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Centromere function on minichromosomes isolated from budding yeast

J Kingsbury1, D Koshland

  • 1Department of Embryology, Carnegie Institute of Washington, Baltimore, Maryland 21210.

Molecular Biology of the Cell
|August 1, 1993
PubMed
Summary
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Budding yeast minichromosomes reveal centromere structure. Centromere-microtubule binding is stable, ATP-inhibited, and salt-sensitive, suggesting a two-domain model for centromere function.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Centromeres are crucial for chromosome segregation during mitosis.
  • They comprise centromere DNA (CEN DNA) and proteins, mediating microtubule attachment.
  • Understanding centromere assembly and function is key to cell division.

Purpose of the Study:

  • To investigate the properties of in vivo assembled centromeres using budding yeast minichromosomes.
  • To determine factors influencing centromere-microtubule binding activity.
  • To elucidate the structural organization of the yeast centromere.

Main Methods:

  • Isolation of budding yeast minichromosomes with intact centromeres.
  • In vitro binding assays of minichromosomes to microtubules.

Related Experiment Videos

  • Analysis of binding under varying salt concentrations, competitor DNA, and ATP levels.

    • Main Results:

    • Centromere-microtubule binding is independent of chromosomal DNA topology and telomere proximity.
    • Binding is stable against competitor CEN DNA, indicating a strong protein-DNA complex.
    • Binding efficiency depends on microtubule concentration and is inhibited by ATP.
    • Salt concentration affects binding, dissociating some factors from CEN DNA.

    Conclusions:

    • The yeast centromere has a stable core of CEN DNA and binding proteins.
    • A distinct second domain mediates microtubule interactions, functioning like a motor protein.
    • This two-domain model provides insight into the molecular mechanisms of chromosome segregation.