ArticleJournal of bacteriology2011
Genetic and biochemical analysis of PadR-padC promoter interactions during the phenolic acid stress response in Bacillus subtilis 168.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 47 citations in OpenAlex.
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- Establishing Tunable Genetic Logic Gates with Versatile Dynamic Performance by Varying Regulatory Parameters.ACS synthetic biology · 2023Article
- Identifying, Characterizing, and Engineering a Phenolic Acid-Responsive Transcriptional Factor fromACS synthetic biology · 2023Article
- Linocin M18 protein from the insect pathogenic bacterium Brevibacillus laterosporus isolates.Applied microbiology and biotechnology · 2023Article
- Revised Aspects into the Molecular Bases of Hydroxycinnamic Acid Metabolism in Lactobacilli.Antioxidants (Basel, Switzerland) · 2023Review
- Unveiling the complete genome sequence of Alicyclobacillus acidoterrestris DSM 3922T, a taint-producing strain.G3 (Bethesda, Md.) · 2022Article
- Harnessing plasmid replication mechanism to enable dynamic control of gene copy in bacteria.Metabolic engineering · 2022Article
- Agr Quorum Sensing influences the Wood-Ljungdahl pathway in Clostridium autoethanogenum.Scientific reports · 2022Article
- Identification of a PadR-type regulator essential for intracellular pathogenesis of Burkholderia pseudomallei.Scientific reports · 2021Article
- Elements in the LftR Repressor Operator Interface Contributing to Regulation of Aurantimycin Resistance in Listeria monocytogenes.Journal of bacteriology · 2021Article
- Optimization of aACS synthetic biology · 2021Article
- Comparative Analysis of the Global Transcriptomic Response to Oxidative Stress ofMicroorganisms · 2020Article
- A versatile genetic control system in mammalian cells and mice responsive to clinically licensed sodium ferulate.Science advances · 2020Article
- Involvement of a PadR regulator PrhP on virulence of Ralstonia solanacearum by controlling detoxification of phenolic acids and type III secretion system.Molecular plant pathology · 2019Article
- 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
- Crystal structure and DNA binding activity of a PadR family transcription regulator from hypervirulent Clostridium difficile R20291.BMC microbiology · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacillus subtilis 168 is resistant to phenolic acids by expression of an inducible enzyme, the phenolic acid decarboxylase (PadC), that decarboxylates these acids into less toxic vinyl derivatives. In the phenolic acid stress response (PASR), the repressor of padC, PadR, is inactivated by these acids. Inactivation of PadR is followed by a strong expression of padC. To elucidate the functional interaction between PadR and the padC promoter, we performed (i) footprinting assays to identify the region protected by PadR, (ii) electrophoretic mobility shift assays (EMSAs) with a modified padC promoter protected region to determine the interacting sequences, and (iii) random mutagenesis of padR to identify amino acid residues essential for the function of PadR. We identified an important consensus dyad sequence called IR1-2 (ATGT-8N-ACAT) overlapping a second dyad element (GTGT-8N-ACAT) that we named dIR1-2bis. The entire dIR1-2bis/IR1-2 sequence permits binding of two PadR dimers in EMSAs, which may be observed for bacteria grown under noninduced conditions where the padC promoter is completely repressed. Three groups of modified PadRs giving a PASR phenotype were characterized in vivo. The DNA sequences of certain mutant padR alleles indicate that important residues are all located in the region containing the coiled-coil leucine zipper domain that is involved in dimerization. These substitutions reduce the affinity of PadR binding to the padC promoter. Of particular interest are residue L128, located at the center of the putative coiled-coil leucine zipper domain, and residue E97, which is conserved among all PadRs.
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