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Differential recognition of heat shock elements by members of the heat shock transcription factor family
Author(s) -
Yamamoto Noritaka,
Takemori Yukiko,
Sakurai Mayumi,
Sugiyama Kazuhisa,
Sakurai Hiroshi
Publication year - 2009
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2009.06923.x
Subject(s) - heat shock factor , hsf1 , hspa12a , heat shock protein , microbiology and biotechnology , biology , transcription factor , heat shock , promoter , gene , hspa4 , regulator , transcription (linguistics) , genetics , gene expression , hsp70 , linguistics , philosophy
Heat shock transcription factor (HSF), an evolutionarily conserved stress response regulator, forms trimers and binds to heat shock element (HSE), comprising at least three continuous inverted repeats of the sequence 5′‐nGAAn‐3′. The single HSF of yeast is also able to bind discontinuously arranged nGAAn units. We investigated interactions between three human HSFs and various HSE types in vitro , in yeast cells, and in HeLa cells. Human HSF1, a stress‐activated regulator, preferentially bound to continuous HSEs rather than discontinuous HSEs, and heat shock of HeLa cells caused expression of reporter genes containing continuous HSEs. HSF2, whose function is implicated in neuronal specification and spermatogenesis, exhibited a slightly higher binding affinity to discontinuous HSEs than did HSF1. HSF4, a protein required for ocular lens development, efficiently recognized discontinuous HSEs in a trimerization‐dependent manner. Among four human γ‐ crystallin genes encoding structural proteins of the lens, heat‐induced HSF1 preferred HSEs on the γA‐ crystallin and γB‐ crystallin promoters, whereas HSF4 preferred HSE on the γC‐ crystallin promoter. These results suggest that the HSE architecture is an important determinant of which HSF members regulate genes in diverse cellular processes.