ArticleNucleic acids research2018
A peculiar IclR family transcription factor regulates para-hydroxybenzoate catabolism in Streptomyces coelicolor.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- The transcriptional repressor PheR regulates uptake and catabolism of phenanthrene in Sphingobium sp. SHPJ-2.The Journal of biological chemistry · 2026Article
- Systematic Engineering of Proteases in Saccharopolyspora Spinosa Reveals Synergistic Enhancement of Spinosad Biosynthesis via Substrate Flux Optimization.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Multi-proteomics reveals integrated metabolic and regulatory networks for xylan catabolism inMicrobiology spectrum · 2026Article
- A conservedFrontiers in microbiology · 2026Article
- Function and regulation ofApplied and environmental microbiology · 2025Article
- Comparative Proteomic Analysis of Transcriptional and Regulatory Proteins Abundances inInternational journal of molecular sciences · 2022Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
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Abstract
In Streptomyces coelicolor, we identified a para-hydroxybenzoate (PHB) hydroxylase, encoded by gene pobA (SCO3084), which is responsible for conversion of PHB into PCA (protocatechuic acid), a substrate of the β-ketoadipate pathway which yields intermediates of the Krebs cycle. We also found that the transcription of pobA is induced by PHB and is negatively regulated by the product of SCO3209, which we named PobR. The product of this gene is highly unusual in that it is the apparent fusion of two IclR family transcription factors. Bioinformatic analyses, in vivo transcriptional assays, electrophoretic mobility shift assays (EMSAs), DNase I footprinting, and isothermal calorimetry (ITC) were used to elucidate the regulatory mechanism of PobR. We found that PobR loses its high affinity for DNA (i.e., the pobA operator) in the presence of PHB, the inducer of pobA transcription. PHB binds to PobR with a KD of 5.8 μM. Size-exclusion chromatography revealed that PobR is a dimer in the absence of PHB and a monomer in the presence of PHB. The crystal structure of PobR in complex with PHB showed that only one of the two IclR ligand binding domains was occupied, and defined how the N-terminal ligand binding domain engages the effector ligand.
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