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PMID: 3119324 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The nuclear migration signal of Xenopus laevis nucleoplasmin.

The EMBO journal ·Vol. 6 ·No. 9 ·1987-09-00 ·Pages 2617-25

Bürglin TR, De Robertis EM

Abstract

Nucleoplasmin is the most abundant protein in the nucleus of Xenopus laevis oocytes. Its ability to target to the nucleus when microinjected into the cytoplasm has been the subject of many studies central to our understanding of how proteins segregate into nuclei. Using a cDNA clone we constructed beta-galactosidase-nucleoplasmin hybrids in modified bacterial expression vectors. The fusion proteins were expressed in Escherichia coli, purified and injected into the cytoplasm of X. laevis oocytes. The distribution of the fusion proteins between the cytoplasmic and nuclear compartments were analysed after incubation of various lengths of time. The results show that the signal sequence for nuclear transport is located close to the carboxy terminus of the protein. The signal sequence has been mapped to a small stretch of amino acids, containing a stretch of four lysines analogous to the SV40 large-T antigen signal.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Chromosome Deletion Cloning, Molecular Escherichia coli/genetics Female Genes Genetic Vectors Molecular Sequence Data Nuclear Proteins/genetics,physiology Nucleoplasmins Oocytes/metabolism Phosphoproteins Protein Biosynthesis Transcription, Genetic Xenopus laevis beta-Galactosidase/genetics
Chemicals
Nuclear Proteins Nucleoplasmins Phosphoproteins beta-Galactosidase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bürglin T R
Biocenter of the University of Basel, Switzerland.
De Robertis E M
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1987-09-00
Pages
2617-25
Language
English
Region
England
NLM ID
8208664
PMCID
PMC553682
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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