ArticlePloS one2015
Molecular Binding Mechanism of TtgR Repressor to Antibiotics and Antimicrobials.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Engineering rhizobacterial communities for soil and plant health.Microbiology (Reading, England) · 2026Review
- Engineered TtgR-Based Whole-Cell Biosensors for Quantitative and Selective Monitoring of Bioactive Compounds.Biosensors · 2025Article
- The Impact of Plant-Derived Polyphenols on Combating Efflux-Mediated Antibiotic Resistance.International journal of molecular sciences · 2025Review
- Highly multiplexed design of an allosteric transcription factor to sense new ligands.Nature communications · 2024Article
- Adsorption of Flavonoids in a Transcriptional Regulator TtgR: Relative Binding Free Energies and Intermolecular Interactions.The journal of physical chemistry. B · 2024Article
- RND Efflux Pump Induction: A Crucial Network Unveiling Adaptive Antibiotic Resistance Mechanisms of Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2024Review
- Highly multiplexed design of an allosteric transcription factor to sense novel ligands.bioRxiv : the preprint server for biology · 2024Article
- Quantum biochemical analysis of the TtgR regulator and effectors.Scientific reports · 2024Article
- What Approaches to Thwart Bacterial Efflux Pumps-Mediated Resistance?Antibiotics (Basel, Switzerland) · 2022Review
- A new quinolinone-chalcone hybrid with potential antibacterial and herbicidal properties using in silico approaches.Journal of molecular modeling · 2022Article
- Bacterial Multidrug Efflux Pumps at the Frontline of Antimicrobial Resistance: An Overview.Antibiotics (Basel, Switzerland) · 2022Review
- Engineering genetic devices for in vivo control of therapeutic T cell activity triggered by the dietary molecule resveratrol.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structures of Neisseria gonorrhoeae MtrR-operator complexes reveal molecular mechanisms of DNA recognition and antibiotic resistance-conferring clinical mutations.Nucleic acids research · 2021Article
- Predicting DNA binding protein-drug interactions based on network similarity.BMC bioinformatics · 2020Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A disturbing phenomenon in contemporary medicine is the prevalence of multidrug-resistant pathogenic bacteria. Efflux pumps contribute strongly to this antimicrobial drug resistance, which leads to the subsequent failure of clinical treatments. The TtgR protein of Pseudomonas putida is a HTH-type transcriptional repressor that controls expression of the TtgABC efflux pump, which is the main contributor to resistance against several antimicrobials and toxic compounds in this microbe. One of the main strategies to modulate the bacterial resistance is the rational modification of the ligand binding target site. We report the design and characterization of four mutants-TtgRS77A, TtgRE78A, TtgRN110A and TtgRH114A - at the active ligand binding site. The biophysical characterization of the mutants, in the presence and in the absence of different antimicrobials, revealed that TtgRN110A is the variant with highest thermal stability, under any of the experimental conditions tested. EMSA experiments also showed a different dissociation pattern from the operator for TtgRN110A, in the presence of several antimicrobials, making it a key residue in the TtgR protein repression mechanism of the TtgABC efflux pump. We found that TtgRE78A stability is the most affected upon effector binding. We also probe that one mutation at the C-terminal half of helix-α4, TtgRS77A, provokes a severe protein structure distortion, demonstrating the important role of this residue in the overall protein structure and on the ligand binding site. The data provide new information and deepen the understanding of the TtgR-effector binding mechanism and consequently the TtgABC efflux pump regulation mechanism in Pseudomonas putida.
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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.