Open AccessSuppression of heat-induced hsp70 expression by the 70-kDa subunit of the human Ku autoantigen.
Author(s) -
Gloria C. Li,
Shaohua Yang,
Dooha Kim,
André Nussenzweig,
Hong Ouyang,
Jiaqin Wei,
Paul Burgman,
Ligeng Li
Publication year - 1995
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.92.10.4512
Subject(s) - hsf1 , hsp70 , heat shock factor , heat shock protein , activator (genetics) , hspa4 , protein subunit , biology , heat shock , transcription factor , microbiology and biotechnology , phosphorylation , gene expression , hspa14 , gene , biochemistry
Expression of the 70-kDa polypeptide of human Ku autoantigen in rat cells is shown to suppress specifically the induction of hsp70 upon heat shock. Thermal induction of other heat shock proteins is not significantly affected, nor is the state of phosphorylation or the DNA-binding ability of the heat shock transcription factor HSF1. These findings support a model in which hsp70 gene expression is controlled by a second regulatory factor in addition to the positive activator HSF1. The Ku autoantigen, or a protein closely related to it, is likely to be involved in the regulation of hsp70 expression.