Molecular and evolutionary aspects of microbial sensory rhodopsins |
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Authors: | Keiichi Inoue Takashi Tsukamoto Yuki Sudo |
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Affiliation: | 1. Department of Frontier Materials, Nagoya Institute of Technology, Showa-ku, Nagoya 466–8555, Japan;2. Japan Science and Technology Agency (JST), PRESTO, 4-1-8 Honcho Kawaguchi, Saitama 332–0012, Japan;3. Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya, 464–8602, Japan;4. Department of Life and Coordination-Complex Molecular Science, Institute for Molecular Science, 38 Nishigo-Naka, Myodaiji, Okazaki, Japan |
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Abstract: | Retinal proteins (~ rhodopsins) are photochemically reactive membrane-embedded proteins, with seven transmembrane α-helices which bind the chromophore retinal (vitamin A aldehyde). They are widely distributed through all three biological kingdoms, eukarya, bacteria and archaea, indicating the biological significance of the retinal proteins. Light absorption by the retinal proteins triggers a photoisomerization of the chromophore, leading to the biological function, light-energy conversion or light-signal transduction. This article reviews molecular and evolutionary aspects of the light-signal transduction by microbial sensory receptors and their related proteins. This article is part of a Special Issue entitled: Retinal Proteins - You can teach an old dog new tricks. |
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Keywords: | BR, bacteriorhodopsin HR, halorhdopsin SRI, sensory rhodopsin I SRII, sensory rhodopsin II MR, middle rhodopsin ASR, anabaena sensory rhodopsin AR3, archaearhodopsin-3 |
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