Interdependence between a 55 kDa protein (p55) and a 12 kDa protein (p12) in facilitating the nuclear entry of goat uterine estrogen receptor under cell-free conditions.

Abstract

A 55 kDa nuclear localization signal binding protein (p55) is involved in the transport of the goat uterine estrogen receptor from the cytoplasm to the nuclear pore complex (NPC). p55 forms a complex with a 12 kDa protein (p12) which in turn becomes 'docked' at the NPC. The present study reports on the purification and functional characterization of p12. Both p55 and p12 are Mg2+-dependent ATPases. The protein-protein interactions that take place between these two molecules at the NPC cause an enhancement in the net ATPase activity associated with the protein complex. Presumably, this enhanced ATPase function helps in the final nuclear entry of the estrogen receptor; p55 remains associated with p12 at the nuclear entry site under these conditions.