Nucleoplasmin: the archetypal molecular chaperone.
Nucleoplasmin was the first protein to be described as a molecular chaperone. Studies of nucleoplasmin have resulted in advances in two areas of cell biology. Firstly, the pathway of nucleosome assembly in Xenopus oocytes and eggs has been elucidated and is the only assembly pathway known in detail. Nucleosome assembly represents the major chaperoning function of nucleoplasmin. Secondly, nucleoplasmin has been used to elucidate the transport of proteins into the nucleus, revealing a selective entry mechanism for nuclear proteins, passage through the nuclear pore complex, and a two-step mechanism of transport. The properties and functions of nucleoplasmin are reviewed, together with other proteins which are related either structurally or functionally to nucleoplasmin.
Dingwall
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Medical Research Council, Laboratory of Molecular Biology, Cambridge, UK.
Laskey
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RA
D000818:Animals; D002352:Carrier Proteins / Q000502:physiology; D018833:Chaperonins; D015394:Molecular Structure; D009687:Nuclear Proteins / Q000737:chemistry* / Q000502:physiology; D056489:Nucleoplasmins; D009707:Nucleosomes / Q000737:chemistry; D010750:Phosphoproteins; D011506:Proteins / Q000737:chemistry* / Q000502:physiology; D012689:Sequence Homology, Nucleic Acid; D014981:Xenopus
D002352:Carrier Proteins; D009687:Nuclear Proteins; D056489:Nucleoplasmins; D009707:Nucleosomes; D010750:Phosphoproteins; D011506:Proteins; D018833:Chaperonins