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. 1994 Sep;176(18):5601–5606. doi: 10.1128/jb.176.18.5601-5606.1994

The torR gene of Escherichia coli encodes a response regulator protein involved in the expression of the trimethylamine N-oxide reductase genes.

G Simon 1, V Méjean 1, C Jourlin 1, M Chippaux 1, M C Pascal 1
PMCID: PMC196761  PMID: 8083154

Abstract

Expression of the Escherichia coli torCAD operon encoding the trimethylamine N-oxide (TMAO) reductase system is induced by both TMAO and anaerobiosis. A torR insertion mutant unable to express the torA gene had previously been isolated. The torR gene was cloned and sequenced. It encodes a 25,000-Da protein which shares homology with response regulators of two-component systems and belongs to the OmpR-PhoB subclass. Overproduction of TorR mimics the presence of the inducer TMAO while the anaerobic control is unchanged, suggesting that TorR mediates only the TMAO induction. The overproduced TorR protein was purified to more than 90%. The torR gene is located just upstream of the torCAD operon, with an opposite transcription direction. The torR-torCAD intergenic region is unusual in that it contains four direct repeats of a 10-nucleotide motif. Part or all of these motifs could be involved in the binding of TorR. The gene encoding the sensor partner does not seem to be adjacent to torR, since the divergent open reading frame found immediately downstream of torR exhibits none of the features of a protein histidine kinase.

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Selected References

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