Chimeras of channelrhodopsin-1 and-2 from chlamydomonas reinhardtii exhibit distinctive light-induced structural changes from channelrhodopsin-2

Asumi Inaguma, Hisao Tsukamoto, Hideaki E. Kato, Tetsunari Kimura, Toru Ishizuka, Satomi Oishi, Hiromu Yawo, Osamu Nureki, Yuji Furutani

    Research output: Contribution to journalArticle

    17 Citations (Scopus)

    Abstract

    Background: Channelrhodopsins, light-gated cation channels, are widely used for optogenetics. Results: Channelrhodopsin-1/2 chimeras exhibit light-induced conformational changes with reduced Glu-129 deprotonation (Glu-90 in channelrhodopsin-2). Conclusion: First and second channelrhodopsin-1 transmembrane helices are prerequisite for converting photostationary state of channelrhodopsin-2 into reduced desensitized state. Significance Channelrhodopsin-2 has some structural differences from a channelrhodopsin chimera whose X-ray crystal structure has been solved.

    Original languageEnglish
    Pages (from-to)11623-11634
    Number of pages12
    JournalJournal of Biological Chemistry
    Volume290
    Issue number18
    DOIs
    Publication statusPublished - 2015 May 1

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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    Inaguma, A., Tsukamoto, H., Kato, H. E., Kimura, T., Ishizuka, T., Oishi, S., Yawo, H., Nureki, O., & Furutani, Y. (2015). Chimeras of channelrhodopsin-1 and-2 from chlamydomonas reinhardtii exhibit distinctive light-induced structural changes from channelrhodopsin-2. Journal of Biological Chemistry, 290(18), 11623-11634. https://doi.org/10.1074/jbc.M115.642256