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Related Experiment Videos

Yeast mitochondria contain ATP-sensitive, reversible actin-binding activity

D A Lazzarino1, I Boldogh, M G Smith

  • 1Department of Anatomy and Cell Biology, Columbia University College of Physicians and Surgeons, New York, New York 10032.

Molecular Biology of the Cell
|July 1, 1994
PubMed
Summary

Yeast mitochondria bind to actin filaments via ATP-sensitive surface proteins. This interaction is crucial for mitochondrial distribution during cell division, as shown by defects in actin mutants.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Mitochondria are essential organelles involved in cellular energy production.
  • Actin filaments (microfilaments) are key components of the cytoskeleton, providing structure and facilitating intracellular transport.
  • The precise mechanisms governing the interaction between mitochondria and the actin cytoskeleton in yeast are not fully understood.

Purpose of the Study:

  • To investigate and characterize the binding interactions between isolated yeast mitochondria and F-actin.
  • To identify the molecular basis and functional significance of these actin-mitochondrial interactions in yeast.

Main Methods:

  • Sedimentation assays were employed to analyze the binding of isolated yeast mitochondria to stabilized yeast F-actin.

Related Experiment Videos

  • Protease digestion of mitochondrial outer membrane proteins and saturation of actin-binding sites with myosin S1 subfragment were used to probe the binding interface.
  • Subcellular fractionation was performed to assess co-purification of actin with mitochondria.
  • A yeast mutant with a temperature-sensitive mutation in the ACT1 gene (act1-3) was utilized to study the in vivo relevance of actin-mitochondrial interactions.

    • Main Results:

    • Yeast mitochondria bind to F-actin in an ATP-sensitive, saturable, and reversible manner, independent of mitochondrial membrane potential.
    • Binding is mediated by proteins on the mitochondrial outer membrane and can be blocked by protease treatment or myosin S1 subfragment.
    • Actin was found to co-purify with mitochondria and could be released by ATP treatment, suggesting in vivo interactions.
    • The act1-3 mutant exhibited temperature-dependent defects in mitochondrial transfer from mother cells to daughter buds during mitosis.

    Conclusions:

    • A mitochondrial surface protein(s) mediates ATP-sensitive binding to the lateral surface of F-actin filaments.
    • These findings suggest that actin-mitochondrial interactions occur in intact yeast cells and are important for mitochondrial distribution.
    • The study highlights a functional link between actin dynamics and mitochondrial inheritance during yeast cell division.