Protonation Behavior of Histidine during HSF1 Activation by Physiological Acidification
文献类型：期刊论文
| 作者 | Lu, Ming1,2; Park, Jang-Su2 |
| 刊名 | JOURNAL OF CELLULAR BIOCHEMISTRY
 |
| 出版日期 | 2015-06-01 |
| 卷号 | 116期号:6页码:977-984 |
| 关键词 | HEAT SHOCK FACTOR 1 (HSF1) PROTONATION HISTIDINE ACIDIFICATION |
| 英文摘要 | The expression of eukaryoticmolecular chaperones (heat shock proteins, HSPs) is triggered in response to a wide range of environmental stresses, including: heat shock, hydrogen peroxide, heavy metal, low-pH, or virus infection. Biochemical and genetic studies have clearly shown the fundamental roles of heat shock factor 1 (HSF1) in stress-inducible HSP gene expression, resistance to stress-induced cell death, carcinogenesis, and other biological phenomena. Previous studies show that acidic pH changes within the physiological range directly activate the HSF1 function in vitro. However, the detailed mechanism is unclear. Though computational pKa-predications of the amino acid side-chain, acidic-pH induced protonation of a histidine residue was found to be most-likely involved in this process. The histidine 83 (His83) residue, which could be protonated by mild decrease in pH, causes mild acidic-induced HSF1 activation (including in-vitro trimerization, DNA binding, in-vivo nuclear accumulation, and HSPs expression). His83, which is located in the loop region of the HSF1 DNA binding domain, was suggested to enhance the intermolecular force with Arginine 79, which helps HSF1 form a DNA-binding competent. Therefore, low-pH-induced activation of HSF1 by the protonation of histidine can help us better to understand the HSF1 mechanism and develop more therapeutic applications (particularly in cancer therapy). (C) 2015 Wiley Periodicals, Inc. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology ; Cell Biology |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Cell Biology |
| 关键词[WOS] | SHOCK TRANSCRIPTION FACTOR ; DNA-BINDING DOMAIN ; HEAT-SHOCK ; INTRACELLULAR PH ; STRESS ; PROTEINS ; FACTOR-1 ; CANCER ; TRIMERIZATION ; METABOLISM |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000352816400010 |
| 公开日期 | 2015-12-24 |
| 源URL | [http://ir.qibebt.ac.cn/handle/337004/6733]  |
| 专题 | 青岛生物能源与过程研究所_微生物资源团队 |
| 作者单位 | 1.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Lab Biofuels, Qingdao 266061, Peoples R China 2.Pusan Natl Univ, Dept Chem, Pusan 609735, South Korea |
| 推荐引用方式 GB/T 7714 | Lu, Ming,Park, Jang-Su. Protonation Behavior of Histidine during HSF1 Activation by Physiological Acidification[J]. JOURNAL OF CELLULAR BIOCHEMISTRY,2015,116(6):977-984. |
| APA | Lu, Ming,&Park, Jang-Su.(2015).Protonation Behavior of Histidine during HSF1 Activation by Physiological Acidification.JOURNAL OF CELLULAR BIOCHEMISTRY,116(6),977-984. |
| MLA | Lu, Ming,et al."Protonation Behavior of Histidine during HSF1 Activation by Physiological Acidification".JOURNAL OF CELLULAR BIOCHEMISTRY 116.6(2015):977-984. |
入库方式： OAI收割
来源：青岛生物能源与过程研究所
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