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Báo cáo khoa học: Differential recognition of heat shock elements by members of the heat shock transcription factor family

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 typesin vitro, in yeast cells, and in HeLa cells. | ễFEBS Journal Differential recognition of heat shock elements by members of the heat shock transcription factor family Noritaka Yamamoto1 Yukiko Takemori1 Mayumi Sakurai2 Kazuhisa Sugiyama2 and Hiroshi Sakurai1 1 Department of ClinicalLaboratory Science Kanazawa University Graduate Schoolof MedicalScience Japan 2 Department of Ophthalmology and VisualScience Kanazawa University Graduate Schoolof MedicalScience Japan Keywords crystallin heat shock element heat shock protein heat shock response heat shock transcription factor Correspondence H. Sakurai Department of Clinical Laboratory Science Kanazawa University Graduate Schoolof MedicalScience 5-11-80 Kodatsuno Kanazawa Ishikawa 920-0942 Japan Fax 81 76 234 4369 Tel 81 76 265 2588 E-mail sakurai@kenroku.kanazawa-u.ac.jp Received 5 November 2008 revised 14 January 2009 accepted 21 January 2009 doi 10.1111 j.1742-4658.2009.06923.x 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 c-crystallin genes encoding structural proteins of the lens heat-induced HSF1 preferred HSEs on the cA-crystallin and cB-crys-tallin promoters whereas HSF4 preferred HSE