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Mitochondrial sulfide detoxification requires a functional isoform O-acetylserine(thiol)lyase C in Arabidopsis thaliana.
Mol Plant 2012; 5(6):1217-26MP

Abstract

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 metabolized by the β-cyanoalanine synthase CYS-C1, catalyzing 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 catalyzes 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 properly detoxify cyanide and the resulting sulfide because the latter cannot re-assimilate into cysteine in the oas-c null mutant. Consequently, we observe an accumulation of sulfide and cyanide and of the alternative oxidase, which is unable to prevent the production of reactive oxygen species probably due to the accumulation of both toxic molecules. Our results allow us to suggest that the significance of OAS-C is related to its role in the proper sulfide and cyanide detoxification in mitochondria.

Authors+Show Affiliations

Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas y Universidad de Sevilla, Avda. Américo Vespucio, 49, 41092 Sevilla, Spain.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22511607

Citation

Álvarez, Consolación, et al. "Mitochondrial Sulfide Detoxification Requires a Functional Isoform O-acetylserine(thiol)lyase C in Arabidopsis Thaliana." Molecular Plant, vol. 5, no. 6, 2012, pp. 1217-26.
Álvarez C, García I, Romero LC, et al. Mitochondrial sulfide detoxification requires a functional isoform O-acetylserine(thiol)lyase C in Arabidopsis thaliana. Mol Plant. 2012;5(6):1217-26.
Álvarez, C., García, I., Romero, L. C., & Gotor, C. (2012). Mitochondrial sulfide detoxification requires a functional isoform O-acetylserine(thiol)lyase C in Arabidopsis thaliana. Molecular Plant, 5(6), pp. 1217-26. doi:10.1093/mp/sss043.
Álvarez C, et al. Mitochondrial Sulfide Detoxification Requires a Functional Isoform O-acetylserine(thiol)lyase C in Arabidopsis Thaliana. Mol Plant. 2012;5(6):1217-26. PubMed PMID: 22511607.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Mitochondrial sulfide detoxification requires a functional isoform O-acetylserine(thiol)lyase C in Arabidopsis thaliana. AU - Álvarez,Consolación, AU - García,Irene, AU - Romero,Luis C, AU - Gotor,Cecilia, Y1 - 2012/04/17/ PY - 2012/4/19/entrez PY - 2012/4/19/pubmed PY - 2013/12/16/medline SP - 1217 EP - 26 JF - Molecular plant JO - Mol Plant VL - 5 IS - 6 N2 - 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 metabolized by the β-cyanoalanine synthase CYS-C1, catalyzing 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 catalyzes 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 properly detoxify cyanide and the resulting sulfide because the latter cannot re-assimilate into cysteine in the oas-c null mutant. Consequently, we observe an accumulation of sulfide and cyanide and of the alternative oxidase, which is unable to prevent the production of reactive oxygen species probably due to the accumulation of both toxic molecules. Our results allow us to suggest that the significance of OAS-C is related to its role in the proper sulfide and cyanide detoxification in mitochondria. SN - 1752-9867 UR - https://www.unboundmedicine.com/medline/citation/22511607/Mitochondrial_sulfide_detoxification_requires_a_functional_isoform_O_acetylserine_thiol_lyase_C_in_Arabidopsis_thaliana_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1674-2052(14)60149-0 DB - PRIME DP - Unbound Medicine ER -