Cooperative action of Hsp70, Hsp90, and DnaJ proteins in protein renaturation

Biochemistry
R J SchumacherDavid O Toft

Abstract

The proteins required for the repair of damaged proteins in the eukaryotic cytoplasm remain largely uncharacterized. The renaturation of thermally denatured firefly luciferase readily occurs in rabbit reticulocyte lysate by an ATP-dependent process. Earlier studies had shown that this chaperoning activity could be reconstituted, in part, using purified preparations of hsp70 and hsp90. We have extended the description of this system by clarifying the importance of hsp70 and hsp90 and have tested for additional factors that enhance renaturation. Using mutant hsp70 proteins, we have shown that hsp70 is required for luciferase renaturation. We have also found that hsp70 and hsp90 preparations purified by common procedures were contaminated with low levels of DnaJ proteins that are essential for the renaturing activity. When hsp70 and hsp90 preparations free of DnaJ proteins are used, the system must be supplemented with a DnaJ protein to obtain renaturation activity. The yeast DnaJ protein, YDJ-1, was found to be very effective for this purpose. Although significant renaturation can occur with only hsp70 and DnaJ proteins, hsp90 also contributes to the renaturation process, both in the complex environment of reticulocyte lysate and...Continue Reading

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