| Title | Analysis of quaternary structure of leucine-responsive regulatory protein (Lrp) by crosslink experiments | ||
| Author | Euiho Lee, Robert Pokoo, Loi Thuan Nguyen, and Chan Yong Lee* | ||
| Address | Department of Biochemistry, Chungnam National University, Daejeon 34134, Republic of Korea | ||
| Bibliography | Korean Journal of Microbiology, 53(4),297-303, 2017 | ||
| DOI | https://doi.org/10.7845/kjm.2017.7063 | ||
| Key Words | crosslink, global regulatory protein, leucine, Lrp | ||
| Abstract | 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. | ||
| Download PDF | 09_[297-303]17-063.pdf | ||