ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2017
Structural characterization of the DNA-binding mechanism underlying the copper(II)-sensing MarR transcriptional regulator.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 30 citations in OpenAlex.
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Development of anBiosensors · 2024Article
- Biophysical and Biochemical Characterization of the Binding of the MarR-like Transcriptional Regulator Saro_0803 to theBiomolecules · 2023Article
- Diverse MarR bacterial regulators of auxin catabolism in the plant microbiome.Nature microbiology · 2022Article
- Identification of a MarR Subfamily That Regulates Arsenic Resistance Genes.Applied and environmental microbiology · 2021Article
- Exploring the Tunability and Dynamic Properties of MarR-PmarO Sensor System inACS synthetic biology · 2021Article
- Article
- The evolution of MarR family transcription factors as counter-silencers in regulatory networks.Current opinion in microbiology · 2020Review
- Article
- Structural mechanism for regulation of DNA binding of BpsR, a Bordetella regulator of biofilm formation, by 6-hydroxynicotinic acid.PloS one · 2019Article
- Tuning site-specific dynamics to drive allosteric activation in a pneumococcal zinc uptake regulator.eLife · 2018Article
- Comparative genetic and genomic analysis of the novel fusellovirus Sulfolobus spindle-shaped virus 10.Virus evolution · 2018Article
- Regulation of Metabolic Pathways by MarR Family Transcription Factors.Computational and structural biotechnology journal · 2017Review
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8 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Multiple antibiotic resistance regulator (MarR) family proteins are widely conserved transcription factors that control bacterial resistance to antibiotics, environmental stresses, as well as the regulation of virulence determinants. Escherichia coli MarR, the prototype member of this family, has recently been shown to undergo copper(II)-catalyzed inter-dimer disulfide bond formation via a unique cysteine residue (Cys80) residing in its DNA-binding domain. However, despite extensive structural characterization of the MarR family proteins, the structural mechanism for DNA binding of this copper(II)-sensing MarR factor remains elusive. Here, we report the crystal structures of DNA-bound forms of MarR, which revealed a unique, concerted generation of two new helix-loop-helix motifs that facilitated MarR's DNA binding. Structural analysis and electrophoretic mobility shift assays (EMSA) show that the flexibility of Gly116 in the center of helix α5 and the extensive hydrogen-bonding interactions at the N-terminus of helix α1 together assist the reorientation of the wHTH domains and stabilize MarR's DNA-bound conformation.
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