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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
35
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pubmed:dateCreated |
1991-1-23
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pubmed:abstractText |
Untransformed steroid receptors in cytosol preparations are associated with the 90-kDa heat shock protein hsp90, but the study of how hsp90 affects receptor function has been held back by the inability to reassociate steroid receptors with hsp90 in cell-free systems. Recently we showed (Dalman, F.C., Bresnick, E. H., Patel, P. D., Perdew, G. H., Watson, S. J., and Pratt, W. B. (1989) J. Biol. Chem. 264, 19815-19821) that glucocorticoid receptors translated in rabbit reticulocyte lysate bind to hsp90 at the termination of receptor translation. In this work we show that rabbit reticulocyte lysate promotes the temperature-dependent association of hsp90 with immunopurified mouse L cell glucocorticoid receptors. Reticulocyte lysate also promotes the temperature-dependent dissociation of hormone-free receptors from a prebound receptor-DNA complex. The glucocorticoid receptor is released from DNA in association with rabbit hsp90, and reconstitution of the receptor-hsp90 complex is accompanied by complete restitution of steroid binding activity and repression of DNA binding activity. This is the first time that transformation of a DNA-bound steroid receptor has been reversed and it raises the question of whether the same or a similar system is involved in the termination of transcriptional activation when steroid dissociates from DNA-bound receptors in intact cells.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glucocorticoids,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Glucocorticoid
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
|
pubmed:volume |
265
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
21397-400
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2254299-Animals,
pubmed-meshheading:2254299-Cell-Free System,
pubmed-meshheading:2254299-DNA,
pubmed-meshheading:2254299-DNA-Binding Proteins,
pubmed-meshheading:2254299-Glucocorticoids,
pubmed-meshheading:2254299-Heat-Shock Proteins,
pubmed-meshheading:2254299-Immunologic Techniques,
pubmed-meshheading:2254299-Macromolecular Substances,
pubmed-meshheading:2254299-Protein Binding,
pubmed-meshheading:2254299-Rabbits,
pubmed-meshheading:2254299-Receptors, Glucocorticoid
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pubmed:year |
1990
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pubmed:articleTitle |
Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex.
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pubmed:affiliation |
Department of Pharmacology, University of Michigan Medical School, Ann Arbor 48109.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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