ArticleNucleic acids research2013
Peptide-binding dependent conformational changes regulate the transcriptional activity of the quorum-sensor NprR.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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.
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.
Who cites it
34 citing papers in PubMed.
- Review
- High-resolution visualization of biofilm matrix development in space and time using fluorescent stains for cellulose.NPJ biofilms and microbiomes · 2026Article
- Bacterial quorum-sensing systems in cell-cell communication.FEMS microbiology reviews · 2026Review
- RRNPP quorum-sensing repertoires in the salivarius group genomes: overrepresentation and synchronous activation of SHP/Rgg systems inJournal of bacteriology · 2025Article
- Targeting Peptide-Based Quorum Sensing Systems for the Treatment of Gram-Positive Bacterial Infections.Peptide science (Hoboken, N.J.) · 2023Article
- Development and utilization of peptide-based quorum sensing modulators in Gram-positive bacteria.Organic & biomolecular chemistry · 2020Review
- Rap-Phr Systems from Plasmids pAW63 and pHT8-1 Act Together To Regulate Sporulation in the Bacillus thuringiensis Serovar kurstaki HD73 Strain.Applied and environmental microbiology · 2020Article
- Inactivation of the dimeric RappLS20 anti-repressor of the conjugation operon is mediated by peptide-induced tetramerization.Nucleic acids research · 2020Article
- Multiple and Overlapping Functions of Quorum Sensing Proteins for Cell Specialization inJournal of bacteriology · 2020Review
- Quorum sensing for population-level control of bacteria and potential therapeutic applications.Cellular and molecular life sciences : CMLS · 2020Review
- Ratiometric population sensing by a pump-probe signaling system in Bacillus subtilis.Nature communications · 2020Article
- Integrated Transcriptomic and Proteomic Analyses Reveal the Role of NprR inFrontiers in microbiology · 2020Article
- Article
- TheMicrobiology spectrum · 2019Review
- Deciphering the Molecular Mechanism Underpinning Phage Arbitrium Communication Systems.Molecular cell · 2019Article
- Article
- Structural insights into DNA recognition by AimR of the arbitrium communication system in the SPbeta phage.Cell discovery · 2019Article
- Structural basis of the arbitrium peptide-AimR communication system in the phage lysis-lysogeny decision.Nature microbiology · 2018Article
- Genetic and Structural Analyses of RRNPP Intercellular Peptide Signaling of Gram-Positive Bacteria.Annual review of genetics · 2017Review
- Structural analyses of theThe Journal of biological chemistry · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transcriptional regulator NprR controls the expression of genes essential for the adaptative response of Bacillus cereus. NprR belongs to the RNPP family of directly regulated quorum sensors from Gram-positive bacteria. It is activated by the re-imported signaling peptide NprX. To elucidate the activation mechanism of this quorum-sensing system, we analyzed the conformation changes induced on binding of NprX. We solved the crystal structure of the NprR/NprX binary complex and characterized the apo form of NprR in solution. We demonstrated that apo NprR is a dimer that switches to a tetramer in the presence of NprX. Mutagenesis, and functional analysis allowed us to identify the protein and peptide residues directly involved in the NprR activation process. Based on the comparison with the Rap proteins, we propose a model for the peptide-induced conformational change allowing the apo dimer to switch to an active tetramer specifically recognizing target DNA sequences.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.