Evidence map›Paper›PMID 25491472›Full record

ArticleMolecular microbiology2015

Identification of the amino acids essential for LytSR-mediated signal transduction in Staphylococcus aureus and their roles in biofilm-specific gene expression.

McKenzie K Lehman, Jeffrey L Bose, Batu K Sharma-Kuinkel, Derek E Moormeier, Jennifer L Endres, Marat R Sadykov, Indranil Biswas, Kenneth W Bayles

Abstract read
In one paragraph

Article in Molecular microbiology, 2015. 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
–field-weighted citation impact
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.

  1. Global Transcriptional Differences inAntibiotics (Basel, Switzerland) · 2026
    Article
  2. Characterization ofBiofilm · 2025
    Article
  3. Characterizing theJournal of bacteriology · 2025
    Article
  4. YjbH contributes toVirulence · 2024
    Article
  5. First whole genome sequencing ofOpen veterinary journal · 2024
    Article
  6. Article
  7. A Review of Biofilm Formation ofAntibiotics (Basel, Switzerland) · 2022
    Review
  8. Review
  9. Article
  10. Bacterial Protein Kinases.Advances in experimental medicine and biology · 2021
    Article
  11. Staphylococcal Biofilm Development: Structure, Regulation, and Treatment Strategies.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Transcriptomic Adjustments ofFrontiers in microbiology · 2019
    Article
  19. Article
  20. Review
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

8 authors.

McKenzie K LehmanDepartment of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE, 68198, USA.
Jeffrey L Bose
Batu K Sharma-Kuinkel
Derek E Moormeier
Jennifer L Endres
Marat R Sadykov
Indranil Biswas
Kenneth W Bayles

Funding

The S. aureus biofilm lifecycleP01AI083211 · NIAID · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI BAYLES, KENNETH W. · 2009 to 2023
$32.1M
The molecular control of bacterial autolysisR01AI038901 · NIAID · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI BAYLES, KENNETH W. · 2003 to 2012
$3.1M
NIAID NIH HHS P01 AI083211NIAID NIH HHS P01-AI83211NIAID NIH HHS R01 AI038901NIAID NIH HHS R01-AI038901
6 · The paper itself

Abstract

Recent studies have demonstrated that expression of the Staphylococcus aureus lrgAB operon is specifically localized within tower structures during biofilm development. To gain a better understanding of the mechanisms underlying this spatial control of lrgAB expression, we carried out a detailed analysis of the LytSR two-component system. Specifically, a conserved aspartic acid (Asp53) of the LytR response regulator was shown to be the target of phosphorylation, which resulted in enhanced binding to the lrgAB promoter and activation of transcription. In addition, we identified His390 of the LytS histidine kinase as the site of autophosphorylation and Asn394 as a critical amino acid involved in phosphatase activity. Interestingly, LytS-independent activation of LytR was observed during planktonic growth, with acetyl phosphate acting as a phosphodonor to LytR. In contrast, mutations disrupting the function of LytS prevented tower-specific lrgAB expression, providing insight into the physiologic environment within these structures. In addition, overactivation of LytR led to increased lrgAB promoter activity during planktonic and biofilm growth and a change in biofilm morphology. Overall, the results of this study are the first to define the LytSR signal transduction pathway, as well as determine the metabolic context within biofilm tower structures that triggers these signaling events.

Indexed as

Signal TransductionAmino AcidsAspartic AcidBacterial ProteinsBiofilmsGene ExpressionGene Expression Regulation, BacterialOperonPoint MutationPromoter Regions, GeneticStaphylococcus aureusTranscription FactorsTranscription, GeneticAmino AcidsAspartic AcidBacterial ProteinsLytR protein, Staphylococcus aureusLytS protein, Staphylococcus aureusTranscription Factors

Identifiers

PMID25491472
PMCPMC4347461

What OpenQuestion holds

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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.