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A polysome-membrane binding system from rat liver. I. Basic characterization of the binding system.

M Takagi, M B Hoagland

    Journal of Biochemistry
    |December 1, 1975
    PubMed
    Summary
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    This study reveals that nascent protein chains on free polysomes can transfer to endoplasmic reticulum membranes during protein synthesis. Ribosomes are released, leaving the growing protein chains attached to the membrane.

    Area of Science:

    • Cell Biology
    • Molecular Biology
    • Biochemistry

    Background:

    • Polysomes, the complexes of messenger RNA and ribosomes, are involved in protein synthesis.
    • The interaction between polysomes and the endoplasmic reticulum membrane is crucial for the synthesis of specific proteins.

    Purpose of the Study:

    • To investigate the binding of polysomes to endoplasmic reticulum membranes.
    • To understand the fate of ribosomes and nascent protein chains during in vitro protein synthesis.

    Main Methods:

    • Developed a reaction system using Sephadex G-25 treated post-mitochondrial fraction (Sephadex-PM) from rat liver as a membrane source.
    • Utilized radioactive free polysomes from rat liver for in vitro experiments.

    Main Results:

    Related Experiment Videos

    • Nascent protein chains on free polysomes were transferred to membranes in vitro, a process requiring protein synthesis.
    • Polysome binding to membranes occurred in two steps: initial binding followed by ribosome release during synthesis, leaving nascent chains.
    • Some membrane-bound ribosomes released their nascent chains onto the membranes in vitro.

    Conclusions:

    • Demonstrated a mechanism for nascent chain transfer from free polysomes to ER membranes in vitro.
    • Provided insights into the dynamic interaction of polysomes with membranes during protein synthesis.