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Related Experiment Videos

Structure and function of chicken gizzard myosin.

H Suzuki, H Onishi, K Takahashi

    Journal of Biochemistry
    |December 1, 1978
    PubMed
    Summary

    Chicken gizzard myosin thick filaments disassemble with ATP, forming dimers with low ATPase activity. Phosphorylation of myosin light chains creates ATP-resistant filaments, preventing dimer formation and maintaining ATPase activity.

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    Area of Science:

    • Biochemistry
    • Muscle Physiology
    • Molecular Biology

    Background:

    • Chicken gizzard myosin thick filaments readily disassemble with ATP.
    • ATP-disassembled gizzard myosin exhibits significantly lower ATPase activity compared to KCl-disassembled myosin.

    Purpose of the Study:

    • Investigate the structural states of unphosphorylated gizzard myosin thick filaments.
    • Determine the effect of phosphorylation on gizzard myosin thick filament stability and ATPase activity.

    Main Methods:

    • Ultracentrifugation to analyze myosin forms.
    • Preparation of thick filaments under varying conditions.
    • ATPase activity assays.

    Main Results:

    • Unphosphorylated gizzard myosin thick filaments, regardless of structure, disassemble with ATP into dimers.
    • Dimeric gizzard myosin shows markedly reduced Mg-ATPase activity compared to monomeric form.
    • Phosphorylation of myosin light chains yields ATP-resistant thick filaments.
    • Skeletal L-meromyosin forms ATP-resistant hybrid filaments, preserving gizzard myosin ATPase activity at low ionic strength.

    Conclusions:

    • Gizzard myosin thick filament stability and ATPase activity are regulated by phosphorylation.
    • Myosin dimerization, induced by ATP in unphosphorylated myosin, causes significant ATPase activity depression.
    • Phosphorylation prevents ATP-induced disassembly and activity loss, suggesting a regulatory role in muscle function.

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