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GrainGenes Reference Report: PYC-65-1629

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Reference	PYC-65-1629
Title	Thioredoxin targets of developing wheat seeds identified by complementary proteomic approaches
Journal	Phytochemistry
Year	2004
Volume	65
Pages	1629-1640
Author	Wong JH [ Show all 7 ]
Abstract	The role of thioredoxin in wheat starchy endosperm was investigated utilizing two proteomic approaches. Thioredoxin targets were isolated from total KCl-soluble extracts of endosperm and flour and separated by 2-DE following (1) reduction of the extract by the NADP/thioredoxin system and labeling the newly generated sulfhydryl (SH) groups with monobromobimane (mBBr), and, in parallel, (2) trapping covalently interacting proteins on an affinity column prepared with mutant thioredoxin h in which one of the active site cysteines was replaced by serine. The two procedures were complementary: of the total targets, one-third were observed with both procedures and one-third were unique to each. Altogether 68 potential targets were identified; almost all containing conserved cysteines. In addition to confirming known interacting proteins, we identified 40 potential thioredoxin targets not previously described in seeds. A comparison of the results obtained with young endosperm (isolated 10 days after flowering) to those with mature endosperm (isolated 36 days after flowering) revealed a unique set of proteins functional in processes characteristic of each developmental stage. Flour contained 36 thioredoxin targets, most of which have been found in the isolated developing endosperm
External Databases	Pubmed: 15276458
Keyword	[ Hide all but 1 of 24 ] barley developing endosperm disulfide proteins disulfide proteome endosperm flour flowering germination monobromobimane mutant plant thioredoxins proteomics redox changes reductase reduction starchy endosperm storage protein sulfhydryl-disulfide changes thioredoxin thioredoxin h thioredoxin-h triticum aestivum wheat endosperm wheat flour

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