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The regulatory protein NsrR, a member of the Rrf2 family of transcription repressors, is specifically dedicated to sensing nitric oxide (NO) in a variety of pathogenic and non-pathogenic bacteria. It has been proposed that NO directly modulates NsrR activity by interacting with a predicted [Fe-S] cluster in the NsrR protein, but no experimental evidence has been published to support this hypothesis. Here we report the purification of NsrR from the obligate aerobe Streptomyces coelicolor.

We demonstrate using UV-visible, near UV CD and EPR spectroscopy that the protein contains an NO-sensitive [2Fe-2S] cluster when purified from E. Upon exposure of NsrR to NO, the cluster is nitrosylated, which results in the loss of DNA binding activity as detected by bandshift assays. Shivaji maharaj serial star pravah mp3 song. Removal of the [2Fe-2S] cluster to generate apo-NsrR also resulted in loss of DNA binding activity.

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This is the first demonstration that NsrR contains an NO-sensitive [2Fe-2S] cluster that is required for DNA binding activity. Introduction Nitric oxide (NO) is a highly reactive and toxic free radical gas that can freely diffuse into cells and attack the redox centers of proteins.

Human macrophages produce NO as a very early line of defense against invading bacterial pathogens. Soil bacteria are exposed to NO produced by denitrifying microbes and by the NO synthases of plants and microbes. Bacteria have evolved specific NO sensor proteins that regulate the expression of enzymes required for rapid detoxification of NO, usually by reduction to nitrous oxide (N 2O), a greenhouse gas 300 times more potent than CO 2.

Understanding the ways in which bacteria sense and respond to NO is fundamentally important and has serious implications for human health, agriculture and the environment. The Gram-negative bacterium Escherichia coli encodes several proteins that are known to sense NO directly, including the [4Fe-4S] oxygen sensing transcription factor FNR and the [2Fe-2S] transcription factor SoxR. However, two proteins appear to be dedicated solely to sensing NO in E.

The first is NorR, which senses NO directly through a mononuclear non-heme iron center and responds by switching on expression of the flavorubredoxin NorVW to detoxify NO,,. More recently a second protein, named NsrR, was shown to sense NO in E. Coli and to control a regulon of at least 30 genes. This regulon includes hmp, which encodes an NO detoxifying flavohaemoglobin that converts NO to N 2O or to nitrate (NO 3 −). NsrR, unlike NorR, appears to be a global regulator of NO-induced stress and has been identified and studied in a wide range of Gram-negative and Gram-positive bacteria including Bacillus subtilis, Salmonella enterica, and the obligate human pathogens Neisseria meningitidis and N. NsrR belongs to the Rrf2 family that includes the [2Fe-2S] containing transcription factor IscR and the iron regulator RirA,. As a result it has been predicted that NsrR might also contain a [2Fe-2S] cluster that can sense NO directly.