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A more recent version of this article appeared on March 14, 2003
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Papers In Press, published online ahead of print January 15, 2003
J. Biol. Chem, 10.1074/jbc.M212462200
Submitted on December 6, 2002
Revised on January 14, 2003
Accepted on January 15, 2003

Regulation of the nitric oxide reduction operon (norRVW) in Escherichia coli: Role of NorR and Sigma 54 in the nitric oxide stress response

Anne M. Gardner, Christopher R. Gessner, and Paul R. Gardner

Division of Critical Care Medicine, Children's Hospital Medical Center, Cincinnati, OH 45229

Corresponding Author: anne.gardner{at}cchmc.org

Nitric oxide (NO) induces NO-detoxifying enzymes in Escherichia coli suggesting sensitive mechanisms for coordinate control of NO defense genes in response to NO stress. Exposure of E. coli to sub-micromolar NO levels under anaerobic conditions rapidly induced transcription of the NO reductase (NOR) structural genes, norV and norW, as monitored by lac gene fusions. Disruption of rpoN (sigma 54) impaired the NO-mediated induction of norV and norW transcription and NOR expression, whereas disruption of the upstream regulatory gene, norR, completely ablated NOR induction. NOR inducibility was restored to NorR null mutants by expressing NorR in trans. Further, an internal deletion of the amino terminal domain of NorR activated NOR expression independent of NO exposure. Neither NorR nor sigma 54 was essential for NO-mediated induction of the NO dioxygenase (flavohemoglobin) encoded by hmp. However, elevated NOR activity inhibited NO dioxygenase induction, and in the presence of dioxygen, NO dioxygenase inhibited norV induction by NO. The results demonstrate the role of NorR as a sigma 54-dependent regulator of norVW expression. A role for the NorR amino terminal domain as a transducer or sensor for NO is suggested.


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