Evidence map›Paper›PMID 25275625›Full record

ArticlePLoS genetics2014

Evidence of a bacterial receptor for lysozyme: binding of lysozyme to the anti-σ factor RsiV controls activation of the ecf σ factor σV.

Jessica L Hastie, Kyle B Williams, Carolina Sepúlveda, Jon C Houtman, Katrina T Forest, Craig D Ellermeier

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Identification of DraRS inJournal of bacteriology · 2023
    Article
  3. Article
  4. Review
  5. Disruption of theJournal of bacteriology · 2022
    Article
  6. Article
  7. Article
  8. Activation of the extracytoplasmic function σ factor σCurrent opinion in microbiology · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. 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

6 authors at 2 institutions in 1 country.

Jessica L HastieDepartment of Microbiology, Carver College of Medicine, University of Iowa, Iowa City, Iowa, United States of America.
Kyle B WilliamsDepartment of Microbiology, Carver College of Medicine, University of Iowa, Iowa City, Iowa, United States of America.
Carolina SepúlvedaDepartment of Bacteriology, University of Wisconsin Madison, Madison, Wisconsin, United States of America.
Jon C HoutmanDepartment of Microbiology, Carver College of Medicine, University of Iowa, Iowa City, Iowa, United States of America.
Katrina T ForestDepartment of Bacteriology, University of Wisconsin Madison, Madison, Wisconsin, United States of America.
Craig D EllermeierDepartment of Microbiology, Carver College of Medicine, University of Iowa, Iowa City, Iowa, United States of America.
University of Iowa · USUniversity of Wisconsin–Madison · US

Funding

TRAINING IN MECHANISMS OF PARASITISMT32AI007511 · NIAID · UNIVERSITY OF IOWA · PI BUTLER, NOAH SULLIVAN, WEBER, MARY · 1996 to 2025
$8.1M
Identification of daptomycin resistance mechanisms in Clostridioides difficileR01AI087834 · NIAID · UNIVERSITY OF IOWA · PI ELLERMEIER, CRAIG D · 2011 to 2025
$5.6M
NIAID NIH HHS R01 AI087834NIAID NIH HHS R01AI087834NIAID NIH HHS T32 AI007511NIAID NIH HHS T32 AI07511
6 · The paper itself

Abstract

σ factors endow RNA polymerase with promoter specificity in bacteria. Extra-Cytoplasmic Function (ECF) σ factors represent the largest and most diverse family of σ factors. Most ECF σ factors must be activated in response to an external signal. One mechanism of activation is the stepwise proteolytic destruction of an anti-σ factor via Regulated Intramembrane Proteolysis (RIP). In most cases, the site-1 protease required to initiate the RIP process directly senses the signal. Here we report a new mechanism in which the anti-σ factor rather than the site-1 protease is the sensor. We provide evidence suggesting that the anti-σ factor RsiV is the bacterial receptor for the innate immune defense enzyme, lysozyme. The site-1 cleavage site is similar to the recognition site of signal peptidase and cleavage at this site is required for σV activation in Bacillus subtilis. We reconstitute site-1 cleavage in vitro and demonstrate that it requires both signal peptidase and lysozyme. We demonstrate that the anti-σ factor RsiV directly binds to lysozyme and muramidase activity is not required for σV activation. We propose a model in which the binding of lysozyme to RsiV activates RsiV for signal peptidase cleavage at site-1, initiating proteolytic destruction of RsiV and activation of σV. This suggests a novel mechanism in which conformational change in a substrate controls the cleavage susceptibility for signal peptidase. Thus, unlike other ECF σ factors which require regulated intramembrane proteolysis for activation, the sensor for σV activation is not the site-1 protease but the anti-σ factor.

Indexed as

Bacillus subtilisBacterial ProteinsCalorimetryClostridioides difficileEndopeptidasesEnterococcus faecalisGene Expression Regulation, BacterialMembrane ProteinsMuramidaseProprotein ConvertasesSerine EndopeptidasesSigma FactorBacterial ProteinsEndopeptidaseshen egg lysozymemembrane-bound transcription factor peptidase, site 1Membrane ProteinsMuramidasemutanolysinProprotein ConvertasesSerine EndopeptidasesSigma Factortype I signal peptidase

Identifiers

PMID25275625
PMCPMC4183432
OpenAlexW2029744830

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.