ArticlePloS one2012
Crystal structures of two transcriptional regulators from Bacillus cereus define the conserved structural features of a PadR subfamily.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 42 citations in OpenAlex.
- Research on Prophages in Aquaculture from the Perspective of Paradigm Borrowing: Advances in Pathogen Virulence, Antimicrobial Resistance, and Environmental Regulation.Microorganisms · 2026Review
- Unveiling Putative Functions of Burkholderia pseudomallei K96243 Hypothetical Proteins Via High-Throughput Characterization of Structural Similarities.Interdisciplinary sciences, computational life sciences · 2026Article
- Exploring PadR Proteins for Artificial Enzyme Design.Chembiochem : a European journal of chemical biology · 2026Article
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- A Genetic Locus inAntibiotics (Basel, Switzerland) · 2024Article
- Comparative Genomics of Marine Sponge-DerivedFrontiers in microbiology · 2019Article
- Article
- A designer enzyme for hydrazone and oxime formation featuring an unnatural catalytic aniline residue.Nature chemistry · 2018Article
- Structural basis of effector and operator recognition by the phenolic acid-responsive transcriptional regulator PadR.Nucleic acids research · 2017Article
- Transcriptional Repressor PtvR Regulates Phenotypic Tolerance to Vancomycin in Streptococcus pneumoniae.Journal of bacteriology · 2017Article
- Towards the complete proteinaceous regulome ofMicrobial genomics · 2017Article
- Crystal structure and DNA binding activity of a PadR family transcription regulator from hypervirulent Clostridium difficile R20291.BMC microbiology · 2016Article
- Increased acid resistance of the archaeon, Metallosphaera sedula by adaptive laboratory evolution.Journal of industrial microbiology & biotechnology · 2016Article
- Draft Genome Sequence of Streptomyces fradiae olg1-1, a Strain Resistant to Nitrone-Oligomycin.Genome announcements · 2015Article
- Structures of archaeal DNA segregation machinery reveal bacterial and eukaryotic linkages.Science (New York, N.Y.) · 2015Article
- Functional analysis of filipin tailoring genes from Streptomyces filipinensis reveals alternative routes in filipin III biosynthesis and yields bioactive derivatives.Microbial cell factories · 2015Article
- Mutations associated with reduced surotomycin susceptibility in Clostridium difficile and Enterococcus species.Antimicrobial agents and chemotherapy · 2015Article
- Transcriptional regulation of the vanillate utilization genes (vanABK Operon) of Corynebacterium glutamicum by VanR, a PadR-like repressor.Journal of bacteriology · 2015Article
- The PadR-like transcriptional regulator LftR ensures efficient invasion of Listeria monocytogenes into human host cells.Frontiers in microbiology · 2015Article
- In silico target fishing and pharmacological profiling for the isoquinoline alkaloids of Macleaya cordata (Bo Luo Hui).Chinese medicine · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PadR-like transcriptional regulators form a structurally-related family of proteins that control the expression of genes associated with detoxification, virulence and multi-drug resistance in bacteria. Only a few members of this family have been studied by genetic, biochemical and biophysical methods, and their structure/function relationships are still largely undefined. Here, we report the crystal structures of two PadR-like proteins from Bacillus cereus, which we named bcPadR1 and bcPadR2 (products of gene loci BC4206 and BCE3449 in strains ATCC 14579 and ATCC 10987, respectively). BC4206, together with its neighboring gene BC4207, was previously shown to become significantly upregulated in presence of the bacteriocin AS-48. DNA mobility shift assays reveal that bcPadR1 binds to a 250 bp intergenic region containing the putative BC4206-BC4207 promoter sequence, while in-situ expression of bcPadR1 decreases bacteriocin tolerance, together suggesting a role for bcPadR1 as repressor of BC4206-BC4207 transcription. The function of bcPadR2 (48% identical in sequence to bcPadR1) is unknown, but the location of its gene just upstream from genes encoding a putative antibiotic ABC efflux pump, suggests a role in regulating antibiotic resistance. The bcPadR proteins are structurally similar to LmrR, a PadR-like transcription regulator in Lactococcus lactis that controls expression of a multidrug ABC transporter via a mechanism of multidrug binding and induction. Together these proteins define a subfamily of conserved, relatively small PadR proteins characterized by a single C-terminal helix for dimerization. Unlike LmrR, bcPadR1 and bcPadR2 lack a central pore for ligand binding, making it unclear whether the transcriptional regulatory roles of bcPadR1 and bcPadR2 involve direct ligand recognition and induction.
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