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A more recent version of this article appeared on February 1, 2002
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Submitted on June 22, 2001
Revised on October 26, 2001
Accepted on November 21, 2001
1 Swiss Federal Institute of Technology Zurich (ETH), Institute of Biochemistry, Universitätstr. 16, CH 8092 Zurich, Switzerland (Present address: Department of Zoology, University of British Columbia, 6270 University Boulevard, Vancouver BC, V6T 1Z4, Canada)
2 Institute of Medical Virology, Justus Liebig University, Frankfurter Str. 107, D-35392 Giessen, Germany
* Corresponding author. E-mail address: pante{at}zoology.ubc.ca.
Bidirectional transport of macromolecules between the nucleus and the cytoplasm occurs through the nuclear pore complexes (NPCs) by a signal-mediated mechanism which is directed by targeting signals (NLSs) residing on the transported molecules or 'cargoes'. Nuclear transport starts after interaction of the targeting signal with soluble cellular receptors. After the formation of the cargo-receptor complex in the cytosol, this complex crosses the NPC. Here we use gold particles of various sizes coated with cargo-receptor complexes in order to determine precisely how large macromolecules crossing the NPC by the signal-mediated transport mechanism could be. We found that cargo-receptor-gold complexes with diameter close to 39 nm could be translocated by the NPC. This implies that macromolecules much larger than the assumed functional NPC diameter of 26 nm are able to be transported into the karyoplasm. The physiological relevance of this finding was supported by the observation that intact nucleocapsids of human hepatitis B virus with diameters of 32 and 36 nm are able to cross the nuclear pore without disassembly.
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