Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins.

  title={Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins.},
  author={Gary A. Flom and Marta Kinga Lemieszek and E. Fortunato and J. L. Johnson},
  journal={Molecular biology of the cell},
  volume={19 12},
Ydj1 of Saccharomyces cerevisiae is an abundant cytosolic Hsp40, or J-type, molecular chaperone. Ydj1 cooperates with Hsp70 of the Ssa family in the translocation of preproteins to the ER and mitochondria and in the maturation of Hsp90 client proteins. The substrate-binding domain of Ydj1 directly interacts with steroid receptors and is required for the activity of diverse Hsp90-dependent client proteins. However, the effect of Ydj1 alteration on client interaction was unknown. We analyzed the… CONTINUE READING


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Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway.

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