Bc. Freeman et al., MOLECULAR CHAPERONE MACHINES - CHAPERONE ACTIVITIES OF THE CYCLOPHILIN CYP-40 AND THE STEROID APORECEPTOR-ASSOCIATED PROTEIN P23, Science, 274(5293), 1996, pp. 1718-1720
Molecular chaperones are essential proteins that participate in the re
gulation of steroid receptors in eukaryotes. The steroid aporeceptor c
omplex contains the molecular chaperones Hsp90 and Hsp70, p48, the cyc
lophilin Cyp-40, and the associated proteins p23 and p60. In vitro fol
ding assays showed that Cyp-40 and p23 functioned as molecular chapero
nes in a manner similar to that of Hsp90 or Hsp70. Although neither Cy
p-40 nor p23 could completely refold an unfolded substrate, both prote
ins interacted with the substrate to maintain a nonnative folding-comp
etent intermediate. Thus, the steroid aporeceptor complexes have multi
ple chaperone components that maintain substrates in an intermediate f
olded state.