Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins.

@article{Sun2012CharacterizationOT,
  title={Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins.},
  author={Liang Sun and Thomas Prince and Jacob R. Manjarrez and Bradley T. Scroggins and Robert L. Matts},
  journal={Biochimica et biophysica acta},
  year={2012},
  volume={1823 6},
  pages={1092-101}
}
The activator of Hsp90 ATPase, Aha1, is an Hsp90 co-chaperone that has been suggested to act as a general stimulator of Hsp90 function. In this report, we have characterized the interaction of Aha1 with Hsp90 and its co-chaperones in rabbit reticulocyte lysate (RRL) and in HeLa cell extracts. Complexes formed by Aha1 with Hsp90 in RRL were stabilized by molybdate and contained the co-chaperones FKBP52 and p23/Sba1, but lacked HOP/Sti1 and Cdc37. Aha1 complexes isolated from HeLa cell extracts… CONTINUE READING

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