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Nucleolar specific acidic phosphoprotein C23 is highly methylated

M A Lischwe, K D Roberts, L C Yeoman

    The Journal of Biological Chemistry
    |December 25, 1982
    PubMed
    Summary

    Protein C23 is a major nucleolar phosphoprotein in Novikoff hepatoma cells. This highly phosphorylated and methylated protein contains significant levels of NG,NG-dimethylarginine.

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    Purification of a group of HeLa nuclear proteins that bind to a regulatory element (-1430/-1327) of the human proliferating cell nucleolar protein P120 gene.

    Biochemical and biophysical research communications·1991

    Area of Science:

    • Molecular Biology
    • Cell Biology
    • Biochemistry

    Background:

    • The nucleolus is a key cellular organelle involved in ribosome biogenesis.
    • Identifying major nucleolar proteins is crucial for understanding nucleolar function.
    • Novikoff hepatoma cells provide a model system for studying nucleolar composition.

    Purpose of the Study:

    • To characterize the major phosphoprotein in Novikoff hepatoma cell nucleoli.
    • To determine the biochemical properties of this major nucleolar protein, designated Protein C23.

    Main Methods:

    • Biochemical analysis of nucleolar proteins from Novikoff hepatoma cells.
    • Quantification of phosphorylation and methylation levels.
    • Identification of specific methylated amino acid residues.

    Main Results:

    • Protein C23 was identified as the major phosphoprotein in Novikoff hepatoma cell nucleoli, accounting for 9.5% of total nucleolar protein.
    • Protein C23 has a molecular weight of 110,000 and an isoelectric point of 5.5.
    • The protein is highly phosphorylated (1.2 mol % phosphoserine) and methylated, containing 1.3 mol % NG,NG-dimethylarginine and trace NG-monomethylarginine.

    Conclusions:

    • Protein C23 is a significant and highly modified component of the nucleolus in Novikoff hepatoma cells.
    • The extensive phosphorylation and methylation suggest a regulatory role for Protein C23 within the nucleolus.
    • Further investigation into Protein C23's function is warranted based on its abundance and modification status.

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