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J Biol Chem, Vol. 273, Issue 23, 14194-14199, June 5, 1998
From the The catalytic A subunit of ricin can inactivate
eukaryotic ribosomes, including those of Ricinus communis
where the toxin is naturally produced. How such plant cells avoid
intoxication has remained an open question. Here we report the
transient expression of a number of ricin A chain-encoding cDNA
constructs in tobacco protoplasts. Ricin A chain entered the
endoplasmic reticulum lumen, where it was efficiently glycosylated, but
it was toxic to the cells and disappeared with time in a brefeldin
A-insensitive manner, suggesting reverse translocation to the cytosol
and eventual degradation. Proricin (the natural precursor form
containing A and B chains joined together by a linker sequence) was
glycosylated, transported to the vacuole, and processed to its mature
form, but was not toxic. Free ricin A chain and proricin were not
secreted, whereas free ricin B chain was found entirely in the
extracellular medium. The coexpression of ricin A and B chains resulted
in the formation of disulfide-linked, transport-competent heterodimers,
which were secreted, with a concomitant reduction in the observed
cytotoxicity. These results suggest that the production of ricin as a
precursor is essential for its routing to the vacuole and for
protection of ricin-producing cells.
Free Ricin A Chain, Proricin, and Native Toxin Have Different
Cellular Fates When Expressed in Tobacco Protoplasts
§,,, and
Istituto Biosintesi Vegetali, Consiglio
Nazionale delle Ricerche, via Bassini 15, 20133 Milano, Italy and
the § Department of Biological Sciences, University of
Warwick, Coventry CV4 7AL, United Kingdom
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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