J Cell Biochem 1995 May 01;581:105-14. doi: 10.1002/jcb.240580113.

Intranuclear binding of nucleoplasmin.

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Many proteins--including not only structural proteins, but also enzymes, hormone receptors, and other transcription factors--accumulate to much higher nuclear than cytoplasmic concentrations. Nuclear localization sequences or signals (NLSs) within their primary structures entrain specific transport of these proteins through the nuclear pore complexes. This transport process is energy-dependent, but evidence for a true active transport mechanism is not conclusive. An alternative mechanism--facilitated transport of NLS proteins followed by their intranuclear binding--has been implicated by experiments with oil-isolated nuclei. However, there has been no agreement as to a role for binding in the in vivo nuclear accumulation of NLS-containing proteins. We demonstrate herein that a prototypical NLS protein, nucleoplasmin (Np), binds within the nucleus of the living Xenopus oocyte and that this binding accounts for its nuclear accumulation.

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Species referenced: Xenopus laevis
Genes referenced: npm1