ArticleNucleic acids research2015
Structural basis of the mercury(II)-mediated conformational switching of the dual-function transcriptional regulator MerR.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 77 citations in OpenAlex.
- Core elements play distinct roles in promoter birth and transcriptional regulation.Nature communications · 2026Article
- Lithium-selective supramolecular assembly and capture by tripeptide gelators.Chemical science · 2026Article
- MerR-type regulator ZccR links zinc homeostasis to biofilm formation and interspecies competition inFrontiers in cellular and infection microbiology · 2026Article
- Metals in Motion: Understanding Labile Metal Pools in Bacteria.Biochemistry · 2025Review
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- AsJournal of the American Chemical Society · 2024Article
- Determinants ofGenes · 2024Article
- The Copper Efflux Regulator (CueR).Sub-cellular biochemistry · 2024Review
- Chimeric MerR-Family Regulators and Logic Elements for the Design of Metal Sensitive Genetic Circuits inACS synthetic biology · 2023Article
- CvkR is a MerR-type transcriptional repressor of class 2 type V-K CRISPR-associated transposase systems.Nature communications · 2023Article
- Metabolic engineering of the carotenoid biosynthetic pathway toward a specific and sensitive inorganic mercury biosensor.RSC advances · 2022Article
- The protein scaffold calibrates metal specificity and activation in MerR sensors.Microbial biotechnology · 2022Article
- Identification of a Bile Acid-Binding Transcription Factor inACS chemical biology · 2022Article
- Involvement of BldC in the Formation of Physiologically Mature Sporangium in Actinoplanes missouriensis.Journal of bacteriology · 2022Article
- Bacterial Multidrug Efflux Pumps at the Frontline of Antimicrobial Resistance: An Overview.Antibiotics (Basel, Switzerland) · 2022Review
- Bacterial MerR family transcription regulators: activationby distortion.Acta biochimica et biophysica Sinica · 2022Review
- Development of a bioavailable Hg(II) sensing system based on MerR-regulated visual pigment biosynthesis.Scientific reports · 2021Article
- New Insights into Alterations in PL Proteins Affecting Their Binding to DNA after Exposure ofInternational journal of molecular sciences · 2021Article
- Light-Triggered Carotenogenesis inMicroorganisms · 2021Review
- Potential Whole-Cell Biosensors for Detection of Metal Using MerR Family Proteins fromMicromachines · 2021Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mer operon confers bacterial resistance to inorganic mercury (Hg(2+)) and organomercurials by encoding proteins involved in sensing, transport and detoxification of these cytotoxic agents. Expression of the mer operon is under tight control by the dual-function transcriptional regulator MerR. The metal-free, apo MerR binds to the mer operator/promoter region as a repressor to block transcription initiation, but is converted into an activator upon Hg(2+)-binding. To understand how MerR interacts with Hg(2+) and how Hg(2+)-binding modulates MerR function, we report here the crystal structures of apo and Hg(2+)-bound MerR from Bacillus megaterium, corresponding respectively to the repressor and activator conformation of MerR. To our knowledge, the apo-MerR structure represents the first visualization of a MerR family member in its intact and inducer-free form. And the Hg(2+)-MerR structure offers the first view of a triligated Hg(2+)-thiolate center in a metalloprotein, confirming that MerR binds Hg(2+) via trigonal planar coordination geometry. Structural comparison revealed the conformational transition of MerR is coupled to the assembly/disassembly of a buried Hg(2+) binding site, thereby providing a structural basis for the Hg(2+)-mediated functional switching of MerR. The pronounced Hg(2+)-induced repositioning of the MerR DNA-binding domains suggests a plausible mechanism for the transcriptional regulation of the mer operon.
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