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- W2096903211 abstract "The thioredoxin (Trx) system is known to play a pivotal role in cellular redox regulation, but its target proteins in plant mitochondria remain largely uncharacterized. In this study, we systemically screened Trx target candidates in plant mitochondria. Mitochondrial protein extracts were prepared from Arabidopsis shoots, spinach leaves and potato tubers, and then subfractionated into soluble matrix and insoluble membrane fractions. Protein extracts were loaded onto an affinity column immobilizing Arabidopsis mitochondria-localized o-type Trx mutant protein, in which one of two internal cysteines at the active site was substituted by serine. Proteins forming mixed-disulfide intermediates with the mutated Trx were identified by proteomic approaches. This procedure allowed the determination of 101 Trx target candidate proteins involved in a broad spectrum of mitochondrial processes. Furthermore, biochemical assay revealed that one of the potential Trx target proteins, alternative oxidase, is actually redox regulated by Trx. This study provides insights into the regulatory mechanism of diverse functions in mitochondrial biology that are mediated through the Trx system." @default.
- W2096903211 created "2016-06-24" @default.
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- W2096903211 creator A5026889135 @default.
- W2096903211 creator A5040684273 @default.
- W2096903211 creator A5070445171 @default.
- W2096903211 date "2013-04-17" @default.
- W2096903211 modified "2023-10-14" @default.
- W2096903211 title "Systematic Exploration of Thioredoxin Target Proteins in Plant Mitochondria" @default.
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- W2096903211 doi "https://doi.org/10.1093/pcp/pct037" @default.
- W2096903211 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23444301" @default.
- W2096903211 hasPublicationYear "2013" @default.
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