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PLANT PHYSIOLOGY , Vol 103, Issue 3 719-726, Copyright © 1993 by American Society of Plant Biologists
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METABOLISM AND ENZYMOLOGY |
Expression and Localization of Plant Protein Disulfide Isomerase
B. S. Shorrosh, J. Subramaniam, K. R. Schubert and R. A. Dixon
Plant Biology Division, The Samuel Roberts Noble Foundation, Ardmore, Oklahoma 73402 (B.S.S., R.A.D.)
A cDNA clone encoding a putative protein disulfide isomerase (PDI, EC
5.3.4.1) from alfalfa (Medicago sativa L.) was expressed in Escherichia
coli cells, and an antiserum was raised against the expressed PDI-active
protein. The antiserum recognized a protein of approximately 60 kD in
extracts from alfalfa, soybean, and tobacco roots and stems. Levels of this
protein remained relatively constant on exposure of alfalfa cell suspension
cultures to the protein glycosylation inhibitor tunicamycin, whereas a
slightly lower molecular mass form, also detected by the antiserum, was
induced by this treatment. A lower molecular mass form of PDI was also
observed in roots of alfalfa seedlings during the first 5 weeks after
germination. PDI levels increased in developing soybean seeds up to 17 d
after fertilization and then declined. Tissue print immunoblots revealed
highest levels of PDI protein in the cambial tissues of soybean stems and
petioles and in epidermal, subepidermal, cortical, and pith tissues of
stems of alfalfa and tobacco. Immunogold electron microscopy confirmed the
localization of PDI to the endoplasmic reticulum in soybean root nodules.
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