Both the N- and C-terminal chaperone sites of Hsp90 participate in protein refolding.

@article{Minami2001BothTN,
  title={Both the N- and C-terminal chaperone sites of Hsp90 participate in protein refolding.},
  author={Michiko Minami and Mitsuhiro Nakamura and Y. Emori and Yasufumi Minami},
  journal={European journal of biochemistry},
  year={2001},
  volume={268 8},
  pages={
          2520-4
        }
}
Hsp90 is able to bind partially unfolded firefly luciferase and maintain it in a refoldable state; the subsequent successive action of the 20S proteasome activator PA28, Hsc70 and Hsp40 enables its refolding. Hsp90 possesses two chaperone sites in the N- and C-terminal domains that prevent the aggregation of denatured proteins. Here we show that both chaperone sites of Hsp90 are effective not only in capturing thermally denatured luciferase, but also in holding it in a state prerequisite for… CONTINUE READING
BETA

Citations

Publications citing this paper.
SHOWING 1-10 OF 15 CITATIONS

Similar Papers

Loading similar papers…