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Targeting of karyophilic proteins to nuclear pores is known to
require several cytoplasmic factors, including the nuclear location
signal-binding protein. Using a digitonin-permeabilized cell-free
transport assay, we have obtained a cytoplasmic fraction containing
factors that specifically bind to karyophilic protein and support the
nuclear binding step of the transport. Components in this fraction form
a stable complex with the karyophile through interaction with nuclear
location signal. Since this complex shows nuclear pore binding activity
prior to nuclear entry in the absence of other cytosolic factors, we
call it nuclear pore-targeting complex. It consists of karyophilic
protein and four proteins of 54, 56, 66, and 90 kDa. In our
reconstitution experiments, a complex with 54 and 90 kDa proteins is
capable of targeting karyophiles to the nuclear pores.
Volume 270,
Number 15,
Issue of April 14, pp. 8559-8565, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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