C23 interacts with B23, a putative nucleolar-localization-signal-binding protein.
The human protein C23 (nucleolin) is a major nucleolar protein. Its interactions with other proteins were studied with the two-hybrid system which identified nucleolar protein B23 (nucleophosmin) as being associated with C23. Both proteins were co-immunoprecipitated from HeLa cell nuclear extract by either monoclonal anti-C23 or monoclonal anti-B23. Binding studies ... utilizing deletion mutants indicated that the binding of C23 and B23 involves specific motifs. In addition to an approximately 46-amino-acid-binding domain in B23 (amino acids 194-239), amino acids 540-628 of C23 were required for binding; this region of C23 is required for the nucleolar localization. In addition, nucleolar protein p120 was also found to be co-immunoprecipitated with B23. A fragment of p120 containing a functional nucleolar localization signal bound to the truncated binding domain of B23, as did C23. These results suggest that the interaction of C23 and B23 may represent a nucleolar-targeting mechanism in which B23 acts as a nucleolar-localization signal-binding protein.
Mesh Terms:
Glutathione Transferase, Hela Cells, Humans, Nuclear Proteins, Nucleolus Organizer Region, Phosphoproteins, Precipitin Tests, Protein Binding, Protein Sorting Signals, RNA-Binding Proteins, Recombinant Fusion Proteins, Saccharomyces cerevisiae
Glutathione Transferase, Hela Cells, Humans, Nuclear Proteins, Nucleolus Organizer Region, Phosphoproteins, Precipitin Tests, Protein Binding, Protein Sorting Signals, RNA-Binding Proteins, Recombinant Fusion Proteins, Saccharomyces cerevisiae
Eur. J. Biochem.
Date: Apr. 01, 1996
PubMed ID: 8620867
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