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Gene Review

LOC397921  -  nucleoplasmin

Xenopus laevis

 
 
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Disease relevance of LOC397921

  • Selective accumulation of fluorescent nucleoplasmin is observed microscopically within 30 min with rat liver nuclei, Xenopus embryonic nuclei, regrown Xenopus sperm nuclei, or nuclei reconstituted in vitro from bacteriophage lambda DNA [1].
  • In another set of experiments, fluorescently labeled nucleoplasmin was injected, alone or together with WGA, into the cytoplasm of rat hepatoma cells, and its nucleocytoplasmic distribution was studied by quantitative laser fluorescence microscopy [2].
  • Wheat germ agglutinin (WGA) blocked the nuclear transport of nucleoplasmin, a nuclear protein of Xenopus laevis oocytes, and of nonnuclear proteins conjugated with a synthetic peptide containing the nuclear localization signal sequence for simian virus 40 (SV40) large T antigen [3].
  • Fourier transform infrared spectroscopy, circular dichroism and prediction techniques have been used to investigate the conformational properties of nucleoplasmin isolated from oocytes and eggs of Xenopus. laevis and overexpressed in Escherichia coli [4].
 

High impact information on LOC397921

 

Biological context of LOC397921

  • The mRNA is detected during oogenesis but not during embryogenesis, suggesting that nucleoplasmin may be an exclusively maternally expressed gene [8].
  • In this work, we show that the mutation of only four acidic amino acid residues of the small A1 tract drastically reduces nucleoplasmin decondensing activity, pointing out this region as the potential binding site for sperm proteins [9].
  • Novobiocin, an inhibitor of prokaryotic DNA gyrase and eukaryotic type II topoisomerase enzymes, interferes with in vitro chromatin assembly using purified histones, DNA and nucleoplasmin [10].
  • Assembly in vitro of nuclei active in nuclear protein transport: ATP is required for nucleoplasmin accumulation [11].
  • Nucleoplasmin regulates chromatin condensation during apoptosis [12].
 

Anatomical context of LOC397921

 

Associations of LOC397921 with chemical compounds

  • The following experimental procedure was employed: Colloidal gold particles, varying in size from approximately 20 to 170 A in diameter were coated with nucleoplasmin, a 165,000-mol-wt karyophilic protein, which is known to be transported through the envelope [17].
  • Colloidal gold coated with trypsin-digested nucleoplasmin (which lacks the polypeptide domain required for transport) or exogenous polyvinylpyrrolidone were largely excluded from the nucleus and showed no evidence of transport [17].
  • The properties of the carboxy-terminal domain of H1 and the possible involvement of the amino acids lysine, proline and alanine in migration are discussed and compared with those of a domain that specifies migration of nucleoplasmin into the oocyte nucleus [18].
  • Its relative molecular weight of 130,000-170,000, as determined by gel filtration, sucrose density gradient centrifugation, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the cross-linked complexes, excludes the association of a histone octamer with nucleoplasmin [19].
  • We find that the pentameric form of egg nucleoplasmin exhibits an apparent molecular mass approximately 15 000 daltons larger than its oocyte counterpart upon sodium dodecyl sulfate (SDS)-acrylamide gel electrophoresis [20].
 

Other interactions of LOC397921

 

