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Gene Review

ncl  -  nucleolin

Xenopus laevis

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High impact information on LOC397919


Biological context of LOC397919

  • While the role of the C-terminal domain of nucleolin in vivo has yet to be established, our findings suggest that it may act to unfold regions of ribosomal RNA so that a second domain of nucleolin has access to its specific binding site [3].
  • This gene, designated RNP1, encodes an acidic protein that is similar in sequence to a variety of previously isolated RNA binding proteins, including nucleolin, poly (A) binding protein, and small nuclear ribonucleoproteins [4].
  • In contrast, the monoclonal antibody Nu-1H6 binds poorly to the modified forms of nucleolin arising during meiosis and mitosis [5].
  • In addition, either an acidic domain of nucleolin without phosphorylation sites, or an acidic domain containing 4 CK2 sites, or a cluster of 5 cdc2 sites was fused to the MBP-nuclear localization signal (MBP-NLS) [6].

Anatomical context of LOC397919

  • The two nucleolin polypeptides of 95 kDa and 90 kDa molecular mass are both expressed in oocytes and are found predominantly in the nucleoli [7].
  • Staining of the coilin- and Sm-depleted coiled bodies was normal with antibodies against two nucleolar proteins, fibrillarin and nucleolin [8].
  • The particle has a protein kinase activity that phosphorylates its own mRNP3+4, nucleolin, and a 31-kDa polypeptide component and exhibits translational inhibition in both the wheat germ extract and rabbit reticulocyte lysate systems [9].

Associations of LOC397919 with chemical compounds

  • The glycine-rich domain of nucleolin has an unusual supersecondary structure responsible for its RNA-helix-destabilizing properties [3].

Other interactions of LOC397919

  • Quite surprisingly, the immuno-depleted extracts still promoted the assembly of nuclear bodies which lacked either fibrillarin, nucleolin, xNopp180 or B23/NO38 [10].
  • A comparative analysis of FRGY2 and nucleolin C-terminal domains has revealed common structural features representing the signature of a particular type of auxiliary domain, which has co-evolved with the CSD and the RRM [11].

Analytical, diagnostic and therapeutic context of LOC397919

  • Direct analysis of rDNA transcription units by electron microscopy reveals that the number of polymerase complexes/rDNA unit is drastically reduced in the presence of increased amounts of nucleolin and corresponds to the level of reduction of 40 S pre-rRNA [2].


  1. Nucleolin from Xenopus laevis: cDNA cloning and expression during development. Caizergues-Ferrer, M., Mariottini, P., Curie, C., Lapeyre, B., Gas, N., Amalric, F., Amaldi, F. Genes Dev. (1989) [Pubmed]
  2. Repression of RNA polymerase I transcription by nucleolin is independent of the RNA sequence that is transcribed. Roger, B., Moisand, A., Amalric, F., Bouvet, P. J. Biol. Chem. (2002) [Pubmed]
  3. The glycine-rich domain of nucleolin has an unusual supersecondary structure responsible for its RNA-helix-destabilizing properties. Ghisolfi, L., Joseph, G., Amalric, F., Erard, M. J. Biol. Chem. (1992) [Pubmed]
  4. A protein containing conserved RNA-recognition motifs is associated with ribosomal subunits in Saccharomyces cerevisiae. Ripmaster, T.L., Woolford, J.L. Nucleic Acids Res. (1993) [Pubmed]
  5. Subcellular distribution of distinct nucleolin subfractions recognized by two monoclonal antibodies. Schwab, M.S., Gossweiler, U., Dreyer, C. Exp. Cell Res. (1998) [Pubmed]
  6. Protein phosphorylation sites regulate the function of the bipartite NLS of nucleolin. Schwab, M.S., Dreyer, C. Eur. J. Cell Biol. (1997) [Pubmed]
  7. Requirements for nuclear translocation and nucleolar accumulation of nucleolin of Xenopus laevis. Messmer, B., Dreyer, C. Eur. J. Cell Biol. (1993) [Pubmed]
  8. Coiled bodies without coilin. Bauer, D.W., Gall, J.G. Mol. Biol. Cell (1997) [Pubmed]
  9. A translation regulatory particle containing the Xenopus oocyte Y box protein mRNP3+4. Yurkova, M.S., Murray, M.T. J. Biol. Chem. (1997) [Pubmed]
  10. Prenucleolar bodies contain coilin and are assembled in Xenopus egg extract depleted of specific nucleolar proteins and U3 RNA. Bell, P., Scheer, U. J. Cell. Sci. (1997) [Pubmed]
  11. RNA-binding strategies common to cold-shock domain- and RNA recognition motif-containing proteins. Manival, X., Ghisolfi-Nieto, L., Joseph, G., Bouvet, P., Erard, M. Nucleic Acids Res. (2001) [Pubmed]
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