| Literature DB >> 25384477 |
Ken Vercammen1, Qing Wei1, Daniel Charlier2, Andreas Dötsch3, Susanne Haüssler3, Sebastian Schulz3, Francesca Salvi4, Giovanni Gadda5, Jim Spain6, Morten Levin Rybtke7, Tim Tolker-Nielsen7, Jozef Dingemans1, Lumeng Ye1, Pierre Cornelis8.
Abstract
The PA4203 gene encodes a LysR regulator and lies between the ppgL gene (PA4204), which encodes a periplasmic gluconolactonase, and, in the opposite orientation, the PA4202 (nmoA) gene, coding for a nitronate monooxygenase, and ddlA (PA4201), encoding a d-alanine alanine ligase. The intergenic regions between PA4203 and ppgL and between PA4203 and nmoA are very short (79 and 107 nucleotides, respectively). Here we show that PA4203 (nmoR) represses its own transcription and the expression of nmoA. A chromatin immunoprecipitation analysis showed the presence of a single NmoR binding site between nmoA and nmoR, which was confirmed by electrophoretic mobility shift assays (EMSAs) with the purified NmoR protein. Despite this observation, a transcriptome analysis revealed more genes to be affected in an nmoR mutant, including genes known to be part of the MexT LysR activator regulon. The PA1225 gene, encoding a quinone oxidoreductase, was the most highly upregulated gene in the nmoR deletion mutant, independently of MexT. Finally, deletion of the nmoA gene resulted in an increased sensitivity of the cells to 3-nitropropionic acid (3-NPA), confirming the role of the nitronate monooxygenase protein in the detoxification of nitronate.Entities:
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Year: 2014 PMID: 25384477 PMCID: PMC4336338 DOI: 10.1128/JB.01991-14
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490