Publication Date:
1996-12-06
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freeman, B C -- Toft, D O -- Morimoto, R I -- GM38109/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1718-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology and Cell Biology, Rice Institute for Biomedical Research, Northwestern University, 2153 North Campus Drive, Evanston, IL 60208, USA. r-morimoto@nwu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939864" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Isomerases/metabolism/*physiology
;
Carrier Proteins/metabolism/*physiology
;
*Cyclophilins
;
HSC70 Heat-Shock Proteins
;
HSP40 Heat-Shock Proteins
;
HSP70 Heat-Shock Proteins/metabolism
;
Heat-Shock Proteins/metabolism
;
Hot Temperature
;
Molecular Chaperones/metabolism/*physiology
;
*Peptidylprolyl Isomerase
;
Phosphoproteins/metabolism/*physiology
;
Protein Conformation
;
Protein Denaturation
;
*Protein Folding
;
Solubility
;
beta-Galactosidase/chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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