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PLANT PHYSIOLOGY , Vol 108, Issue 1 327-335, Copyright © 1995 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Purification, Characterization, and Intracellular Localization of Glycosylated Protein Disulfide Isomerase from Wheat Grains
Y. Shimoni, Xz. Zhu, H. Levanony, G. Segal and G. Galili
Department of Plant Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel
Wheat (Triticum aestivum) storage proteins fold and assemble into complexes
that are linked by intra- and intermolecular disulfide bonds, but it is not
yet clear whether these processes are spontaneous or require the assistance
of endoplasmic reticulum (ER)-resident enzymes and molecular chaperones.
Aiming to unravel these processes, we have purified and characterized the
enzyme protein disulfide isomerase (PDI) from wheat endosperm, as well as
studied its developmental expression and intracellular localization. This
ER-resident enzyme was previously shown to be involved in the formation of
disulfide bonds in secretory proteins. Wheat PDI appears as a 60-kD
glycoprotein and is among the most abundant proteins within the ER of
developing grains. PDI is notably up-regulated in developing endosperm in
comparison to embryos, leaves, and roots. In addition, the increase in PDI
expression in grains appears at relatively early stages of development,
preceding the onset of storage protein accumulation by several days.
Subcellular localization analysis and immunogold labeling of electron
micrographs showed that PDI is not only present in the lumen of the ER but
is also co-localized with the storage proteins in the dense protein bodies.
These observations are consistent with the hypothesis that PDI is involved
in the assembly of wheat storage proteins within the ER.
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