Marcus F, Chamberlain S H, Chu C, Masiarz F R, Shin S, Yee B C, Buchanan B B
Chiron Research Laboratories, Chiron Corporation, Emeryville, California 94608.
Arch Biochem Biophys. 1991 May 15;287(1):195-8. doi: 10.1016/0003-9861(91)90406-9.
Thioredoxin h has been purified to electrophoretic homogeneity from spinach roots using a procedure devised for leaves. The root thioredoxin (h2 form) differed from chloroplast and animal thioredoxins in showing an atypical active site (Cys-Ala-Pro-Cys) but otherwise resembled animal thioredoxin in structure. Sequence data for a total of 72 residues of spinach root thioredoxin h2 (about 69% of the primary structure) showed 43-44% identity with rabbit and rat thioredoxin. Analysis of cell fractions from the endosperm of germinating castor beans revealed that thioredoxin h occurs in the cytosol, endoplasmic reticulum, and mitochondria. The present findings demonstrate a similarity between plant thioredoxin h and animal thioredoxins in structure and intracellular location and raise the question of whether these proteins have similar functions.