Two cytosolic fractions (A and B) from Xenopus oocytes are sufficient
to support protein import into the nuclei of digitonin-permeabilized c
ells1. Fraction A recognizes the nuclear localization sequence (NLS) a
nd binds the import substrate to the nuclear envelope, whereas fractio
n B mediates the subsequent passage of the bound substrate into the nu
cleus. Here we report that two interacting components are required for
full fraction-B activity, purify one of these components to homogenei
ty, and show that it is the highly abundant GTP-binding protein Ran (R
as-related nuclear protein)/TC4.