Repression of Heat Shock Transcription Factor HSF1 Activation by HSP90 (HSP90 Complex) that Forms a Stress-Sensitive Complex with HSF1
Heat shock and other proteotoxic stresses cause accumulation of nonnative proteins that trigger activation of heat shock protein (Hsp) genes. A chaperone/Hsp functioning as repressor of heat shock transcription factor (HSF) could make activation of hsp genes dependent on protein unfolding. In a nove...
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| Veröffentlicht in: | Cell 1998-08, Vol.94 (4), p.471-480 |
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| creator | Zou, Jiangying Guo, Yongle Guettouche, Toumy Smith, David F Voellmy, Richard |
| description | Heat shock and other proteotoxic stresses cause accumulation of nonnative proteins that trigger activation of heat shock protein (Hsp) genes. A chaperone/Hsp functioning as repressor of heat shock transcription factor (HSF) could make activation of
hsp genes dependent on protein unfolding. In a novel in vitro system, in which human HSF1 can be activated by nonnative protein, heat, and geldanamycin, addition of Hsp90 inhibits activation. Reduction of the level of Hsp90 but not of Hsp/c70, Hop, Hip, p23, CyP40, or Hsp40 dramatically activates HSF1. In vivo, geldanamycin activates HSF1 under conditions in which it is an Hsp90-specific reagent. Hsp90-containing HSF1 complex is present in the unstressed cell and dissociates during stress. We conclude that Hsp90, by itself and/or associated with multichaperone complexes, is a major repressor of HSF1. |
| doi_str_mv | 10.1016/S0092-8674(00)81588-3 |
| format | Article |
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We conclude that Hsp90, by itself and/or associated with multichaperone complexes, is a major repressor of HSF1.</description><subject>Benzoquinones</subject><subject>Cell-Free System</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Heat Shock Transcription Factors</subject><subject>HSP90 Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Lactams, Macrocyclic</subject><subject>Models, Genetic</subject><subject>Protein Binding - drug effects</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>Quinones - pharmacology</subject><subject>Repressor Proteins - metabolism</subject><subject>Rifabutin - pharmacology</subject><subject>Transcription Factors - metabolism</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhS0EKtOWR6jkFWoXodeJndgrVI0YplKloqasLY9zozFM4mB7Cn0BnhvPD912daV7v3OO5UPIBYNPDFh93QKospB1wy8BriQTUhbVGzJjoJqCs6Z8S2YvyHtyGuMPAJBCiBNyopqy4Qpm5O8DTgFjdH6kvqdLNIm2a29_0sdgxmiDm9LutjA2-UCX7YLRG5vck9mvV8959U0BvTyMuR-mDf65ommdjRY-DJEa2qZdRNHiGF2W4n-M_nZpvfc8J-96s4n44TjPyPfFl8f5sri7_3o7v7krbH5tKhgA8gZVhV3dVT23lRS2FtZy0dhSdsoYxRXj2FdQZ1KolcRGrKqaMVWXvDojHw--U_C_thiTHly0uNmYEf026qaSEmQpXwVZLXjNVZlBcQBt8DEG7PUU3GDCs2agd0XpfVF614IG0PuidJV1F8eA7WrA7kV1bCbfPx_umL_jyWHQ0TocLXYuoE268-6VhH8d1aCn</recordid><startdate>19980821</startdate><enddate>19980821</enddate><creator>Zou, Jiangying</creator><creator>Guo, Yongle</creator><creator>Guettouche, Toumy</creator><creator>Smith, David F</creator><creator>Voellmy, Richard</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>19980821</creationdate><title>Repression of Heat Shock Transcription Factor HSF1 Activation by HSP90 (HSP90 Complex) that Forms a Stress-Sensitive Complex with HSF1</title><author>Zou, Jiangying ; Guo, Yongle ; Guettouche, Toumy ; Smith, David F ; Voellmy, Richard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c490t-100e47e93ed6d3f4c385c65cc457c28d9aa94914ef306e4759b8e75b361196243</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Benzoquinones</topic><topic>Cell-Free System</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Heat Shock Transcription Factors</topic><topic>HSP90 Heat-Shock Proteins - metabolism</topic><topic>Humans</topic><topic>Lactams, Macrocyclic</topic><topic>Models, Genetic</topic><topic>Protein Binding - drug effects</topic><topic>Protein Conformation</topic><topic>Protein Denaturation</topic><topic>Quinones - pharmacology</topic><topic>Repressor Proteins - metabolism</topic><topic>Rifabutin - pharmacology</topic><topic>Transcription Factors - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zou, Jiangying</creatorcontrib><creatorcontrib>Guo, Yongle</creatorcontrib><creatorcontrib>Guettouche, Toumy</creatorcontrib><creatorcontrib>Smith, David F</creatorcontrib><creatorcontrib>Voellmy, Richard</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zou, Jiangying</au><au>Guo, Yongle</au><au>Guettouche, Toumy</au><au>Smith, David F</au><au>Voellmy, Richard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Repression of Heat Shock Transcription Factor HSF1 Activation by HSP90 (HSP90 Complex) that Forms a Stress-Sensitive Complex with HSF1</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1998-08-21</date><risdate>1998</risdate><volume>94</volume><issue>4</issue><spage>471</spage><epage>480</epage><pages>471-480</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>Heat shock and other proteotoxic stresses cause accumulation of nonnative proteins that trigger activation of heat shock protein (Hsp) genes. 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hsp genes dependent on protein unfolding. In a novel in vitro system, in which human HSF1 can be activated by nonnative protein, heat, and geldanamycin, addition of Hsp90 inhibits activation. Reduction of the level of Hsp90 but not of Hsp/c70, Hop, Hip, p23, CyP40, or Hsp40 dramatically activates HSF1. In vivo, geldanamycin activates HSF1 under conditions in which it is an Hsp90-specific reagent. Hsp90-containing HSF1 complex is present in the unstressed cell and dissociates during stress. We conclude that Hsp90, by itself and/or associated with multichaperone complexes, is a major repressor of HSF1.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9727490</pmid><doi>10.1016/S0092-8674(00)81588-3</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Benzoquinones Cell-Free System DNA-Binding Proteins - metabolism Heat Shock Transcription Factors HSP90 Heat-Shock Proteins - metabolism Humans Lactams, Macrocyclic Models, Genetic Protein Binding - drug effects Protein Conformation Protein Denaturation Quinones - pharmacology Repressor Proteins - metabolism Rifabutin - pharmacology Transcription Factors - metabolism |
| title | Repression of Heat Shock Transcription Factor HSF1 Activation by HSP90 (HSP90 Complex) that Forms a Stress-Sensitive Complex with HSF1 |
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