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KMID : 0364820170530040297
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Korean Journal of Microbiology
2017 Volume.53 No. 4 p.297 ~ p.303
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Analysis of quaternary structure of leucine-responsive regulatory protein (Lrp) by crosslink experiments
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Lee Eui-Ho
Robert Pokoo
Loi Thuan Nguyen
Lee Chan-Yong
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Abstract
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Leucine-responsive regulatory protein (LRP) is a regulatory protein of molecular weight 18.8 kDa and is widely known to regulate many metabolic and functional activities of operons in Escherichia coli. The gene for Lrp from Escherichia coli in pQE system of 6 × His-tagging was expressed and 3 H-labeled protein, as well as the wild type Lrp, was purified. The crosslink experiments were performed to analyze the quaternary structure of Lrp at high of 5 μM and at low concentrations below 0.3 μM with cross linkers, such as glutaraldehyde, 1, 2, 3, 4-diepoxybutane (DEB), and ethylene glycol bis (succinimidyl succinate) (EGS). In the experiments, we found that the Lrp protein can be formed higher conformation states of tetramer, hexamer, octamer, as well as dimeric state when incubated with the above cross linkers.
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KEYWORD
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crosslink, global regulatory protein, leucine, Lrp
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