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THE PLANT CELL, Vol 2, Issue 11 1091-1106, Copyright © 1990 by American Society of Plant Biologists
In Vitro Processing of Aleurain, a Barley Vacuolar Thiol Protease
B. C. Holwerda, N. J. Galvin, T. J. Baranski and J. C. Rogers
Division of Hematology/Oncology, Departments of Internal Medicine and Biology, Washington University School of Medicine, St. Louis, Missouri 63110
Aleurain, originally described from its cDNA as a thiol protease [Rogers,
J.C., Dean, D., and Heck, G.R. (1985). Proc. Natl. Acad. Sci. USA 82,
6512-6516], is characterized here as a glycoprotein that is targeted to a
distinct vacuolar compartment in aleurone cells. Monospecific antibodies to
a bacterial trpE-aleurain fusion protein were used to show that aleurain is
made as a 42-kilodalton (kD) proenzyme (proaleurain) that is
proteolytically processed in a post-Golgi compartment in two steps to form
a 32-kD protein. The first processing step is the discrete loss of 9 kD
from proaleurain to yield a 33-kD intermediate that is further processed by
the gradual loss of 1 kD resulting in mature 32-kD aleurain. Using
proaleurain secreted from Xenopus oocytes as a substrate, we established an
in vitro system using aleurone cell extracts that correctly processes
proaleurain to a stable protein that is indistinguishable from native
barley aleurain as judged by partial digestion with staphylococcal V8
protease. Proaleurain is not capable of self-cleavage in the absence of
aleurone cell extracts and mature aleurain appears not to participate in
processing in vitro.
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