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Preference of Proteomonas sulcata anion channelrhodopsin for NO3- revealed using a pH electrode method
| Title: | Preference of Proteomonas sulcata anion channelrhodopsin for NO3- revealed using a pH electrode method |
| Authors: | Kikuchi, Chihiro Browse this author | | Kurane, Hina Browse this author | | Watanabe, Takuma Browse this author | | Demura, Makoto Browse this author | | Kikukawa, Takashi Browse this author | | Tsukamoto, Takashi Browse this author →KAKEN DB |
| Issue Date: | 12-Apr-2021 |
| Publisher: | Nature Research |
| Journal Title: | Scientific reports |
| Volume: | 11 |
| Issue: | 1 |
| Start Page: | 7908 |
| Publisher DOI: | 10.1038/s41598-021-86812-z |
| Abstract: | Ion channel proteins are physiologically important molecules in living organisms. Their molecular functions have been investigated using electrophysiological methods, which enable quantitative, precise and advanced measurements and thus require complex instruments and experienced operators. For simpler and easier measurements, we measured the anion transport activity of light-gated anion channelrhodopsins (ACRs) using a pH electrode method, which has already been established for ion pump rhodopsins. Using that method, we successfully measured the anion transport activity and its dependence on the wavelength of light, i.e. its action spectra, and on the anion species, i.e. its selectivity or preference, of several ACRs expressed in yeast cells. In addition, we identified the strong anion transport activity and the preference for NO3- of an ACR from a marine cryptophyte algae Proteomonas sulcata, named PsuACR_353. Such a preference was discovered for the first time in microbial pump- or channel-type rhodopsins. Nitrate is one of the most stable forms of nitrogen and is used as a nitrogen source by most organisms including plants. Therefore, PsuACR_353 may play a role in NO3- transport and might take part in NO3--related cellular functions in nature. Measurements of a mutant protein revealed that a Thr residue in the 3(rd) transmembrane helix, which corresponds to Cys102 in GtACR1, contributed to the preference for NO3-. These findings will be helpful to understand the mechanisms of anion transport, selectivity and preference of PsuACR_353. |
| Type: | article |
| URI: | http://hdl.handle.net/2115/81733 |
| 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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