Analytical, diagnostic and therapeutic context of LOC397921

References

  1. In vitro transport of a fluorescent nuclear protein and exclusion of non-nuclear proteins. Newmeyer, D.D., Finlay, D.R., Forbes, D.J. J. Cell Biol. (1986) [Pubmed]
  2. Inhibition of nuclear accumulation of karyophilic proteins in living cells by microinjection of the lectin wheat germ agglutinin. Dabauvalle, M.C., Schulz, B., Scheer, U., Peters, R. Exp. Cell Res. (1988) [Pubmed]
  3. Reversible inhibition of protein import into the nucleus by wheat germ agglutinin injected into cultured cells. Yoneda, Y., Imamoto-Sonobe, N., Yamaizumi, M., Uchida, T. Exp. Cell Res. (1987) [Pubmed]
  4. Structural and functional properties of Escherichia coli-derived nucleoplasmin. A comparative study of recombinant and natural proteins. Hierro, A., Arizmendi, J.M., De Las Rivas, J., Urbaneja, M.A., Prado, A., Muga, A. Eur. J. Biochem. (2001) [Pubmed]
  5. Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence. Robbins, J., Dilworth, S.M., Laskey, R.A., Dingwall, C. Cell (1991) [Pubmed]
  6. Nuclear protein migration involves two steps: rapid binding at the nuclear envelope followed by slower translocation through nuclear pores. Richardson, W.D., Mills, A.D., Dilworth, S.M., Laskey, R.A., Dingwall, C. Cell (1988) [Pubmed]
  7. Sequential binding of import ligands to distinct nucleopore regions during their nuclear import. Panté, N., Aebi, U. Science (1996) [Pubmed]
  8. Cloning of nucleoplasmin from Xenopus laevis oocytes and analysis of its developmental expression. Bürglin, T.R., Mattaj, I.W., Newmeyer, D.D., Zeller, R., De Robertis, E.M. Genes Dev. (1987) [Pubmed]
  9. Mutation of the small acidic tract A1 drastically reduces nucleoplasmin activity. Salvany, L., Chiva, M., Arnan, C., Ausió, J., Subirana, J.A., Saperas, N. FEBS Lett. (2004) [Pubmed]
  10. Novobiocin inhibits passive chromatin assembly in vitro. Sealy, L., Cotten, M., Chalkley, R. EMBO J. (1986) [Pubmed]
  11. Assembly in vitro of nuclei active in nuclear protein transport: ATP is required for nucleoplasmin accumulation. Newmeyer, D.D., Lucocq, J.M., Bürglin, T.R., De Robertis, E.M. EMBO J. (1986) [Pubmed]
  12. Nucleoplasmin regulates chromatin condensation during apoptosis. Lu, Z., Zhang, C., Zhai, Z. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  13. The effects of variations in the number and sequence of targeting signals on nuclear uptake. Dworetzky, S.I., Lanford, R.E., Feldherr, C.M. J. Cell Biol. (1988) [Pubmed]
  14. Purification of a novel, nucleoplasmin-like protein from somatic nuclei. Cotten, M., Chalkley, R. EMBO J. (1987) [Pubmed]
  15. Three-dimensional visualization of the route of protein import: the role of nuclear pore complex substructures. Rutherford, S.A., Goldberg, M.W., Allen, T.D. Exp. Cell Res. (1997) [Pubmed]
  16. Characterization of the ooplasmic factor inducing decondensation of and protamine removal from toad sperm nuclei: involvement of nucleoplasmin. Ohsumi, K., Katagiri, C. Dev. Biol. (1991) [Pubmed]
  17. Movement of a karyophilic protein through the nuclear pores of oocytes. Feldherr, C.M., Kallenbach, E., Schultz, N. J. Cell Biol. (1984) [Pubmed]
  18. Accumulation of the isolated carboxy-terminal domain of histone H1 in the Xenopus oocyte nucleus. Dingwall, C., Allan, J. EMBO J. (1984) [Pubmed]
  19. Co-existence of two different types of soluble histone complexes in nuclei of Xenopus laevis oocytes. Kleinschmidt, J.A., Fortkamp, E., Krohne, G., Zentgraf, H., Franke, W.W. J. Biol. Chem. (1985) [Pubmed]
  20. Xenopus nucleoplasmin: egg vs. oocyte. Sealy, L., Cotten, M., Chalkley, R. Biochemistry (1986) [Pubmed]
  21. The nuclear-cytoplasmic distribution of the Xenopus nuclear factor, xnf7, coincides with its state of phosphorylation during early development. Miller, M., Reddy, B.A., Kloc, M., Li, X.X., Dreyer, C., Etkin, L.D. Development (1991) [Pubmed]
  22. Association of nucleoplasmin with transcription products as revealed by immunolocalization in the amphibian oocyte. Moreau, N., Angelier, N., Bonnanfant-Jais, M.L., Gounon, P., Kubisz, P. J. Cell Biol. (1986) [Pubmed]
  23. Regulated unmasking of in vivo synthesized maternal mRNA at oocyte maturation. A role for the chaperone nucleoplasmin. Meric, F., Matsumoto, K., Wolffe, A.P. J. Biol. Chem. (1997) [Pubmed]
  24. The characterization of amphibian nucleoplasmins yields new insight into their role in sperm chromatin remodeling. Frehlick, L.J., Eirín-López, J.M., Jeffery, E.D., Hunt, D.F., Ausió, J. BMC Genomics (2006) [Pubmed]
 
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