德洛索菲拉热冲击因子的合作结合,与保存的5bp单位数组结合
1Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853.
Cell
|February 8, 1991
概括
草虫热冲击因子 (HSF) 形成了多重分子,可以协同结合DNA. 这种合作性增强了HSF与多个部位的结合,这对于热冲击基因调节至关重要.
科学领域:
- 分子生物学分子生物学
- 遗传学 是一个遗传学.
- 生物化学 生物化学
背景情况:
- 果虫热冲击因子 (HSF) 存在于溶液中的多重体和与其调节元件 (热冲击元件 - HSE) 结合时.
- 之前的研究表明,HSF子单元结合成同位素,每个子单元与HSE中的保存5bpDNA序列接触.
研究的目的:
- 研究HSF在两个不同的层面上的合作结合:在多元体内的子单元之间,以及在多个HSF多元体之间.
- 了解HSF合作性在37°C的结合中的作用及其对体内结合要求及其差异性热冲击基因表达的影响.
主要方法:
- 热冲击因子 (HSF) 多元化和DNA结合的实验分析.
- 评估邻近的HSF结合地点的合作结合亲缘关系.
主要成果:
- 在两个层面上,HSF结合表现出高度的合作性:在HSF多元体内和多元体之间.
- 将HSF结合到两个相邻的三结合点中的一个,将HSF与第二个结合点的结合增强了2000倍以上.
- 这种合作性在37°C时尤为显著.
结论:
- 在HSF结合中观察到的高度合作性对其功能至关重要.
- 这种合作性可能解释了在体内多个HSE的必要性.
- 它还有助于热冲击基因在应对热应激时的差异表达.
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Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
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