The Role of DNA Binding Domain in hHSF1 through Redox State
作者：
DOI: 10.5352/JLS.2006.16.6.1052
关键词: Conformational change 、 Biochemistry 、 DNA-binding domain 、 DNA 、 Cysteine 、 Biophysics 、 Heat shock protein 、 Chemistry 、 HMG-box 、 Heat shock 、 Binding domain
摘要: The heat shock response is induced by environmental stress, pathophysiological state and non-stress conditions wide spread from bacteria to human. Although translations of most proteins are stopped under a response, (HSPs) produced protect cell stress. When induced, conformation HSF1 was changed monomer trimer specifically binds DNA, which called element(HSE) within the promoter genes. Human HSF1(hHSF1) contains five cysteine(Cys) residues. A thiol group(R-SH) Cys strong nucleophile, readily oxidized nitrosylated in amino acid chain. This consideration suggests that residues may regulate change activity hHSF1 through redox-dependent thiol/disulfide exchange reaction. We want construct role hHSF redox reagents. According two studies, related formation hHSF1. In this study, we demonstrate correlation between structural DNA-binding forming disulfide bond trimerization. results, could deduce DNA binding domain wasn't affected for always expose outside easily bind DNA. wild-type HSF's conformational change, as structure (trimerization) caused domain.
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