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 |
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Main Authors: | , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
England
Elsevier B.V
17-07-2003
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Subjects: | |
Online Access: | Get full text |
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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. |
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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 ObjectType-Feature-2 content type line 23 |
ISSN: | 0014-5793 1873-3468 1873-3468 |
DOI: | 10.1016/S0014-5793(03)00696-3 |