ArticleScientific reports2017
Dynamic equilibrium on DNA defines transcriptional regulation of a multidrug binding transcriptional repressor, LmrR.
Article in Scientific reports, 2017. 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, 9 citations in OpenAlex.
- Activity-Enhancing Mutations in an LmrR-Based Artificial Metalloenzyme Destabilize the Protein Scaffold and Alter its Conformational Plasticity.Chembiochem : a European journal of chemical biology · 2025Article
- Computation-guided engineering of distal mutations in an artificial enzyme.Faraday discussions · 2024Article
- In Vivo Assembly of Artificial Metalloenzymes and Application in Whole-Cell Biocatalysis*.Angewandte Chemie (International ed. in English) · 2021Article
- Structural equilibrium underlying ligand-dependent activation of βNature chemical biology · 2020Article
- Conformational equilibrium defines the variable induction of the multidrug-binding transcriptional repressor QacR.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- NMR-based investigations into target DNA search processes of proteins.Methods (San Diego, Calif.) · 2018Review
- Single-round isolation of diverse RNA aptamers from a random sequence pool.Biology methods & protocols · 2018Article
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LmrR is a multidrug binding transcriptional repressor that controls the expression of a major multidrug transporter, LmrCD, in Lactococcus lactis. Promiscuous compound ligations reduce the affinity of LmrR for the lmrCD operator by several fold to release the transcriptional repression; however, the affinity reduction is orders of magnitude smaller than that of typical transcriptional repressors. Here, we found that the transcriptional regulation of LmrR is achieved through an equilibrium between the operator-bound and non-specific DNA-adsorption states in vivo. The effective dissociation constant of LmrR for the lmrCD operator under the equilibrium is close to the endogenous concentration of LmrR, which allows a substantial reduction of LmrR occupancy upon compound ligations. Therefore, LmrR represents a dynamic type of transcriptional regulation of prokaryotic multidrug resistance systems, where the small affinity reduction induced by compounds is coupled to the functional relocalization of the repressor on the genomic DNA via nonspecific DNA adsorption.
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