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Related Experiment Videos

Ribosome conformational changes associated with protein S6 phosphorylation.

R Kisilevsky, M A Treloar, L Weiler

    The Journal of Biological Chemistry
    |January 25, 1984
    PubMed
    Summary

    Rat liver ribosomal proteins undergo conformational changes when S6 is phosphorylated. This affects the accessibility of specific small and large subunit proteins, indicating a dynamic ribosomal structure.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Background:

    • Ribosomes are essential for protein synthesis.
    • Ribosomal protein S6 phosphorylation is a key regulatory event.
    • Understanding ribosomal structure dynamics is crucial for comprehending gene expression regulation.

    Purpose of the Study:

    • To investigate the impact of S6 phosphorylation on rat liver ribosomal protein accessibility.
    • To identify specific ribosomal proteins involved in conformational changes.

    Main Methods:

    • Utilized reductive methylation to assess protein accessibility in rat liver ribosomes.
    • Compared accessibility in unphosphorylated and phosphorylated S6 ribosome states.

    Main Results:

    • Phosphorylation of S6 altered the accessibility of several ribosomal proteins.
    • Specifically, small subunit proteins S3, S4, S7, and S23/24, and large subunit proteins L9, L10, L12, L18, L27, L34, and L36 showed altered accessibility.
    • These changes suggest a ribosomal conformational shift.

    Conclusions:

    • S6 phosphorylation induces significant conformational changes in rat liver ribosomes.
    • Specific ribosomal proteins are implicated in mediating these structural rearrangements.
    • This highlights the dynamic nature of ribosomes in response to cellular signaling.

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