Journal
MOLECULAR PLANT
Volume 2, Issue 3, Pages 378-389Publisher
CELL PRESS
DOI: 10.1093/mp/ssn096
Keywords
Protein structure; proteomics; cereal grains; disulfide reduction; seed germination; thioredoxin reductase
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Funding
- Danish National Research Council for Agricultural and Veterinary Science
- Danish National Research Council for Natural Sciences
- Danish Center for Advanced Food Studies
- Iranian Ministry for Science Research and Technology
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Thioredoxins (Trx) are ubiquitous proteins that participate in thiol disulfide reactions via two active site cysteine residues, allowing Trx to reduce disulfide bonds in target proteins. Recent progress in proteome analysis has resulted in identification of a wide range of potential target proteins for Trx, indicating that Trx plays a key role in several aspects of cell metabolism. In contrast to other organisms, plants contain multiple forms of Trx that are classified based on their primary structures and sub-cellular localization. The reduction of cytosolic and mitochondrial types of Trx is dependent on NADPH and catalyzed by NADPH-dependent thioredoxin reductase (NTR). In barley, two isoforms each of Trx and NTR have been identified and investigated using proteomics, gene expression, and structural studies. This review outlines the diverse roles suggested for cytosolic/mitochondrial-type Trx systems in cereal seeds and summarizes the current knowledge of the barley system including recent data on function, regulation, interactions, and structure. Directions for future research are discussed.
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