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Influence of polyamines on DNA binding of heat shock and activator protein 1 transcription factors induced by heat shock
Author(s) -
Desiderio Maria Alfonsina,
Dansi Paola,
Tacchini Lorenza,
Bernelli-Zazzera Aldo
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00873-x
Subject(s) - spermidine , heat shock factor , polyamine , hsf1 , transcription (linguistics) , hsp70 , heat shock protein , activator (genetics) , heat shock , transcription factor , microbiology and biotechnology , dna , chemistry , biology , biochemistry , enzyme , gene , linguistics , philosophy
Polyamine depletion, obtained in FAO cells with specific inhibitors of biosynthetic enzymes, prevents or decreases the accumulation of hsp 70 mRNA following heat shock [Desiderio et al., Hepatology 24 (1996) 150–156]. The present study shows that under conditions of spermidine depletion caused by α‐difluoromethylornithine, the DNA binding capacity of the transcription factor HSF induced by heat shock undergoes a severe and prompt deactivation. Replenishment of the spermidine pool before heat shock re‐establishes the DNA binding activity of HSF and the inducibility of hsp 70 mRNA. Similar to HSF, but with a different time‐course, the DNA binding of the transcription factor AP‐1 activated by heat shock is also impaired in spermidine‐depleted cells and reversed by exogenous spermidine. STAT3 provides an example of a transcription factor slightly activated by heat shock but insensitive to polyamine decrease.