Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23

Brian C. Freeman, David O. Toft, Richard I. Morimoto*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

279 Scopus citations

Abstract

Molecular chaperones are essential proteins that participate in the regulation of steroid receptors in eukaryotes. The steroid aporeceptor complex contains the molecular chaperones Hsp90 and Hsp70, p48, the cyclophilin Cyp-40, and the associated proteins p23 and p60. In vitro folding assays showed that Cyp-40 and p23 functioned as molecular chaperones in a manner similar to that of Hsp90 or Hsp70. Although neither Cyp-40 nor p23 could completely refold an unfolded substrate, both proteins interacted with the substrate to maintain a nonnative folding-competent intermediate. Thus, the steroid aporeceptor complexes have multiple chaperone components that maintain substrates in an intermediate folded state.

Original languageEnglish (US)
Pages (from-to)1718-1720
Number of pages3
JournalScience
Volume274
Issue number5293
DOIs
StatePublished - Dec 6 1996

ASJC Scopus subject areas

  • General

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