Binding of Escherichia coli lexA repressor to the RecA operator
Binding of Escherichia coli lexA repressor to the RecA operator
复制标题
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
中科院分区:
文献类型:
--
作者:
S. Shaner;Elisabeth S. Gaissarian
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.
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影响因子:
3.9
作者:
A. Thliveris;J. W. Little;D. Mount
通讯作者:
A. Thliveris;J. W. Little;D. Mount
影响因子:
16.6
作者:
G. C. Walker
通讯作者:
G. C. Walker
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:
--
作者:
LITTLE, JW;MOUNT, DW;YANISCHPERRON, CR
通讯作者:
YANISCHPERRON, CR
DOI:
10.1101/sqb.1983.047.01.055
发表时间:
1983
期刊:
Cold Spring Harbor symposia on quantitative biology
影响因子:
--
作者:
Shaner,SL;Melançon,P;Lee,KS;Burgess,RR;RecordJr,MT
通讯作者:
RecordJr,MT
DOI:
10.1073/pnas.89.10.4500
发表时间:
1992
影响因子:
11.1
作者:
Thliveris,AT;Mount,DW
通讯作者:
Mount,DW