative "ring-building motif" domain did not disrupt T3S activity per se, the calcium-dependent regulation of the T3S apparatus was affected. The extreme C-terminal region of YscD (residues 354 to 419) was essential for secretion activity and had a strong dominant-negative effect on the T3S process when exported to the periplasm of the wild-type parent strain. Coimmunoprecipitation studies demonstrated that this region of YscD mediates the interaction of YscD with the outer membrane YscC secretin complex. Finally, replacement of the YscD TM domain with a TM domain of dissimilar sequence had no effect on the T3S process, indicating that the TM domain has no sequence-specific function in the assembly or function of the T3SS.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsCell MembraneConserved SequenceGene Expression Regulation, BacterialMembrane Transport ProteinsModels, MolecularMolecular Sequence DataMultigene FamilyProtein BindingProtein ConformationProtein Structure, TertiaryYersinia pestisBacterial Outer Membrane ProteinsMembrane Transport ProteinsYscC protein, Yersinia pestis

Identifiers

PMID21357482
PMCPMC3133092
OpenAlexW2091115293

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.