Protein folding activity of hsp70 is modified differentially by the hsp40 co-chaperones sis1 and ydj1*

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• who: Zhen Lu from the cient at refolding itParadoxically, Sis, and Ydj, bind chemically denatured luciferase in a similar manner. Because Sis, lacks the zinc finger-like domain that is present in Ydj1, this structural dissimilarity may account for differences in the activities of these chaperones. Indeed, mutation of the zinc fingerlike region of Ydj, reduces its ability to assist Hsp, in refolding luciferase about, fold but does not significantly reduce its ability to bind denatured protein (24). How the zinc finger-like region enhances the protein folding activity of Ydj, is unknown. We identified the conserved . . .
  

   

  

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