ArticleNature communications2015
Structure and dynamics of polymyxin-resistance-associated response regulator PmrA in complex with promoter DNA.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 59 citations in OpenAlex.
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- A lignan compound regulates LPS modifications via PmrA/B signaling cascades to potentiate colistin efficacy in vivo.PLoS pathogens · 2025Article
- PmrA Mutations in Drug-ResistantMicroorganisms · 2025Article
- Combatting Antibiotic-ResistantJournal of chemical information and modeling · 2024Article
- Structural basis of DNA recognition of themBio · 2024Article
- Conserved patterns of sequence diversification provide insight into the evolution of two-component systems inMicrobial genomics · 2024Article
- Cross-regulation of Aps-promoters in Lacticaseibacillus paracasei by the PsdR response regulator in response to lantibiotics.Scientific reports · 2024Article
- Regulatory role ofFrontiers in microbiology · 2024Article
- Pseudomonas aeruginosa two-component system CprRS regulates HigBA expression and bacterial cytotoxicity in response to LL-37 stress.PLoS pathogens · 2024Article
- Mechanistic and biophysical characterization of polymyxin resistance response regulator PmrA inFrontiers in microbiology · 2024Article
- Structural basis of transcriptional activation by the OmpR/PhoB-family response regulator PmrA.Nucleic acids research · 2023Article
- Substrate DNA Promoting Binding ofMicroorganisms · 2023Article
- Structural insights into the transcription activation mechanism of the global regulator GlnR from actinobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Salmonella Subpopulations Identified from Human Specimens Express Heterogenous Phenotypes That Are Relevant to Clinical Diagnosis.Microbiology spectrum · 2023Article
- A Copper-Responsive Two-Component System Governs Lipoprotein Remodeling in Listeria monocytogenes.Journal of bacteriology · 2023Article
- Structural basis of phosphorylation-induced activation of the response regulator VbrR.Acta biochimica et biophysica Sinica · 2023Article
- Real-time detection of response regulator phosphorylation dynamics in live bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- CovS inactivation reduces CovR promoter binding at diverse virulence factor encoding genes in group A Streptococcus.PLoS pathogens · 2022Article
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PmrA, an OmpR/PhoB family response regulator, manages genes for antibiotic resistance. Phosphorylation of OmpR/PhoB response regulator induces the formation of a symmetric dimer in the N-terminal receiver domain (REC), promoting two C-terminal DNA-binding domains (DBDs) to recognize promoter DNA to elicit adaptive responses. Recently, determination of the KdpE-DNA complex structure revealed an REC-DBD interface in the upstream protomer that may be necessary for transcription activation. Here, we report the 3.2-Å-resolution crystal structure of the PmrA-DNA complex, which reveals a similar yet different REC-DBD interface. However, NMR studies show that in the DNA-bound state, two domains tumble separately and an REC-DBD interaction is transiently populated in solution. Reporter gene analyses of PmrA variants with altered interface residues suggest that the interface is not crucial for supporting gene expression. We propose that REC-DBD interdomain dynamics and the DBD-DBD interface help PmrA interact with RNA polymerase holoenzyme to activate downstream gene transcription.
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