Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/52538
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dc.contributor.authorLópez-Maury, Luis-
dc.contributor.authorSánchez-Riego, Ana María-
dc.contributor.authorReyes, José C.-
dc.contributor.authorFlorencio, Francisco J.-
dc.date.accessioned2012-06-29T08:41:32Z-
dc.date.available2012-06-29T08:41:32Z-
dc.date.issued2009-03-20-
dc.identifierdoi: 10.1128/JB.01798-08-
dc.identifierissn: 0021-9193-
dc.identifiere-issn: 1098-5530-
dc.identifier.citationJournal of Bacteriology 191(11): 3534-3543 (2009)-
dc.identifier.otherPMC2681892-
dc.identifier.otherPMID: 19304854-
dc.identifier.urihttp://hdl.handle.net/10261/52538-
dc.description.abstractArsenic resistance in Synechocystis sp. strain PCC 6803 is mediated by an operon of three genes in which arsC codes for an arsenate reductase with unique characteristics. Here we describe the identification of two additional and nearly identical genes coding for arsenate reductases in Synechocystis sp. strain PCC 6803, which we have designed arsI1 and arsI2, and the biochemical characterization of both ArsC (arsenate reductase) and ArsI. Functional analysis of single, double, and triple mutants shows that both ArsI enzymes are active arsenate reductases but that their roles in arsenate resistance are essential only in the absence of ArsC. Based on its biochemical properties, ArsC belongs to a family that, though related to thioredoxin-dependent arsenate reductases, uses the glutathione/glutaredoxin system for reduction, whereas ArsI belongs to the previously known glutaredoxin-dependent family. We have also analyzed the role in arsenate resistance of the three glutaredoxins present in Synechocystis sp. strain PCC 6803 both in vitro and in vivo. Only the dithiolic glutaredoxins, GrxA (glutaredoxin A) and GrxB (glutaredoxin B), are able to donate electrons to both types of reductases in vitro, while GrxC (glutaredoxin C), a monothiolic glutaredoxin, is unable to donate electrons to either type. Analysis of glutaredoxin mutant strains revealed that only those lacking the grxA gene have impaired arsenic resistance. Copyright © 2009, American Society for Microbiology. All Rights Reserved.-
dc.description.sponsorshipThis research was supported by grants BMC2004-0050 and BFU2007-60300/BMC from the Ministry of Education and Science of Spain and by the Junta de Andalucia (Group BIO-0284), grant CVI-099. A.M.S.-R. is a recipient of a fellowship from the Ministerio de Educación y Ciencia (M.E.C.).-
dc.language.isoeng-
dc.publisherAmerican Society for Microbiology-
dc.rightsclosedAccess-
dc.subjectArsenate reductases-
dc.subjectBacterial proteins-
dc.subjectGlutaredoxins-
dc.subjectThioredoxins-
dc.subjectGlutathione-
dc.subjectArsenic acid-
dc.titleThe glutathione/glutaredoxin system is essential for arsenate reduction in Synechocystis sp. strain PCC 6803-
dc.typeartículo-
dc.identifier.doi10.1128/JB.01798-08-
dc.date.updated2012-06-29T08:41:32Z-
dc.description.versionPeer Reviewed-
dc.identifier.pmid19304854-
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.fulltextNo Fulltext-
item.languageiso639-1en-
item.openairetypeartículo-
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