ArticleNucleic acids research2023
Structural basis of transcriptional activation by the OmpR/PhoB-family response regulator PmrA.
Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- The response regulator BqsR/CarR controls FeNature communications · 2026Article
- Molecular basis of DosR-dependent transcription activation in Mycobacterium tuberculosis.Nature communications · 2026Article
- Orthogonal Biosynthesis of Pyrrolamides through Dehydration by a Pathway-Specific Glycoside Hydrolase-Like Enzyme in Gram-Positive Bacteria.Journal of the American Chemical Society · 2026Article
- Mechanism and reconstitution of circadian transcription in cyanobacteria.Nature structural & molecular biology · 2026Article
- PmrA Mutations in Drug-ResistantMicroorganisms · 2025Article
- Structural insights into transcription regulation of the global OmpR/PhoB family regulator PhoP from Mycobacterium tuberculosis.Nature communications · 2025Article
- ENcyclopedia of TRAnscription Factors in Bacteria and Archaea genomes (ENTRAF) version 2.0.Database : the journal of biological databases and curation · 2025Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
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Abstract
PmrA, an OmpR/PhoB-family response regulator, triggers gene transcription responsible for polymyxin resistance in bacteria by recognizing promoters where the canonical-35 element is replaced by the pmra-box, representing the PmrA recognition sequence. Here, we report a cryo-electron microscopy (cryo-EM) structure of a bacterial PmrA-dependent transcription activation complex (TAC) containing a PmrA dimer, an RNA polymerase σ70 holoenzyme (RNAPH) and the pbgP promoter DNA. Our structure reveals that the RNAPH mainly contacts the PmrA C-terminal DNA-binding domain (DBD) via electrostatic interactions and reorients the DBD three base pairs upstream of the pmra-box, resulting in a dynamic TAC conformation. In vivo assays show that the substitution of the DNA-recognition residue eliminated its transcriptional activity, while variants with altered RNAPH-interacting residues resulted in enhanced transcriptional activity. Our findings suggest that both PmrA recognition-induced DNA distortion and PmrA promoter escape play crucial roles in its transcriptional activation.
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