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J Biol Chem, Vol. 274, Issue 32, 22610-22617, August 6, 1999
From the Nuclear Signalling Laboratory, Division for Biochemistry
and Molecular Biology, John Curtin School of Medical Research, Canberra
ACT 2601, Australia, § Department of Energy Plant Research
Laboratory, Michigan State University, East Lansing, Michigan
48824-1312, ¶ BGFA, Bochum, Germany D-44789, and the Nuclear import of conventional nuclear
localization sequence (NLS)-containing proteins initially involves
recognition by the importin (IMP)
Plant Importin
Binds Nuclear Localization Sequences with
High Affinity and Can Mediate Nuclear Import Independent of
Importin 
, Center
for Cell Signalling, University of Virginia, Charlottesville, Virginia
22908
/
heterodimer, where IMP
binds the NLS and IMP targets the IMP/NLS-containing protein
complex to the nuclear pore. Here we examine IMP from the plant
Arabidopsis thaliana (At-IMP), which exhibits nuclear
envelope localization typical of IMP rather than IMP in other
eukaryotic cell systems. We show that At-IMP recognizes conventional
NLSs of two different types with high affinity (Kd
of 5-10 nM), in contrast to mouse IMP (m-IMP), which
exhibits much lower affinity (Kd of 50-70
nM) and only achieves high affinity in the presence of m-IMP. Unlike m-IMP, At-IMP is thus a high affinity NLS
receptor in the absence of IMP. Interestingly, At-IMP was also
able to bind with high affinity to NLSs recognized specifically by
m-IMP and not m-IMP, including that of the maize transcription
factor Opaque-2. Reconstitution of nuclear import in vitro
indicated that in the absence of exogenous IMP subunit but dependent
on RanGDP and NTF2, At-IMP was able to mediate nuclear accumulation to levels comparable with those mediated by m-IMP/. Neither m-IMP nor - was able to mediate nuclear import in the absence of
the other subunit. At-IMP's novel NLS recognition and nuclear transport properties imply that plants may possess an IMP-mediated nuclear import pathway independent of IMP in addition to that mediated by IMP/.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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