Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics

Application of a thiol-specific probe, monobromobimane, with proteomics and enzyme assays led to the identification of 23 thioredoxin targets in the starchy endosperm of mature wheat seeds ( Triticum aestivum cv. Butte), almost all containing at least two conserved cysteines. The identified targets,...

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Published in:FEBS letters Vol. 547; no. 1; pp. 151 - 156
Main Authors: Wong, Joshua H, Balmer, Yves, Cai, Nick, Tanaka, Charlene K, Vensel, William H, Hurkman, William J, Buchanan, Bob B
Format: Journal Article
Language:English
Published: England Elsevier B.V 17-07-2003
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Summary:Application of a thiol-specific probe, monobromobimane, with proteomics and enzyme assays led to the identification of 23 thioredoxin targets in the starchy endosperm of mature wheat seeds ( Triticum aestivum cv. Butte), almost all containing at least two conserved cysteines. The identified targets, 12 not known to be thioredoxin-linked, function in a spectrum of processes: metabolism (12 targets), protein storage (three), oxidative stress (three), protein degradation (two), protein assembly/folding (one) and unknown reactions (two). In addition to formulating metabolic pathways functional in the endosperm, the results suggest that thioredoxin acts in redox regulation throughout the life cycle of the seed.
Bibliography:http://dx.doi.org/10.1016/S0014-5793(03)00696-3
http://hdl.handle.net/10113/49446
ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:0014-5793
1873-3468
1873-3468
DOI:10.1016/S0014-5793(03)00696-3