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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

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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)

Submitter: 加茂 直樹

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