Rapid translocation of NTF2 through the nuclear pore of isolated nuclei and nuclear envelopes

Affordable Access

Rapid translocation of NTF2 through the nuclear pore of isolated nuclei and nuclear envelopes

Publisher
Oxford University Press
Publication Date
Sep 16, 2002
Source
PMC
Keywords
Disciplines
  • Biology
License
Unknown

Abstract

The mechanism by which macromolecules are translocated through the nuclear pore complex (NPC) is little understood. However, recent measurements of nuclear transport in permeabilized cells showed that molecules binding to phenylalanine-glycine-rich repeats (FG repeats) in NPC proteins were translocated much faster through the NPC than molecules not interacting with FG repeats. We have studied that substrate preference of the NPC in isolated oocyte nuclei and purified nuclear envelopes by optical single transporter recording. NTF2, the transport receptor of RanGDP, was exported ∼30 times faster than green fluorescent protein, an inert molecule of approximately the same size. The data confirm that restricted diffusion of inert molecules and facilitated transport of FG-repeat binding proteins are basic types of translocation through the NPC, demonstrating that the functional integrity of the NPC can be conserved in isolated nuclei and nuclear envelopes and thus opening new avenues to the analysis of nucleocytoplasmic transport.

Report this publication

Statistics

Seen <100 times