Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope

doi:10.1083/jcb.125.3.547

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Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope

EJ Adam and SA Adam
Department of Cell, Molecular and Structural Biology, Northwestern University Medical School, Chicago, Illinois 60611.

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.
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