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Related Experiment Videos

The Cdk-activating kinase (CAK) from budding yeast

P Kaldis1, A Sutton, M J Solomon

  • 1Yale University School of Medicine, Department of Molecular Biophysics and Biochemistry, New Haven, Connecticut 06520-8024, USA.

Cell
|August 23, 1996
PubMed
Summary
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Researchers purified and cloned the Cdk-activating kinase (CAK) from yeast, finding it functions differently than previously studied CAKs. This discovery challenges the role of p40MO15-cyclin H-MAT1 as a physiological CAK in vertebrates.

Area of Science:

  • Molecular Biology
  • Cell Cycle Regulation
  • Biochemistry

Background:

  • Cyclin-dependent kinases (CDKs) activation is crucial for cell cycle progression.
  • This activation requires association with cyclins and specific phosphorylation, notably at threonine residue 161 in human p34cdc2.
  • The Cdk-activating kinase (CAK) is responsible for this essential phosphorylation event.

Purpose of the Study:

  • To purify and clone the CAK from Saccharomyces cerevisiae (yeast).
  • To characterize the properties of yeast CAK (Cak1p) and compare it to CAKs from other organisms.
  • To investigate the physiological role of CAK in cell cycle regulation using genetic approaches.

Main Methods:

  • Purification and cloning of CAK from S. cerevisiae.
  • Expression of yeast CAK in E. coli to assess its activity.

Related Experiment Videos

  • Creation and analysis of a temperature-sensitive mutation in the CAK1 gene.
  • Genetic interaction studies with the CLB2 gene, encoding a major mitotic cyclin.

    • Main Results:

    • Yeast CAK (Cak1p) is active as a monomer and exhibits full activity when expressed in E. coli.
    • Unlike CAKs from other species, Cak1p is not part of the basal transcription factor TFIIH.
    • A temperature-sensitive mutation in CAK1 leads to a G2 cell cycle delay, reduced Cdc28p kinase activity, and genetic interactions with CLB2.

    Conclusions:

    • Yeast CAK (Cak1p) possesses unique biochemical and functional properties compared to CAKs from other organisms.
    • The findings suggest that the previously identified p40MO15-cyclin H-MAT1 complex in vertebrates may not be the primary physiological CAK.
    • This study opens new avenues for understanding the diverse mechanisms of CDK activation across different species.