A domain distinct from nucleoplasmin's nuclear localization sequence influences its transport.
We constructed mutants of the prototypical, nuclear-accumulating protein nucleoplasmin and used them in both in vivo and in vitro nuclear transport assays to search for transport-influencing domains distinct from this protein's recognized nuclear localization sequence. We identified the polyglutamic acid tract on the amino flank of the nuclear localization sequence as being involved in two stages of nuclear transport. This poly-glu tract is required for the facilitated translocation of nucleoplasmin through the nuclear pore complex, and it also enhances the subsequent binding of nucleoplasmin within the nucleus.
Vancurova
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Department of Biological Sciences, St. John's University, Jamaica, New York 11439, USA.
Vancura
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Lou
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Paine
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PL
D000818:Animals; D001692:Biological Transport; D002467:Cell Nucleus / Q000378:metabolism*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D019913:Nuclear Localization Signals; D009687:Nuclear Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D056489:Nucleoplasmins; D009865:Oocytes / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011099:Polyglutamic Acid / Q000737:chemistry* / Q000378:metabolism; D017384:Sequence Deletion; D014981:Xenopus
D019913:Nuclear Localization Signals; D009687:Nuclear Proteins; D056489:Nucleoplasmins; D010750:Phosphoproteins; D011099:Polyglutamic Acid