Viral rhodopsins 1 are unique family of light-gated cation channels

Zabelskii, D.; Alekseev, A.; Kovalev, K.; Rankovic, V.; Balandin, T.; Soloviov, D.; Bratanov, D.; Savelyeva, E.; Podolyak, E.; Volkov, D.; Vaganova, S.; Astashkin, R.; Chizhov, I.; Yutin, N.; Rulev, M.; Popov, A.; Eria-Oliveira, A.; Rokitskaya, T.; Mager, T.; Antonenko, Y.; Rosselli, R.; Armeev, G.; Shaitan, K.; Vivaudou, M.; Büldt, G.; Rogachev, A.; Valera, F.R.; Kirpichnikov, M.; Moser, T.; Offenhäusser, A.; Willbold, D.; Koonin, E.; Bamberg, E.; Gordeliy, V.

Авторы: Zabelskii Dmitrii, Alekseev Alexey, Kovalev Kirill, Rankovic Vladan, Balandin Taras, Soloviov Dmytro, Bratanov Dmitry, Savelyeva Ekaterina, Podolyak Elizaveta, Volkov Dmytro, Vaganova Svetlana, Astashkin Roman, Chizhov Igor, Yutin Natalia, Rulev Maksim, Popov Alexander, Eria-Oliveira Ana-Sofia, Rokitskaya Tatiana, Mager Thomas, Antonenko Yuri, Rosselli Riccardo, Armeev Grigoriy, Shaitan Konstantin, Vivaudou Michel, Büldt Georg, Rogachev Andrey, Valera Francisco Rodriguez, Kirpichnikov Mikhail, Moser Tobias, Offenhäusser Andreas, Willbold Dieter, Koonin Eugene, Bamberg Ernst, Gordeliy Valentin
Журнал: Nature communications
Номер: 11
Год издания: 2020
Издательство: Nature Pub. Group
Местоположение издательства: United Kingdom
Первая страница: 1
Последняя страница: 16
Номер статьи: 5707
DOI: 10.1038/s41467-020-19457-7
Аннотация: Phytoplankton is the base of the marine food chain as well as oxygen and carbon cycles and thusplays a global role in climate and ecology. Nucleocytoplasmic Large DNA Viruses that infectphytoplankton organisms and regulate the phytoplankton dynamics encompass genes ofrhodopsins of two distinct families.Here, we present a functional and structural characterization of two proteins of viral rhodopsingroup 1, OLPVR1 and VirChR1. Functional analysis of VirChR1 shows that it is a highlyselective, 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 neuralfiring. The 1.4 Å resolution structure of OLPVR1 reveals remarkable differences from theknown channelrhodopsins and a unique ion-conducting pathway. Thus, viral rhodopsins 1represent a unique, large group of light-gated channels (viral channelrhodopsins, VirChR1s).In nature, VirChR1s likely mediate phototaxis of algae enhancing the host anabolic processes tosupport virus reproduction, and therefore, might play a major role in global phytoplanktondynamics. Moreover, VirChR1s have unique potential for optogenetics as they lack possiblynoxious Ca2+ permeability.
Добавил в систему: Шайтан Константин Вольдемарович

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Viral rhodopsins 1 are unique family of light-gated cation channelsстатья Исследовательская статья

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