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 bothin vivoandin vitronuclear transport assays to search for transport-influencing domains distinct from this protein's recognized nuclear localization sequence. We identified the polyglutami...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1997-06, Vol.235 (1), p.19-25
Main Authors: Vancurova, Ivana, Vancura, Ales, Lou, Willard, Paine, Philip L.
Format: Article
Language:English
Subjects:
Animals
Biological Transport
Cell Nucleus - metabolism
Cloning, Molecular
Escherichia coli - genetics
Gene Expression
Kinetics
Mutagenesis, Site-Directed
Nuclear Localization Signals
Nuclear Proteins - chemistry
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Nucleoplasmins
Oocytes - metabolism
Phosphoproteins - chemistry
Phosphoproteins - genetics
Phosphoproteins - metabolism
Polyglutamic Acid - chemistry
Polyglutamic Acid - metabolism
Sequence Deletion
Xenopus
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Summary:We constructed mutants of the prototypical, nuclear-accumulating protein nucleoplasmin and used them in bothin vivoandin vitronuclear 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.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1997.6726