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GrainGenes Reference Report: PCP-45-407

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Reference	PCP-45-407
Title	Thioredoxin reduction alters the solubility of proteins of wheat starchy endosperm: An early event in cereal germination
Journal	Plant and Cell Physiology
Year	2004
Volume	45
Pages	407-415
Author	[ Hide all but 1 of 6 ] Wong JH Cai N Tanaka CK Vensel WH Hurkman WJ Buchanan BB
Abstract	Summary: A KCl-soluble, albumin/globulin fraction of wheat (Triticum aestivum L.) starchy endosperm was further separated into a methanol-insoluble fraction that contained metabolic proteins and a methanol-soluble fraction that contained 'chloroform-methanol' or CM-like proteins. Reduction of the disulfide bonds of the CM proteins with thioredoxin or dithiothreitol altered their properties so that, like the metabolic proteins, they were insoluble in methanol. Glutathione had little effect, indicating dithiol specificity. Proteomic analysis of the CM protein fraction revealed the presence of isoforms of low molecular weight disulfide proteins (a-amylase, a-amylase/trypsin and WCI proteinase inhibitors, lipid transfer proteins, g-thionins), stress enzymes (Cu-Zn superoxide dismutase and peroxidase), storage proteins (a-, g- and omega-gliadins, low molecular weight glutenin subunits and globulins of the avenin N9 type), and a component of protein degradation (polyubiquitin). These findings support the view that, in addition to modifying activity and increasing protease sensitivity, reduction by thioredoxin alters protein solubility, thereby promoting processes of the grain starchy endosperm, notably the mobilization of reserves during germination and seedling development
External Databases	Pubmed: 15111715
Keyword	alpha-amylase [ Show all 51 ]

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