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Commun Biol ; 4(1): 235, 2021 02 23.
Artigo em Inglês | MEDLINE | ID: mdl-33623126

RESUMO

Channelrhodopsins (ChRs) are light-gated ion channels extensively applied as optogenetics tools for manipulating neuronal activity. All currently known ChRs comprise a large cytoplasmic domain, whose function is elusive. Here, we report the cation channel properties of KnChR, one of the photoreceptors from a filamentous terrestrial alga Klebsormidium nitens, and demonstrate that the cytoplasmic domain of KnChR modulates the ion channel properties. KnChR is constituted of a 7-transmembrane domain forming a channel pore, followed by a C-terminus moiety encoding a peptidoglycan binding domain (FimV). Notably, the channel closure rate was affected by the C-terminus moiety. Truncation of the moiety to various lengths prolonged the channel open lifetime by more than 10-fold. Two Arginine residues (R287 and R291) are crucial for altering the photocurrent kinetics. We propose that electrostatic interaction between the rhodopsin domain and the C-terminus domain accelerates the channel kinetics. Additionally, maximal sensitivity was exhibited at 430 and 460 nm, the former making KnChR one of the most blue-shifted ChRs characterized thus far, serving as a novel prototype for studying the molecular mechanism of color tuning of the ChRs. Furthermore, KnChR would expand the optogenetics tool kit, especially for dual light applications when short-wavelength excitation is required.


Assuntos
Channelrhodopsins/metabolismo , Clorófitas/metabolismo , Ativação do Canal Iônico , Sequência de Aminoácidos , Animais , Linhagem Celular , Channelrhodopsins/química , Channelrhodopsins/genética , Channelrhodopsins/efeitos da radiação , Clorófitas/genética , Clorófitas/efeitos da radiação , Ativação do Canal Iônico/efeitos da radiação , Cinética , Luz , Potenciais da Membrana , Camundongos , Optogenética , Domínios Proteicos , Ratos , Relação Estrutura-Atividade
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