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A light-driven proton pump from Haloterrigena turkmenica: Functional expression in Escherichia coli membrane and coupling with a H+ co-transporter
Title: | A light-driven proton pump from Haloterrigena turkmenica: Functional expression in Escherichia coli membrane and coupling with a H+ co-transporter |
Authors: | Kamo, Naoki1 Browse this author →KAKEN DB | Hashiba, Tsuyoshi Browse this author | Kikukawa, Takashi Browse this author →KAKEN DB | Araiso, Tsunehisa Browse this author →KAKEN DB | Ihara, Kunio Browse this author →KAKEN DB | Nara, Toshifumi Browse this author →KAKEN DB |
Authors(alt): | 加茂, 直樹1 |
Keywords: | Archaeal rhodopsin | Bacteriorhodopsin | Light-driven proton pump | EmrE | Photocycle | SMR | Deltarhodopsin | Archaerhodopsin | Multi-drug resistance transporter |
Issue Date: | 10-Mar-2006 |
Publisher: | Elsevier |
Journal Title: | Biochemical and Biophysical Research Communications |
Volume: | 341 |
Issue: | 2 |
Start Page: | 285 |
End Page: | 290 |
Publisher DOI: | 10.1016/j.bbrc.2005.12.181 |
PMID: | 16413498 |
Abstract: | A gene encoding putative retinal protein was cloned from Haloterrigena turkmenica (JCM9743). The deduced amino acid sequence was most closely related to that of deltarhodopsin, which functions as a light-driven H+ pump and was identified in a novel strain Haloterrigena sp. arg-4 (K. Ihara, T. Uemura, I. Katagiri, T. Kitajima-Ihara, Y. Sugiyama, Y. Kimura, Y. Mukohata, Evolution of the archaeal rhodopsins: Evolution rate changes by gene duplication and functional differentiation, J. Mol. Biol. 285 (1999) 163–174. GenBank Accession No. AB009620). Thus, we called the present protein H. turkmenica deltarhodopsin (HtdR) in this report. Differing from the Halobacterium salinarum bacteriorhodopsin (bR), functional expression of HtdR was achieved in Escherichia coli membrane with a high yield of 10–15 mg protein/L culture. The photocycle of purified HtdR was similar to that of bR. The photo-induced electrogenic proton pumping activity of HtdR was verified. We co-expressed both HtdR and EmrE, a proton-coupled multi-drug efflux transporter in E. coli, and the cells successfully extruded ethidium, a substrate of EmrE, on illumination. |
Relation: | http://www.sciencedirect.com/science/journal/0006291X |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/5787 |
Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 加茂 直樹
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