Abstract
Stress response is nearly universal. Living organisms respond to the changes in their chemical, physical, and biological environments by synthesizing a group of proteins called stress or heat-shock proteins (1). The preferential synthesis of these proteins appears to be involved in induced transient thermal resistance (2). It is well known that transcription of heat-shock genes is regulated by heat-shock transcription factors (HSFs), which bind to heat-shock elements (HSEs) located in the promoter region of genes encoding heat-shock proteins (3). Heat-shock protein gene promoter contains three heat-shock elements (HSE, 5′-GAAnnTTCnnGAA-3′) (4). The HSE is known as a conserved motif present in the promoters of many heat-inducible heat-shock protein genes. Many studies have demonstrated that stress-induced denatured, unfolded, or malfolded proteins trigger the activation of heat shock transcription factors (HSFs) (5–7). In mammalian cells, the activated HSF binds to the HSE and then stimulates transcription.
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© 2002 Humana Press Inc.
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Lee, Y.J. (2002). Analysis of Heat-Shock Transcription Factor and Element-Binding Activity. In: Armstrong, D. (eds) Oxidants and Antioxidants. Methods in Molecular Biology™, vol 196. Humana Press. https://doi.org/10.1385/1-59259-274-0:131
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DOI: https://doi.org/10.1385/1-59259-274-0:131
Publisher Name: Humana Press
Print ISBN: 978-0-89603-851-6
Online ISBN: 978-1-59259-274-6
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