Dual control of heat shock response: involvement of a constitutive heat shock element-binding factor.
Heat shock factor (HSF) has been implicated as the key regulatory protein in the heat shock response. Our studies on the response of rodent cells to heat shock or sodium arsenite indicate that a high level of HSF-DNA-binding activity, by itself, is not sufficient for the induction of hsp70 mRNA synthesis; furthermore, a high level of HSF binding is also not necessary for this induction. Analysis of the binding of protein factors to the heat shock element (HSE) in extracts of stressed rodent cells indicates that the regulation of heat shock response involves the heat-inducible HSF and a constitutive HSE-binding factor. Our results also suggest that overexpression of human hsp70 may decrease the level of heat-induced HSF-HSE-binding activity in rat cells.
Liu
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RY
Department of Medical Physics, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.
Kim
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Yang
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Li
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GC
D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D002460:Cell Line; D004268:DNA-Binding Proteins / Q000378:metabolism; D005347:Fibroblasts / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides; D011401:Promoter Regions, Genetic; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D051381:Rats; D014158:Transcription, Genetic
D004268:DNA-Binding Proteins; D006360:Heat-Shock Proteins; D009838:Oligodeoxyribonucleotides; D012333:RNA, Messenger