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CDC37 is required for p60v-src activity in yeast

B Dey1, J J Lightbody, F Boschelli

  • 1Department of Biochemistry, Wayne State University Medical School, Detroit, Michigan 48201, USA.

Molecular Biology of the Cell
|September 1, 1996
PubMed
Summary

Mutations in the Cdc37 gene confer resistance to the toxic protein tyrosine kinase p60v-src in yeast. Cdc37 protein is essential for maintaining p60v-src solubility and activity.

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Area of Science:

  • Molecular biology
  • Yeast genetics
  • Protein biochemistry

Background:

  • The protein tyrosine kinase p60v-src is toxic in yeast.
  • Molecular chaperones like Hsp90 and Ydj1p can suppress p60v-src toxicity.
  • Cdc37 is a co-chaperone involved in Hsp90 function.

Purpose of the Study:

  • To isolate and characterize new temperature-sensitive mutants of Cdc37.
  • To investigate the role of Cdc37 in p60v-src toxicity and regulation.
  • To understand the mechanism by which Cdc37 mutations confer p60v-src resistance.

Main Methods:

  • Isolation and characterization of temperature-sensitive cdc37 mutants (cdc37-34, cdc37-17).
  • Assessment of p60v-src levels and kinase activity in mutant strains.
  • Cell cycle analysis using hydroxyurea synchronization.
  • Solubility fractionation of p60v-src using urea and detergent extraction.

Main Results:

  • Novel cdc37 mutants (cdc37-34, cdc37-17) exhibit p60v-src resistance.
  • These mutants show reduced p60v-src levels at permissive temperatures, but not sufficiently low to explain resistance.
  • Inactivation of Cdc37p at restrictive temperatures reduces p60v-src kinase activity and tyrosine phosphorylation.
  • p60v-src is enriched in urea-soluble and depleted from detergent-soluble fractions in cdc37 mutants at restrictive temperatures.

Conclusions:

  • Cdc37 is crucial for maintaining p60v-src in a soluble and active state.
  • Cdc37 mutations confer p60v-src resistance by destabilizing the kinase.
  • These findings highlight Cdc37's role as a key regulator of p60v-src activity in yeast.

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