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Related Experiment Videos

RNA binding fragments from nucleolin contain the ribonucleoprotein consensus sequence.

B Bugler, H Bourbon, B Lapeyre

    The Journal of Biological Chemistry
    |August 15, 1987
    PubMed
    Summary

    Nucleolin, a key nucleolar protein, binds ribosomal RNA. Researchers identified its RNA-binding region in the carboxyl-terminal domain, revealing conserved RNA-binding structures in proteins.

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    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Cell Biology

    Background:

    • Nucleolin is a major nucleolar phosphoprotein.
    • Its primary structure and association with preribosomal RNA are known.

    Purpose of the Study:

    • To identify the RNA binding region of nucleolin.
    • To investigate the structural basis of RNA binding.

    Main Methods:

    • Cyanogen bromide fragmentation of nucleolin.
    • "Western blotting" technique to test RNA binding of fragments.
    • Protein sequencing to localize fragments.
    • Sequence analysis for ribonucleoprotein consensus sequences.

    Main Results:

    • Nucleolin fragments of 13, 33, and 47 kDa bound both 18 S and 28 S ribosomal RNA.

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  • These RNA-binding fragments were localized to the carboxyl-terminal two-thirds of nucleolin.
  • Four copies of an 11-residue sequence, related to the ribonucleoprotein consensus sequence, were found in the RNA-binding region.

    • Conclusions:

    • The carboxyl-terminal region of nucleolin is responsible for RNA binding.
    • Nucleolin utilizes a conserved structure for binding different classes of RNA.
    • This conserved RNA-binding structure may be shared by other proteins.