Preference of Proteomonas sulcata anion channelrhodopsin for NO3 − revealed using a pH electrode method

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....

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Autores principales:	Chihiro Kikuchi, Hina Kurane, Takuma Watanabe, Makoto Demura, Takashi Kikukawa, Takashi Tsukamoto
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/eeb50420ac43488a90e0b2fe181cfcde
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spelling	oai:doaj.org-article:eeb50420ac43488a90e0b2fe181cfcde2021-12-02T18:03:27ZPreference of Proteomonas sulcata anion channelrhodopsin for NO3 − revealed using a pH electrode method10.1038/s41598-021-86812-z2045-2322https://doaj.org/article/eeb50420ac43488a90e0b2fe181cfcde2021-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-86812-zhttps://doaj.org/toc/2045-2322Abstract 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 3rd 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.Chihiro KikuchiHina KuraneTakuma WatanabeMakoto DemuraTakashi KikukawaTakashi TsukamotoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Chihiro Kikuchi Hina Kurane Takuma Watanabe Makoto Demura Takashi Kikukawa Takashi Tsukamoto Preference of Proteomonas sulcata anion channelrhodopsin for NO3 − revealed using a pH electrode method
description	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 3rd 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.
format	article
author	Chihiro Kikuchi Hina Kurane Takuma Watanabe Makoto Demura Takashi Kikukawa Takashi Tsukamoto
author_facet	Chihiro Kikuchi Hina Kurane Takuma Watanabe Makoto Demura Takashi Kikukawa Takashi Tsukamoto
author_sort	Chihiro Kikuchi
title	Preference of Proteomonas sulcata anion channelrhodopsin for NO3 − revealed using a pH electrode method
title_short	Preference of Proteomonas sulcata anion channelrhodopsin for NO3 − revealed using a pH electrode method
title_full	Preference of Proteomonas sulcata anion channelrhodopsin for NO3 − revealed using a pH electrode method
title_fullStr	Preference of Proteomonas sulcata anion channelrhodopsin for NO3 − revealed using a pH electrode method
title_full_unstemmed	Preference of Proteomonas sulcata anion channelrhodopsin for NO3 − revealed using a pH electrode method
title_sort	preference of proteomonas sulcata anion channelrhodopsin for no3 − revealed using a ph electrode method
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/eeb50420ac43488a90e0b2fe181cfcde
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Preference of Proteomonas sulcata anion channelrhodopsin for NO3 − revealed using a pH electrode method

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