ArticleNucleic acids research2019
Deciphering the activation and recognition mechanisms of Staphylococcus aureus response regulator ArlR.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 40 citations in OpenAlex.
- Article
- Subtractive proteomics-driven identification of AgrA and structure-guided discovery of phytochemical and marine natural products as novel anti-quorum sensing therapeutic leads against Enterococcus faecium.Molecular diversity · 2026Article
- ArlR regulates environmental stress tolerance and biofilm formation in foodborneCurrent research in food science · 2026Article
- Potential Natural Inhibitors of MRSA ABC Transporters and MecA Identified Through In Silico Approaches.Microorganisms · 2025Article
- The Functional Study of Response Regulator ArlR Mutants in Staphylococcus Aureus.Applied biochemistry and biotechnology · 2024Article
- Identification and experimental verification of senescence-related gene signatures and molecular subtypes in idiopathic pulmonary arterial hypertension.Scientific reports · 2024Article
- Structural and functional insights underlying recognition of histidine phosphotransfer protein in fungal phosphorelay systems.Communications biology · 2024Article
- Residue coevolution and mutational landscape for OmpR and NarL response regulator subfamilies.Biophysical journal · 2024Article
- Mechanistic and biophysical characterization of polymyxin resistance response regulator PmrA inFrontiers in microbiology · 2024Article
- MP4: a machine learning based classification tool for prediction and functional annotation of pathogenic proteins from metagenomic and genomic datasets.BMC bioinformatics · 2022Article
- Therapeutic Inhibition of Staphylococcus aureus ArlRS Two-Component Regulatory System Blocks Virulence.Antimicrobial agents and chemotherapy · 2022Article
- Experimental Polymorphism Survey in Intergenic Regions of theMicroorganisms · 2022Article
- Structure of the Acinetobacter baumannii PmrA receiver domain and insights into clinical mutants affecting DNA binding and promoting colistin resistance.Journal of biochemistry · 2022Article
- Metagenomics Versus Metatranscriptomics of the Murine Gut Microbiome for Assessing Microbial Metabolism During Inflammation.Frontiers in microbiology · 2022Article
- The Role ofAntibiotics (Basel, Switzerland) · 2021Review
- Proteolysis and multimerization regulate signaling along the two-component regulatory system AdeRS.iScience · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcus aureus ArlRS is a key two-component regulatory system necessary for adhesion, biofilm formation, and virulence. The response regulator ArlR consists of a C-terminal DNA-binding effector domain and an N-terminal receiver domain that is phosphorylated by ArlS, the cognate transmembrane sensor histidine kinase. We demonstrate that the receiver domain of ArlR adopts the canonical α5β5 response regulator assembly, which dimerizes upon activation, using beryllium trifluoride as an aspartate phosphorylation mimic. Activated ArlR recognizes a 20-bp imperfect inverted repeat sequence in the ica operon, which is involved in intercellular adhesion polysaccharide production. Crystal structures of the inactive and activated forms reveal that activation induces a significant conformational change in the β4-α4 and β5-α5-connecting loops, in which the α4 and α5 helices constitute the homodimerization interface. Crystal structures of the DNA-binding ArlR effector domain indicate that it is able to dimerize via a non-canonical β1-β2 hairpin domain swapping, raising the possibility of a new mechanism for signal transduction from the receiver domain to effector domain. Taken together, the current study provides structural insights into the activation of ArlR and its recognition, adding to the diversity of response regulation mechanisms that may inspire novel antimicrobial strategies specifically targeting Staphylococcus.
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.