ArticleNucleic acids research2017
Mechanistic insight into how multidrug resistant Acinetobacter baumannii response regulator AdeR recognizes an intercistronic region.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 32 citations in OpenAlex.
- Previously Uncharacterised Aliphatic Amino Acid Positions Modulate the Apparent Catalytic Activity of the EAL Domain of ZMO_1055 and Other Cyclic Di-GMP-Specific EAL Phosphodiesterases.Microbial biotechnology · 2026Article
- Mutations in two-component signaling systems drive experimental evolution of tigecycline and colistin resistance inAntimicrobial agents and chemotherapy · 2025Article
- Two-Component System Sensor Kinase Inhibitors Target the ATP-Lid of PmrB to Disrupt Colistin Resistance inBiochemistry · 2025Article
- Targeting Acinetobacter baumannii resistance-nodulation-division efflux pump transcriptional regulators to combat antimicrobial resistance.npj antimicrobials and resistance · 2025Review
- AdeABC, AdeFGH, and AdeIJK efflux pumps as key factors in tigecycline resistance of Acinetobacter baumannii: a study from Western Balkan hospitals.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025Article
- Mechanistic and biophysical characterization of polymyxin resistance response regulator PmrA inFrontiers in microbiology · 2024Article
- Gram-negative bacteria resist antimicrobial agents by a DzrR-mediated envelope stress response.BMC biology · 2023Article
- The novel two-component system AmsSR governs alternative metabolic pathway usage inFrontiers in microbiology · 2023Article
- Article
- Proteolysis and multimerization regulate signaling along the two-component regulatory system AdeRS.iScience · 2021Article
- Metal-induced sensor mobilization turns on affinity to activate regulator for metal detoxification in live bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Deciphering the activation and recognition mechanisms of Staphylococcus aureus response regulator ArlR.Nucleic acids research · 2019Article
- Over-Expression of ISFrontiers in microbiology · 2019Article
- Genetic characterization andOncology letters · 2018Article
- Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
AdeR-AdeS is a two-component regulatory system, which controls expression of the adeABC efflux pump involved in Acinetobacter baumannii multidrug resistance. AdeR is a response regulator consisting of an N-terminal receiver domain and a C-terminal DNA-binding-domain. AdeR binds to a direct-repeat DNA in the intercistronic region between adeR and adeABC. We demonstrate a markedly high affinity binding between unphosphorylated AdeR and DNA with a dissociation constant of 20 nM. In addition, we provide a 2.75 Å crystal structure of AdeR DNA-binding-domain complexed with the intercistronic DNA. This structure shows that the α3 and β hairpin formed by β5-β6 interacts with the major and minor groove of the DNA, which in turn leads to the introduction of a bend. The AdeR receiver domain structure revealed a dimerization motif mediated by a gearwheel-like structure involving the D108F109-R122 motif through cation π stack interaction. The structure of AdeR receiver domain bound with magnesium indicated a conserved Glu19Asp20-Asp63 magnesium-binding motif, and revealed that the potential phosphorylation site Asp63OD1 forms a hydrogen bond with Lys112. We thus dissected the mechanism of how AdeR recognizes the intercistronic DNA, which leads to a diverse mode of response regulation. Unlocking the AdeRS mechanism provides ways to circumvent A. baumannii antibiotic resistance.
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