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Related Experiment Videos

Cdc16p, Cdc23p and Cdc27p form a complex essential for mitosis

J R Lamb1, W A Michaud, R S Sikorski

  • 1Department of Molecular Biology and Genetics, Johns Hopkins University, School of Medicine, Baltimore, MD 21205.

The EMBO Journal
|September 15, 1994
PubMed
Summary

Essential yeast proteins Cdc16p, Cdc23p, and Cdc27p form a complex crucial for cell division. A mutation in Cdc27p

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Cdc16p, Cdc23p, and Cdc27p are vital proteins for cell cycle progression in Saccharomyces cerevisiae.
  • These proteins feature multiple tetratricopeptide repeats (TPRs), known for mediating protein interactions.

Purpose of the Study:

  • To investigate the interactions between Cdc16p, Cdc23p, and Cdc27p.
  • To determine the role of TPR domains in mediating these protein-protein interactions.
  • To elucidate the significance of these interactions for mitotic progression.

Main Methods:

  • In vivo two-hybrid analysis to study protein interactions within yeast cells.
  • In vitro co-immunoprecipitation assays to confirm interactions in a cell-free system.
  • Analysis of a temperature-sensitive mutation in the Cdc27p TPR domain.

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Main Results:

  • Cdc16p, Cdc23p, and Cdc27p form a macromolecular complex through self-association and mutual interaction.
  • A specific mutation in the Cdc27p TPR domain significantly impaired its interaction with Cdc23p.
  • This mutation did not affect interactions with wild-type Cdc27p or Cdc16p, indicating interaction specificity.

Conclusions:

  • Tetratricopeptide repeats (TPRs) are critical for mediating specific protein-protein interactions within the Cdc16p-Cdc23p-Cdc27p complex.
  • The identified mutation highlights an essential interaction required for yeast cell cycle progression.
  • The conservation of these proteins suggests the complex's fundamental role in mitosis across eukaryotes.