ArticleNucleic acids research2013
Interaction of bacterial fatty-acid-displaced regulators with DNA is interrupted by tyrosine phosphorylation in the helix-turn-helix domain.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- Oxidative stress is intrinsic to staphylococcal adaptation to fatty acid synthesis antibiotics.iScience · 2024Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- Review
- Phosphoproteome Study ofFrontiers in microbiology · 2021Article
- DNA Binding and Sensor Specificity of FarR, a Novel TetR Family Regulator Required for Induction of the Fatty Acid Efflux Pump FarE inJournal of bacteriology · 2019Article
- The Pkn22 Kinase ofFrontiers in microbiology · 2019Article
- Article
- Structural Analysis of the Hanks-Type Protein Kinase YabT FromFrontiers in microbiology · 2018Article
- Evolution and tinkering: what do a protein kinase, a transcriptional regulator and chromosome segregation/cell division proteins have in common?Current genetics · 2016Review
- Tyrosine Phosphorylation and Dephosphorylation in Burkholderia cenocepacia Affect Biofilm Formation, Growth under Nutritional Deprivation, and Pathogenicity.Applied and environmental microbiology · 2016Article
- Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival.Frontiers in microbiology · 2016Article
- Substrate Specificity of theFrontiers in microbiology · 2016Article
- Protein-tyrosine phosphorylation in Bacillus subtilis: a 10-year retrospective.Frontiers in microbiology · 2015Article
- Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpC.Molecular & cellular proteomics : MCP · 2014Article
- The protein tyrosine kinases EpsB and PtkA differentially affect biofilm formation in Bacillus subtilis.Microbiology (Reading, England) · 2014Article
- Evolution of bacterial protein-tyrosine kinases and their relaxed specificity toward substrates.Genome biology and evolution · 2014Article
- Protein-tyrosine phosphorylation interaction network in Bacillus subtilis reveals new substrates, kinase activators and kinase cross-talk.Frontiers in microbiology · 2014Article
- Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues.Frontiers in microbiology · 2014Article
- Factors that mediate and prevent degradation of the inactive and unstable GudB protein in Bacillus subtilis.Frontiers in microbiology · 2014Article
- Far from being well understood: multiple protein phosphorylation events control cell differentiation in Bacillus subtilis at different levels.Frontiers in microbiology · 2014Article
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Authors and funding
9 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteria possess transcription regulators (of the TetR family) specifically dedicated to repressing genes for cytochrome P450, involved in oxidation of polyunsaturated fatty acids. Interaction of these repressors with operator sequences is disrupted in the presence of fatty acids, and they are therefore known as fatty-acid-displaced regulators. Here, we describe a novel mechanism of inactivating the interaction of these proteins with DNA, illustrated by the example of Bacillus subtilis regulator FatR. FatR was found to interact in a two-hybrid assay with TkmA, an activator of the protein-tyrosine kinase PtkA. We show that FatR is phosphorylated specifically at the residue tyrosine 45 in its helix-turn-helix domain by the kinase PtkA. Structural modelling reveals that the hydroxyl group of tyrosine 45 interacts with DNA, and we show that this phosphorylation reduces FatR DNA binding capacity. Point mutants mimicking phosphorylation of FatR in vivo lead to a strong derepression of the fatR operon, indicating that this regulatory mechanism works independently of derepression by polyunsaturated fatty acids. Tyrosine 45 is a highly conserved residue, and PtkA from B. subtilis can phosphorylate FatR homologues from other bacteria. This indicates that phosphorylation of tyrosine 45 may be a general mechanism of switching off bacterial fatty-acid-displaced regulators.
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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.