A critical role for the proteasome activator PA28 in the Hsp90-dependent protein refolding.

@article{Minami2000ACR,
  title={A critical role for the proteasome activator PA28 in the Hsp90-dependent protein refolding.},
  author={Yasufumi Minami and Hisashi Kawasaki and Michiko Minami and Nobuyuki Tanahashi and Kunihiko Tanaka and Ichiro Yahara},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 12},
  pages={9055-61}
}
The 90-kDa heat shock protein, Hsp90, was previously shown to capture firefly luciferase during thermal inactivation and prevent it from undergoing an irreversible off-pathway aggregation, thereby maintaining it in a folding-competent state. While Hsp90 by itself was not sufficient to refold the denatured luciferase, addition of rabbit reticulocyte lysate remarkably restored the luciferase activity. Here we demonstrate that Hsc70, Hsp40, and the 20 S proteasome activator PA28 are the effective… CONTINUE READING
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