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Wild-type proteasomes of human erythrocytes and the archaeon  Thermoplasma acidophilum  compete with each other for transport into nuclei of digitonin-permeabilized HeLa cells in the presence of an energy-regenerating system and rabbit reticulocyte lysate. ‘NLS’-mutated  Thermoplasma  proteasomes were also able to compete with human proteasomes in the same assay, although with lower efficiency. Furthermore, in contrast to the other archaeal and bacterial cell lysates tested, the  Thermoplasma  cytosol efficiently supported nuclear import of human and  Thermoplasma  proteasomes. However, the same lysate could barely direct the nuclear transport of BSA-NLS SV40  peptide conjugates or the classical NLS-bearing protein, nucleoplasmin. Finally, additional importin α/β significantly decreased the import efficiency of both human and  Thermoplasma  proteasomes. Taken together, these results suggest that nuclear import of proteasomes may use a novel pathway that is different from that of classical NLS-bearing proteins.

The Import Pathway of Human and Thermoplasma 20S Proteasomes into HeLa Cell Nuclei Is Different from That of Classical NLS-Bearing Proteins