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THE PLANT CELL, Vol 8, Issue 8 1337-1352, Copyright © 1996 by American Society of Plant Biologists
Nuclear Import in Permeabilized Protoplasts from Higher Plants Has Unique Features
G. R. Hicks, HMS. Smith, S. Lobreaux and N. V. Raikhel
Michigan State University-Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824-1312
The import of proteins into the nucleus is a poorly understood process that
is thought to require soluble cytosolic factors in vertebrates and yeast.
To test this model in plants and to identify components of the import
apparatus, we developed a direct in vitro nuclear import assay by using
tobacco protoplasts that were permeabilized without detergents such as
digitonin or Triton X-100. Substrates were imported specifically by a
mechanism that required only guanine nucleotides. Moreover, in vitro import
did not require exogenous cytosol. To investigate this novel finding, we
isolated a full-length cDNA encoding an Arabidopsis homolog of vertebrate
and yeast nuclear localization signal receptors and produced an
affinity-purified antibody. The plant receptor was tightly associated with
cellular components in permeabilized protoplasts, even in the presence of
0.1% Triton X-100, indicating that this factor and probably others were
retained to an extent sufficient to support import. The lectin wheat germ
agglutinin bound to the nucleus; however, it did not block translocation in
our system, indicating that direct interaction with polysaccharide
modifications at the nuclear pore complex was probably not essential for
import in plants. Other features of in vitro import included reduced but
significant import at low temperature.
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