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Actin from Saccharomyces cerevisiae.

C Greer, R Schekman

    Molecular and Cellular Biology
    |October 1, 1982
    PubMed
    Summary
    This summary is machine-generated.

    Researchers purified yeast actin, finding it similar to muscle actin but with lower affinity for muscle myosin. This study advances understanding of actin dynamics and interactions in Saccharomyces cerevisiae.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Molecular Biology

    Background:

    • Actin is a crucial protein in eukaryotic cells, involved in muscle contraction and cell motility.
    • Purification of actin from Saccharomyces cerevisiae (yeast) is challenging but essential for studying its properties.

    Purpose of the Study:

    • To purify and characterize actin from Saccharomyces cerevisiae.
    • To compare the biochemical and functional properties of yeast actin with rabbit skeletal muscle actin.

    Main Methods:

    • DNase I inhibition assay for actin purification.
    • Sodium dodecyl sulfate-gel electrophoresis for purity assessment.
    • Polymerization assays induced by KCl or Mg2+.
    • Heavy meromyosin binding and ATPase activity assays.

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  • Drug interaction studies with cytochalasin and phalloidin.

    • Main Results:

    • Yeast actin was purified to approximately 97% purity with a molecular weight of about 43,000.
    • Yeast actin formed 7-nm filaments and bound heavy meromyosin, similar to muscle actin.
    • While Vmax for heavy meromyosin ATPase activity was comparable, yeast actin showed a significantly lower affinity (higher Kapp) for muscle myosin compared to muscle actin.
    • Yeast and muscle filamentous actin responded similarly to cytochalasin and phalloidin.

    Conclusions:

    • Yeast actin shares structural and polymerization properties with muscle actin.
    • Yeast actin exhibits a lower affinity for muscle myosin, suggesting specific differences in their interaction.
    • Cytochalasin and phalloidin interact with yeast actin but do not affect yeast cell growth, indicating distinct regulatory mechanisms in vivo.