Nitrosative stress: activation of the transcription factor OxyR.

Published

Journal Article

Hydrogen peroxide (H2O2) imposes an oxidative stress to Escherichia coli that is manifested by oxidation of glutathione and related redox-sensitive targets. OxyR is a thiol-containing transcriptional activator whose oxidation controls the expression of genes involved in H2O2 detoxification. Here we report that certain S-nitrosothiols (RSNOs) impose what we term a "nitrosative stress" to E. coli, evidenced by lowering of intracellular thiol and the transcriptional activation of OxyR by S-nitrosylation. This cellular and genetic response determines the metabolic fate of RSNOs and thereby contributes to bacterial rescue from stasis. Our studies reveal that signaling by S-nitrosylation can extend to the level of transcription and describe a metabolic pathway that constitutes an adaptation to nitrosative stress.

Full Text

Duke Authors

Cited Authors

  • Hausladen, A; Privalle, CT; Keng, T; DeAngelo, J; Stamler, JS

Published Date

  • September 6, 1996

Published In

Volume / Issue

  • 86 / 5

Start / End Page

  • 719 - 729

PubMed ID

  • 8797819

Pubmed Central ID

  • 8797819

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/s0092-8674(00)80147-6

Language

  • eng

Conference Location

  • United States