Binding of Escherichia coli lexA repressor to the RecA operator

Binding of Escherichia coli lexA repressor to the RecA operator
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大肠杆菌 lexA 阻遏蛋白与 RecA 操纵子的结合

DOI:
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发表时间:
1996
影响因子:
2.7
通讯作者:
Elisabeth S. Gaissarian
Elisabeth S. Gaissarian
中科院分区:
生物学4区
文献类型:
--
作者:
S. Shaner;Elisabeth S. Gaissarian

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通过聚丙烯酰胺凝胶迁移率变动分析研究了大肠杆菌莱克萨阻遏物与recA操纵子的平衡结合,作为溶液条件的函数。在20°C NaCl存在下,与recA操纵子的结合存在显著的盐依赖性,这对于蛋白质-核酸相互作用是典型的,对结合自由能有一些静电贡献。在Na+盐的阴离子从氯离子变为氟离子的初步实验中,发现阴离子身份几乎没有变化。这表明盐对结合相互作用的影响仅来自于离子效应,而不是来自于阴离子结合或复合物形成时蛋白质的释放。将温度升高至37°C改变了在任何给定盐浓度下复合物形成的结合亲和力,并导致复合物形成对NaCl浓度的敏感性的变化。定量分析的数据,以获得平衡结合常数进行了讨论。
Equilibrium binding of Escherichia coli LexA repressor to the recA operator was studied by the polyacrylamide gel mobility shift assay as a function of solution conditions. In the presence of NaCl at 20°C, there was a significant salt dependence in binding to the recA operator, typical for protein–nucleic acid interactions with some electrostatic contribution to the binding free energy. In preliminary experiments in which the anion of the Na+ salt was changed from chloride to fluoride, little change was found with anion identity. This indicates that the salt effect on the binding interaction arises solely from the polyelectrolyte effect, not from anion binding or release by the protein upon complex formation. Increasing the temperature to 37°C changed the binding affinity for complex formation at any given salt concentration and resulted in a change in the sensitivity of complex formation to NaCl concentration. Quantitative analysis of the data to obtain equilibrium binding constants is discussed.
DOI: 10.1016/0300-9084(91)90112-e
发表时间: 1991-04
期刊: Biochimie
影响因子: 3.9
作者:
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影响因子: 16.6
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DOI: 10.1073/pnas.78.7.4199
发表时间: 1981-01-01
期刊: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子: --
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发表时间: 1992
影响因子: 11.1
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