Abstract
Nuclear protein import can be separated into two distinct steps: binding to the nuclear pore complex followed by translocation to the nuclear interior. A previously identified nuclear location sequence (NLS) receptor and a 97-kD protein purified from bovine erythrocytes reconstitute the binding step in a permeabilized cell assay. Binding to the envelope is specific for a functional SV-40 large T antigen NLS and is not ATP or temperature dependent. Modification of p97 with N-ethylmaleimide (NEM) decreases binding to the pore, but interestingly, NEM treatment of the NLS receptor does not. Nuclear envelope binding is inhibited by wheat germ agglutinin suggesting a possible mechanism for the inhibition of transport by the lectin.
Original language | English (US) |
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Pages (from-to) | 547-555 |
Number of pages | 9 |
Journal | Journal of Cell Biology |
Volume | 125 |
Issue number | 3 |
DOIs | |
State | Published - May 1994 |
ASJC Scopus subject areas
- Cell Biology