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dc.contributor.authorLópez-Martín, M. Carmen-
dc.contributor.authorRomero, Luis C.-
dc.contributor.authorGotor, Cecilia-
dc.date.accessioned2009-02-05T10:49:09Z-
dc.date.available2009-02-05T10:49:09Z-
dc.date.issued2008-10-
dc.identifier.citationPlant Signaling & Behavior 3(10): 880-881 (2008)en_US
dc.identifier.issn1559-2316-
dc.identifier.urihttp://hdl.handle.net/10261/10337-
dc.description2 pages.-- Addendum to: Knocking out cytosolic cysteine synthesis compromises the antioxidant capacity of the cytosol to maintain discrete concentrations of hydrogen peroxide in Arabidopsis. López-Martín M.C., Becana M., Romero L.C., Gotor C. Plant Physiol 2008, http://digital.csic.es/handle/10261/5569.en_US
dc.description.abstractCysteine biosynthesis in plants takes place in the three cellular compartments with autonomous protein biosynthesis machinery: cytosol, plastids and mitochondria. This sulfur-containing molecule is synthesized sequentially in these compartments by two enzymatic families, the serine acetyltransferases and the O-acetylserine(thiol)lyases. Each family consists of several isoforms that differ in subcellular localization and abundance. Why so many isoforms are required in plant cell for cysteine biosynthesis has remained unknown to date. The characterization of gene-specific knockout mutants has started to address this question. In our recent work, we have performed a detailed analysis of the Arabidopsis oas-a1 null mutant and showed that the antioxidant capacity of the cytosol is compromised highlighting the contribution of cytosolic Cys in redox signaling.en_US
dc.description.sponsorshipThis work was funded by Ministerio de Educación y Ciencia (grant no. BIO2007-62770) and Junta de Andalucía (grant no. CVI-273), Spain.en_US
dc.format.extent22195 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoengen_US
dc.publisherLandes Bioscienceen_US
dc.rightsclosedAccessen_US
dc.subjectArabidopsisen_US
dc.subjectO-acetylserine(thiol)lyaseen_US
dc.subjectCysteine biosynthesisen_US
dc.subjectRedox regulationen_US
dc.titleCytosolic cysteine in redox signalingen_US
dc.typeartículoen_US
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttp://www.landesbioscience.com/journals/psb/article/6289en_US
dc.identifier.e-issn1559-2324-
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.openairetypeartículo-
item.languageiso639-1en-
item.grantfulltextnone-
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