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Escherichia coli di-iron YtfE protein is necessary for the repair of stress-damaged iron-sulfur clusters

2007-04-06Artigo científico Acesso aberto
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dc.contributor.authorJustino, Marta C.
dc.contributor.authorAlmeida, Cláudia C.
dc.contributor.authorTeixeira, Miguel
dc.contributor.authorSaraiva, Lígia M
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.pblASBMB - American Society for Biochemistry and Molecular Biology
dc.date.accessioned2025-12-03T21:13:21Z
dc.date.available2025-12-03T21:13:21Z
dc.date.issued2007-04-06
dc.description
dc.description.abstractDNA microarray experiments showed that the expression of the Escherichia coli ytfE gene is highly increased upon exposure to nitric oxide. We also reported that deletion of ytfE significantly alters the phenotype of E. coli, generating a strain with enhanced susceptibility to nitrosative stress and defective in the activity of several iron-sulfur-containing proteins. In this work, it is shown that the E. coli ytfE confers protection against oxidative stress. Furthermore, we found that the damage of the [4Fe-4S](2+) clusters of aconitase B and fumarase A caused by exposure to hydrogen peroxide and nitric oxide stress occurs at higher rates in the absence of ytfE. The ytfE null mutation also abolished the recovery of aconitase and fumarase activities, which is observed in wild type E. coli once the stress is scavenged. Notably, upon the addition of purified holo-YtfE protein to the mutant cell extracts, the enzymatic activities of fumarase and aconitase are fully recovered and at rates similar to the wild type strain. We concluded that YtfE is critical for the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent8
dc.format.extent648661
dc.identifier.doi10.1074/jbc.M610656200
dc.identifier.issn0021-9258
dc.identifier.otherPURE: 14892492
dc.identifier.otherPURE UUID: dbeeb762-4e34-4702-9cad-f89bb9d8c89b
dc.identifier.otherPubMed: 17289666
dc.identifier.otherScopus: 34249857689
dc.identifier.urihttp://hdl.handle.net/10362/191449
dc.identifier.urlhttps://www.scopus.com/pages/publications/34249857689
dc.language.isoeng
dc.peerreviewedyes
dc.relationinfo:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F13756%2F2003/PT
dc.relationESTUDO DA FUNÇÃO E REGULAÇÃO DA REDUTASE DE ÓXIDO NÍTRICO EM ESTIRPES DE BACTÉRIAS PATOGÉNICAS
dc.subjectAconitate Hydratase/metabolism
dc.subjectCell-Free System/metabolism
dc.subjectEnzyme Activation/drug effects
dc.subjectEscherichia coli/genetics
dc.subjectEscherichia coli Proteins/genetics
dc.subjectFree Radical Scavengers/pharmacology
dc.subjectFumarate Hydratase/metabolism
dc.subjectHydrogen Peroxide/pharmacology
dc.subjectIron/metabolism
dc.subjectMutation
dc.subjectNitric Oxide/pharmacology
dc.subjectOxidants/pharmacology
dc.subjectOxidative Stress/drug effects
dc.subjectSulfides/metabolism
dc.subjectSulfur/metabolism
dc.titleEscherichia coli di-iron YtfE protein is necessary for the repair of stress-damaged iron-sulfur clustersen
dc.typejournal article
degois.publication.firstPage10352
degois.publication.issue14
degois.publication.lastPage9
degois.publication.titleJournal of Biological Chemistry
degois.publication.volume282
dspace.entity.typePublication
oaire.awardNumberSFRH/BD/13756/2003
oaire.awardTitleESTUDO DA FUNÇÃO E REGULAÇÃO DA REDUTASE DE ÓXIDO NÍTRICO EM ESTIRPES DE BACTÉRIAS PATOGÉNICAS
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F13756%2F2003/PT
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccess
relation.isProjectOfPublicationf52d3247-8117-4f7d-a9d2-fb5852f9a5e0
relation.isProjectOfPublication.latestForDiscoveryf52d3247-8117-4f7d-a9d2-fb5852f9a5e0

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