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Mitochondrial Sulfide Detoxification Requires a Functional Isoform O-Acetylserine(thiol)lyase C in Arabidopsis thaliana

Opened Access Mitochondrial Sulfide Detoxification Requires a Functional Isoform O-Acetylserine(thiol)lyase C in Arabidopsis thaliana

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Autor: Álvarez Nuñez, Consolación
García Fernández, Irene
Romero González, Luis Carlos
Gotor Martínez, Cecilia
Fecha: 2012
Publicado en: Molecular Plant, 5, 1217-1226.
Tipo de documento: Artículo
Resumen: In non-cyanogenic species, the main source of cyanide derives from ethylene and camalexin biosyntheses. In mitochondria, cyanide is a potent inhibitor of the cytochrome c oxidase and is metabolised by the β-Cyanoalanine synthase CYS-C1, catalysing the conversion of cysteine and cyanide to hydrogen sulfide and β- cyanoalanine. The hydrogen sulfide released also inhibits the cytochrome c oxidase and needs to be detoxified by the O-acetylserine(thiol)lyase mitochondrial isoform, OAS-C, which catalyses the incorporation of sulfide to O-acetylserine to produce cysteine, thus generating a cyclic pathway in the mitochondria. The loss of functional OAS-C isoforms causes phenotypic characteristics very similar to the loss of the CYS-C1 enzyme, showing defects in root hair formation. Genetic complementation with the OAS-C gene rescues the impairment of root hair elongation restoring the wild type phenotype. The mitochondria compromise their capacity to proper detoxify cyanide and the resulting ...
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Cita: Álvarez Nuñez, C., García Fernández, I., Romero González, L.C. y Gotor Martínez, C. (2012). Mitochondrial Sulfide Detoxification Requires a Functional Isoform O-Acetylserine(thiol)lyase C in Arabidopsis thaliana. Molecular Plant, 5, 1217-1226.
Tamaño: 5.521Mb
Formato: PDF

URI: https://hdl.handle.net/11441/70839

DOI: 10.1093/mp/sss043

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