Evidence for a Mechanism of Repression of Heat Shock Factor 1 Transcriptional Activity by a Multichaperone Complex

In the absence of stress, human heat shock factor 1 (hHSF1) is in its unactivated form. hHSF1 polypeptide is in a dynamic heterocomplex with Hsp90 and is incapable of specifically binding DNA. When cells are stressed, heterocomplex assembly is disrupted. Unbound hHSF1 homotrimerizes, acquires DNA bi...

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Veröffentlicht in:	The Journal of biological chemistry 2001-12, Vol.276 (49), p.45791-45799
Hauptverfasser:	Guo, Yongle, Guettouche, Toumy, Fenna, Mary, Boellmann, Frank, Pratt, William B., Toft, David O., Smith, David F., Voellmy, Richard
Format:	Artikel
Sprache:	eng
Schlagworte:	Base Sequence Binding Sites DNA Primers DNA-Binding Proteins - antagonists & inhibitors DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism DNA-Binding Proteins - physiology heat shock factor 1 Heat Shock Transcription Factors HSF1 protein HSP90 Heat-Shock Proteins - physiology Humans immunophilins Protein Binding Protein Denaturation Repressor Proteins - physiology Tacrolimus Binding Proteins - metabolism Transcription Factors Transcription, Genetic - physiology
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