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The Ydj1 molecular chaperone facilitates formation of active p60v-src in yeast

B Dey1, A J Caplan, F Boschelli

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

Insights

Yeast dnaJ homologue YDJ1 (Ydj1p) assists in forming active p60v-src tyrosine kinase. While not essential, Ydj1p

Area of Science:

  • Molecular biology
  • Cellular biology
  • Biochemistry

Background:

  • Molecular chaperones, including Hsp90, are crucial for active p60v-src tyrosine kinase formation.
  • Expression of p60v-src in Saccharomyces cerevisiae leads to cell death, dependent on Hsp90 function.

Purpose of the Study:

  • To investigate the role of the yeast dnaJ homologue YDJ1 (Ydj1p) in the formation and activity of p60v-src.
  • To determine if Ydj1p is essential or facilitative for p60v-src function and associated cellular effects.

Main Methods:

  • Utilizing Saccharomyces cerevisiae strains with mutations in YDJ1 (ydj1-39, ydj1-151) and a ydj1 null mutant.
  • Assessing p60v-src mRNA and protein levels, kinase activity in vivo, and co-immunoprecipitation with chaperones Hsp90 and Hsp70.

Main Results:

  • Mutations in YDJ1 suppress p60v-src-induced lethality.
  • A specific ydj1 mutant (ydj1-39) showed reduced p60v-src levels, while a null mutant had normal active p60v-src, indicating Ydj1p facilitates but is not essential.
  • Another ydj1 mutant (ydj1-151) exhibited reduced p60v-src activity in vivo, with increased Hsp90 and Hsp70 association, and Ydj1p was detected in p60v-src complexes.

Conclusions:

  • Ydj1p plays a facilitative role in the formation of active p60v-src tyrosine kinase.
  • Ydj1p functions within molecular chaperone complexes, likely involving Hsp90 and Hsp70, to modulate p60v-src activity.

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