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THE PLANT CELL, Vol 5, Issue 4 433-442, Copyright © 1993 by American Society of Plant Biologists
Protein Isoprenylation in Suspension-Cultured Tobacco Cells
S. K. Randall, M. S. Marshall and D. N. Crowell
Department of Biology, Indiana University-Purdue University at Indianapolis, Indianapolis, Indiana 46202-5132
Many mammalian and yeast proteins, including small ras-like GTP binding
proteins, heterotrimeric G protein [gamma] subunits, and nuclear lamins,
have been shown to be covalently linked to isoprenoid derivatives of
mevalonic acid. Isoprenylation of these proteins is required for their
assembly into membranes and, hence, for their biological activity. In this
report, it is shown that cultured tobacco cells, when pretreated with an
inhibitor of endogenous mevalonic acid synthesis (lovastatin), incorporate
radioactivity from 14C-mevalonic acid into proteins. Most of these proteins
are membrane associated, and many are similar in mass to mammalian ras-like
GTP binding proteins and nuclear lamins. Furthermore, it is shown that
tobacco cell extracts catalyze the transfer of radioactivity from
3H-farnesyl pyrophosphate and 3H-geranylgeranyl pyrophosphate to protein
substrates in vitro. These studies indicate the presence of at least two
distinct prenyl:protein transferases in tobacco extracts: one that utilizes
farnesyl pyrophosphate and preferentially modifies a substrate protein with
a CAIM carboxy terminus (farnesyl:protein transferase) and one that
utilizes geranylgeranyl pyrophosphate and preferentially modifies a
substrate protein with a CAIL carboxy terminus (geranylgeranyl:protein
transferase type I). This work provides a basis for future work on the role
of protein isoprenylation in plant cell growth, signal transduction, and
membrane biogenesis.
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