ArticleNucleic acids research2021
BusR senses bipartite DNA binding motifs by a unique molecular ruler architecture.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Elucidation of the structure and molecular mechanisms of the aspartate antiporter.Communications biology · 2025Article
- Activation of a Secondary-Messenger Receptor via Allosteric Modulation of a Dynamic Conformational Ensemble.Angewandte Chemie (International ed. in English) · 2025Article
- MexR and NalD are pyocyanin-responsive transcriptional repressors of the efflux pump MexAB-OprM in Pseudomonas aeruginosa.Nucleic acids research · 2025Article
- Coordinated regulation of osmotic imbalance by c-di-AMP shapes ß-lactam tolerance in Group BmicroLife · 2024Article
- Structures of the DarR transcription regulator reveal unique modes of second messenger and DNA binding.Nature communications · 2023Article
- Brewing COFFEE: A sequence-specific coarse-grained energy function for simulations of DNA-protein complexes.bioRxiv : the preprint server for biology · 2023Article
- Article
- The many roles of cyclic di-AMP to control the physiology ofmicroLife · 2023Review
- Cyclic di-AMP, a multifaceted regulator of central metabolism and osmolyte homeostasis inmicroLife · 2023Review
- Recent advances and perspectives in nucleotide second messenger signaling in bacteria.microLife · 2023Review
- PmiR senses 2-methylisocitrate levels to regulate bacterial virulence inScience advances · 2022Article
- Using cryo-EM to uncover mechanisms of bacterial transcriptional regulation.Biochemical Society transactions · 2021Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cyclic dinucleotide second messenger c-di-AMP is a major player in regulation of potassium homeostasis and osmolyte transport in a variety of bacteria. Along with various direct interactions with proteins such as potassium channels, the second messenger also specifically binds to transcription factors, thereby altering the processes in the cell on the transcriptional level. We here describe the structural and biochemical characterization of BusR from the human pathogen Streptococcus agalactiae. BusR is a member of a yet structurally uncharacterized subfamily of the GntR family of transcription factors that downregulates transcription of the genes for the BusA (OpuA) glycine-betaine transporter upon c-di-AMP binding. We report crystal structures of full-length BusR, its apo and c-di-AMP bound effector domain, as well as cryo-EM structures of BusR bound to its operator DNA. Our structural data, supported by biochemical and biophysical data, reveal that BusR utilizes a unique domain assembly with a tetrameric coiled-coil in between the binding platforms, serving as a molecular ruler to specifically recognize a 22 bp separated bipartite binding motif. Binding of c-di-AMP to BusR induces a shift in equilibrium from an inactivated towards an activated state that allows BusR to bind the target DNA, leading to transcriptional repression.
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