ArticleJournal of bacteriology2008
Escherichia coli NsrR regulates a pathway for the oxidation of 3-nitrotyramine to 4-hydroxy-3-nitrophenylacetate.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 39 citations in OpenAlex.
- Integrated transcriptomic and metabolomic analysis reveals stage-associated molecular profiles in Ophiocordyceps sinensis.BMC genomics · 2025Article
- Phenelzine and Amoxapine Inhibit Tyramine and d-Glucuronic Acid Catabolism in Clinically SignificantPathogens (Basel, Switzerland) · 2021Article
- Molecular Mechanism for Attractant Signaling to DHMA by E. coli Tsr.Biophysical journal · 2020Article
- Conversion of Norepinephrine to 3,4-Dihdroxymandelic Acid in Escherichia coli Requires the QseBC Quorum-Sensing System and the FeaR Transcription Factor.Journal of bacteriology · 2018Article
- Bacterial iron-sulfur cluster sensors in mammalian pathogens.Metallomics : integrated biometal science · 2015Review
- Primary Amine Oxidase of Escherichia coli Is a Metabolic Enzyme that Can Use a Human Leukocyte Molecule as a Substrate.PloS one · 2015Article
- Chemotaxis of Escherichia coli to norepinephrine (NE) requires conversion of NE to 3,4-dihydroxymandelic acid.Journal of bacteriology · 2014Article
- Finely tuned regulation of the aromatic amine degradation pathway in Escherichia coli.Journal of bacteriology · 2013Article
- How Escherichia coli tolerates profuse hydrogen peroxide formation by a catabolic pathway.Journal of bacteriology · 2013Article
- Evolution of transcriptional regulation in closely related bacteria.BMC evolutionary biology · 2012Article
- Prokaryotic genome regulation: a revolutionary paradigm.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2012Review
- The multidrug efflux pump MdtEF protects against nitrosative damage during the anaerobic respiration in Escherichia coli.The Journal of biological chemistry · 2011Article
- Iron-containing transcription factors and their roles as sensors.Current opinion in chemical biology · 2011Review
- Nitric oxide-sensitive and -insensitive interaction of Bacillus subtilis NsrR with a ResDE-controlled promoter.Molecular microbiology · 2010Article
- Nitroaromatic compounds, from synthesis to biodegradation.Microbiology and molecular biology reviews : MMBR · 2010Review
- Upward mobility and alternative lifestyles: a report from the 10th biennial meeting on Bacterial Locomotion and Signal Transduction.Molecular microbiology · 2009Article
- Conditioning of uropathogenic Escherichia coli for enhanced colonization of host.Infection and immunity · 2009Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chromatin immunoprecipitation and microarray (ChIP-chip) analysis showed that the nitric oxide (NO)-sensitive repressor NsrR from Escherichia coli binds in vivo to the promoters of the tynA and feaB genes. These genes encode the first two enzymes of a pathway that is required for the catabolism of phenylethylamine (PEA) and its hydroxylated derivatives tyramine and dopamine. Deletion of nsrR caused small increases in the activities of the tynA and feaB promoters in cultures grown on PEA. Overexpression of nsrR severely retarded growth on PEA and caused a marked repression of the tynA and feaB promoters. Both the growth defect and the promoter repression were reversed in the presence of a source of NO. These results are consistent with NsrR mediating repression of the tynA and feaB genes by binding (in an NO-sensitive fashion) to the sites identified by ChIP-chip. E. coli was shown to use 3-nitrotyramine as a nitrogen source for growth, conditions which partially induce the tynA and feaB promoters. Mutation of tynA (but not feaB) prevented growth on 3-nitrotyramine. Growth yields, mutant phenotypes, and analyses of culture supernatants suggested that 3-nitrotyramine is oxidized to 4-hydroxy-3-nitrophenylacetate, with growth occurring at the expense of the amino group of 3-nitrotyramine. Accordingly, enzyme assays showed that 3-nitrotyramine and its oxidation product (4-hydroxy-3-nitrophenylacetaldehyde) could be oxidized by the enzymes encoded by tynA and feaB, respectively. The results suggest that an additional physiological role of the PEA catabolic pathway is to metabolize nitroaromatic compounds that may accumulate in cells exposed to NO.
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