期刊
NATURE COMMUNICATIONS
卷 11, 期 1, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/s41467-020-19457-7
关键词
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资金
- HGF-RSF grant (Helmholtz-RSF Joint Research Groups grant (RSF) [19-4406302]
- Agence Nationale de la Recherche (ANR), France
- Deutsche Forschungsgemeinschaft (DFG), Germany [ANR-15-CE11-0029-02/FA 301/11-1]
- DFG Research Unit [FOR 2518, MA 7525/1-1]
- Frankfurt: Cluster of Excellence Frankfurt Macromolecular Complexes by the Max Planck Society
- Commissariat a l'Energie Atomique et aux Energies Alternatives (Institut de Biologie Structurale)-Helmholtz-Gemeinschaft Deutscher Forschungszentren (Forschungszentrum Julich)
- FRISBI [ANR-10-INBS-0502]
- GRAL, a project of the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS [ANR-17-EURE-0003]
- RFBR
- CNRS [19-5215017]
- Russian Foundation for Basic Research [17-00-00164, 20-34-90009, 17-00-00166, 17-00-00167]
- Ministry of Science and Higher Education of the Russian Federation [075-00337-20-03, FSMG -2020-0003]
- European Research Council through the Advanced Grant `OptoHearto T. M. under the European Union's Horizon 2020 Research and Innovation program [670759]
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy [EXC 2067/1-390729940]
- [ANR-19-CE11-0026]
Phytoplankton is the base of the marine food chain as well as oxygen and carbon cycles and thus plays a global role in climate and ecology. Nucleocytoplasmic Large DNA Viruses that infect phytoplankton organisms and regulate the phytoplankton dynamics encompass genes of rhodopsins of two distinct families. Here, we present a functional and structural characterization of two proteins of viral rhodopsin group 1, OLPVR1 and VirChR1. Functional analysis of VirChR1 shows that it is a highly selective, Na+/K+-conducting channel and, in contrast to known cation channelrhodopsins, it is impermeable to Ca2+ ions. We show that, upon illumination, VirChR1 is able to drive neural firing. The 1.4 angstrom resolution structure of OLPVR1 reveals remarkable differences from the known channelrhodopsins and a unique ion-conducting pathway. Thus, viral rhodopsins 1 represent a unique, large group of light-gated channels (viral channelrhodopsins, VirChR1s). In nature, VirChR1s likely mediate phototaxis of algae enhancing the host anabolic processes to support virus reproduction, and therefore, might play a major role in global phytoplankton dynamics. Moreover, VirChR1s have unique potential for optogenetics as they lack possibly noxious Ca2+ permeability. Nucleocytoplasmic Large DNA Viruses (NCLDV) that infect algae encode two distinct families of microbial rhodopsins. Here, the authors characterise two proteins form the viral rhodopsin group 1 OLPVR1 and VirChR1, present the 1.4 angstrom crystal structure of OLPVR1 and show that viral rhodopsins 1 are light-gated cation channels.
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