ArticleNature communications2023
Structures of the DarR transcription regulator reveal unique modes of second messenger and DNA binding.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Regulatory cascade of NdpR and NdpR2 in controlling nicotine degradation operons inApplied and environmental microbiology · 2026Article
- Article
- Molecular basis of antibiotic sensing by the TetR family regulator CecR - a structural perspective.The FEBS journal · 2026Article
- Molecular basis for the transcriptional regulation of an epoxide-based virulence circuit in Pseudomonas aeruginosa.Nucleic acids research · 2024Article
- Molecular basis for the transcriptional regulation of an epoxide-based virulence circuit inbioRxiv : the preprint server for biology · 2024Article
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4 authors at 1 institution in 1 country.
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Abstract
The mycobacterial repressor, DarR, a TetR family regulator (TFR), was the first transcription regulator shown to bind c-di-AMP. However, the molecular basis for this interaction and the mechanism involved in DNA binding by DarR remain unknown. Here we describe DarR-c-di-AMP and DarR-DNA structures and complementary biochemical assays. The DarR-c-di-AMP structure reveals a unique effector binding site for a TFR, located between DarR dimer subunits. Strikingly, we show this motif also binds cAMP. The location of the adenine nucleotide binding site between subunits suggests this interaction may facilitate dimerization and hence DNA binding. Indeed, biochemical assays show cAMP enhances DarR DNA binding. Finally, DarR-DNA structures reveal a distinct TFR DNA-binding mechanism involving two interacting dimers on the DNA. Thus, the combined data unveil a newly described second messenger binding motif and DNA binding mode for this important family of regulators.
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