[HTML][HTML] Stoichiometry, abundance, and functional significance of the hsp90/hsp70-based multiprotein chaperone machinery in reticulocyte lysate
PJM Murphy, KC Kanelakis, MD Galigniana… - Journal of Biological …, 2001 - ASBMB
Rabbit reticulocyte lysate contains a multiprotein chaperone system that assembles the
glucocorticoid receptor (GR) into a complex with hsp90 and converts the hormone binding
domain of the receptor to its high affinity steroid binding state. This system has been
resolved into five proteins, with hsp90 and hsp70 being essential and Hop, hsp40, and p23
acting as co-chaperones that optimize assembly. Hop binds independently to hsp70 and
hsp90 to form an hsp90· Hop· hsp70 complex that acts as a machinery to open up the GR …
glucocorticoid receptor (GR) into a complex with hsp90 and converts the hormone binding
domain of the receptor to its high affinity steroid binding state. This system has been
resolved into five proteins, with hsp90 and hsp70 being essential and Hop, hsp40, and p23
acting as co-chaperones that optimize assembly. Hop binds independently to hsp70 and
hsp90 to form an hsp90· Hop· hsp70 complex that acts as a machinery to open up the GR …