Nitric oxide releases intracellular zinc from prokaryotic metallothionein in Escherichia coli
| Autor: | Robert K. Poole, Jay R. Laver, Marie R.B. Binet, Martin N. Hughes, Hugo Cruz-Ramos |
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| Rok vydání: | 2002 |
| Předmět: |
ATPase
Mutant lac operon chemistry.chemical_element Zinc medicine.disease_cause Nitric Oxide Microbiology Nitric oxide chemistry.chemical_compound Genetics medicine Escherichia coli Metallothionein Promoter Regions Genetic Molecular Biology Adenosine Triphosphatases biology Synechococcus biology.organism_classification chemistry Biochemistry Mutation biology.protein |
| Zdroj: | FEMS microbiology letters. 213(1) |
| ISSN: | 0378-1097 |
| Popis: | Nitric oxide (NO) has a broad spectrum of signalling and regulatory functions and multiple molecular targets. Recently, the intrabacterial toxicity of NO and mechanisms for NO resistance have been intensively investigated. Here we report for the first time that NO elicits release of zinc from a bacterial protein. Using the zinc-responsive expression of zntA (encoding a Zn-exporting P-type ATPase) fused to lacZ, i.e. Phi(zntA-lacZ), to monitor intracellular zinc, and SmtA (the Synechococcus metallothionein) as zinc store, we have shown that the NO donors NOC-5 and NOC-7 elicit zinc ejection. No increase in Phi(zntA-lacZ) activity was observed in a zntR mutant, indicating the specificity of the zntA promoter response to zinc ions. |
| Databáze: | OpenAIRE |
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