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, 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.
Wong
Joshua H
JH
Department of Plant and Microbial Biology, 111 Koshland Hall, University of California, Berkeley, CA 94720, USA.
Balmer
Yves
Y
Cai
Nick
N
Tanaka
Charlene K
CK
Vensel
William H
WH
Hurkman
William J
WJ
Buchanan
Bob B
BB
D017124:Conserved Sequence; D003545:Cysteine; D018384:Oxidative Stress; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D018514:Plant Structures / Q000378:metabolism; D012639:Seeds / Q000378:metabolism*; D013879:Thioredoxins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D014908:Triticum / Q000378:metabolism*
D010940:Plant Proteins; D013879:Thioredoxins; D003545:Cysteine