The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome.

@article{Imai2003TheMC,
  title={The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome.},
  author={Jun Imai and Mikako Maruya and Hideki Yashiroda and Ichiro Yahara and Keiji Tanaka},
  journal={The EMBO journal},
  year={2003},
  volume={22 14},
  pages={3557-67}
}
Hsp90 has a diverse array of cellular roles including protein folding, stress response and signal transduction. Herein we report a novel function for Hsp90 in the ATP-dependent assembly of the 26S proteasome. Functional loss of Hsp90 using a temperature-sensitive mutant in yeast caused dissociation of the 26S proteasome. Conversely, these dissociated constituents reassembled in Hsp90-dependent fashion both in vivo and in vitro; the process required ATP-hydrolysis and was suppressed by the Hsp90… CONTINUE READING

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