ArticleBiochemistry2009
Characterization and structure of the manganese-responsive transcriptional regulator ScaR.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
32 citing papers in PubMed, 52 citations in OpenAlex.
- Structural basis for transcription activation through cooperative recruitment of MntR.Nature communications · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- AsJournal of the American Chemical Society · 2024Article
- Structural Dynamics of theInternational journal of molecular sciences · 2023Article
- Managing Manganese: The Role of Manganese Homeostasis in Streptococcal Pathogenesis.Frontiers in cell and developmental biology · 2022Review
- TroR Negatively Regulates the TroABCD System and Is Required for Resistance to Metal Toxicity and Virulence in Streptococcus suis.Applied and environmental microbiology · 2021Article
- Metal sensing and regulation of adaptive responses to manganese limitation by MtsR is critical for group A streptococcus virulence.Nucleic acids research · 2019Article
- Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species.FEMS microbiology reviews · 2019Review
- Autoregulation of the Streptococcus mutans SloR Metalloregulator Is Constitutive and Driven by an Independent Promoter.Journal of bacteriology · 2018Article
- Metallochaperones and metalloregulation in bacteria.Essays in biochemistry · 2017Review
- Molecular Insights into Hydrogen Peroxide-sensing Mechanism of the Metalloregulator MntR in Controlling Bacterial Resistance to Oxidative Stresses.The Journal of biological chemistry · 2017Article
- Stress Physiology of Lactic Acid Bacteria.Microbiology and molecular biology reviews : MMBR · 2016Review
- Characterisation of the Porphyromonas gingivalis Manganese Transport Regulator Orthologue.PloS one · 2016Article
- Interactions of the Metalloregulatory Protein SloR from Streptococcus mutans with Its Metal Ion Effectors and DNA Binding Site.Journal of bacteriology · 2015Article
- Comparative genomics of DtxR family regulons for metal homeostasis in Archaea.Journal of bacteriology · 2015Article
- Transcription factor-based biosensors enlightened by the analyte.Frontiers in microbiology · 2015Review
- Specificity of metal sensing: iron and manganese homeostasis in Bacillus subtilis.The Journal of biological chemistry · 2014Review
- Structure solution of DNA-binding proteins and complexes with ARCIMBOLDO libraries.Acta crystallographica. Section D, Biological crystallography · 2014Article
- A role for the DtxR family of metalloregulators in gram-positive pathogenesis.Molecular oral microbiology · 2014Review
- Physical characterization of the manganese-sensing pneumococcal surface antigen repressor from Streptococcus pneumoniae.Biochemistry · 2013Article
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 1 country.
Funding
Abstract
The streptococcal coaggregation regulator (ScaR) of Streptococcus gordonii is a manganese-dependent transcriptional regulator. When intracellular manganese concentrations become elevated, ScaR represses transcription of the scaCBA operon, which encodes a manganese uptake transporter. A member of the DtxR/MntR family of metalloregulators, ScaR shares sequence similarity with other family members, and many metal-binding residues are conserved. Here, we show that ScaR is an active dimer, with two dimers binding the 46 base pair scaC operator. Each ScaR subunit binds two manganese ions, and the protein is activated by a variety of other metal ions, including Cd(2+), Co(2+), and Ni(2+) but not Zn(2+). The crystal structure of apo-ScaR reveals a tertiary and quaternary structure similar to its homologue, the iron-responsive regulator DtxR. While each DtxR subunit binds a metal ion in two sites, labeled primary and ancillary, crystal structures of ScaR determined in the presence of Cd(2+) and Zn(2+) show only a single occupied metal-binding site that is novel to ScaR. The site analogous to the primary site in DtxR is unoccupied, and the ancillary site is absent from ScaR. Instead, metal ions bind to ScaR at a site labeled "secondary", which is composed of Glu80, Cys123, His125, and Asp160 and lies roughly 5 A away from where the ancillary site would be predicted to exist. This difference suggests that ScaR and its closely related homologues are activated by a mechanism distinct from that of either DtxR or MntR.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.