Open AccessDual control of heat shock response: involvement of a constitutive heat shock element-binding factor.
Author(s) -
Richard Y. Liu,
Dooha Kim,
Shaohua Yang,
Gloria C. Li
Publication year - 1993
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.90.7.3078
Subject(s) - heat shock factor , hsp70 , heat shock protein , sodium arsenite , heat shock , shock (circulatory) , biology , hsf1 , microbiology and biotechnology , hspa14 , chemistry , biochemistry , gene , medicine , arsenic , organic chemistry
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.