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Expression of salinarum halorhodopsin in Escherichia coli cells : Solubilization in the presence of retinal yields the natural state
Title: | Expression of salinarum halorhodopsin in Escherichia coli cells : Solubilization in the presence of retinal yields the natural state |
Authors: | Yamashita, Yasutaka Browse this author | Kikukawa, Takashi Browse this author →KAKEN DB | Tsukamoto, Takashi Browse this author | Kamiya, Masakatsu Browse this author | Aizawa, Tomoyasu Browse this author | Kawano, Keiichi Browse this author | Miyauchi, Seiji Browse this author | Kamo, Naoki Browse this author | Demura, Makoto Browse this author |
Keywords: | Archaeal rhodopsin | Halorhodopsin | Light-driven chloride pump | Photocycle |
Issue Date: | Dec-2011 |
Publisher: | Elsevier B.V. |
Journal Title: | Biochimica et Biophysica Acta (BBA) : Biomembranes |
Volume: | 1808 |
Issue: | 12 |
Start Page: | 2905 |
End Page: | 2912 |
Publisher DOI: | 10.1016/j.bbamem.2011.08.035 |
PMID: | 21925140 |
Abstract: | Salinarum halorhodopsin (HsHR), a light-driven chloride ion pump of haloarchaeon Halobacterium salinarum, was heterologously expressed in Escherichia coil. The expressed HsHR had no color in the E. coli membrane, but turned purple after solubilization in the presence of all-trans retinal. This colored HsHR was purified by Ni-chelate chromatography in a yield of 3-4 mg per liter culture. The purified HsHR showed a distinct chloride pumping activity by incorporation into the liposomes, and showed even in the detergent-solubilized state, its typical behaviors in both the unphotolyzed and photolyzed states. Upon solubilization, HsHR expressed in the E. coli membrane attains the proper folding and a trimeric assembly comparable to those in the native membranes. |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/48254 |
Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 菊川 峰志
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