Evidence map›Paper›PMID 27283781›Full record

ReviewJournal of molecular biology2016

Structural Mechanisms of Peptide Recognition and Allosteric Modulation of Gene Regulation by the RRNPP Family of Quorum-Sensing Regulators.

Hackwon Do, Muthiah Kumaraswami

Abstract readReview
In one paragraph

Review in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.1field-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

34 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. PepO and CppA modulateVirulence · 2023
    Article
  6. Article
  7. RopB represses the transcription ofLife science alliance · 2023
    Article
  8. Article
  9. Streptococcal peptides and their roles in host-microbe interactions.Frontiers in cellular and infection microbiology · 2023
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Peptide-based quorum sensing systems inLife science alliance · 2020
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  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

2 authors at 1 institution in 1 country.

Hackwon DoCenter for Molecular and Translational Human Infectious Diseases Research, Houston Methodist Hospital Research Institute, and Department of Pathology and Genomic Medicine, Houston Methodist Hospital System, Houston, TX, 77030, USA.
Muthiah KumaraswamiCenter for Molecular and Translational Human Infectious Diseases Research, Houston Methodist Hospital Research Institute, and Department of Pathology and Genomic Medicine, Houston Methodist Hospital System, Houston, TX, 77030, USA. Electronic address: mkumaraswami@houstonmethodist.org.
Houston Methodist · US

Funding

Molecular mechanism of virulence regulation in Streptococcus pyogenesR01AI109096 · NIAID · METHODIST HOSPITAL RESEARCH INSTITUTE · PI KUMARASWAMI, MUTHIAH · 2015 to 2019
$2.0M
NIAID NIH HHS R01 AI109096
6 · The paper itself

Abstract

The members of RRNPP family of bacterial regulators sense population density-specific secreted oligopeptides and modulate the expression of genes involved in cellular processes, such as sporulation, competence, virulence, biofilm formation, conjugative plasmid transfer and antibiotic resistance. Signaling by RRNPP regulators include several steps: generation and secretion of the signaling oligopeptides, re-internalization of the signaling molecules into the cytoplasm, signal sensing by the cytosolic RRNPP regulators, signal-specific allosteric structural changes in the regulators, and interaction of the regulators with their respective regulatory target and gene regulation. The recently determined structures of the RRNPP regulators provide insight into the mechanistic aspects for several steps in this signaling circuit. In this review, we discuss the structural principles underlying peptide specificity, regulatory target recognition, and ligand-induced allostery in RRNPP regulators and its impact on gene regulation. Despite the conserved tertiary structure of these regulators, structural analyses revealed unexpected diversity in the mechanism of activation and molecular strategies that couple the peptide-induced allostery to gene regulation. Although these structural studies provide a sophisticated understanding of gene regulation by RRNPP regulators, much needs to be learned regarding the target DNA binding by yet-to-be characterized RNPP regulators and the several aspects of signaling by Rgg regulators.

Indexed as

Allosteric RegulationBacterial ProteinsGene Expression Regulation, BacterialPeptidesQuorum SensingSignal TransductionVirulenceBacterial ProteinsPeptidesallosterygene regulationpeptide signalingRRNPP familystructural mechanisms

Identifiers

PMID27283781
PMCPMC4938729
OpenAlexW2413666049

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.