Fig. 3: Electrophysiological measurements of variants in the C-terminal region. | Communications Biology

Fig. 3: Electrophysiological measurements of variants in the C-terminal region.

From: Specific residues in the cytoplasmic domain modulate photocurrent kinetics of channelrhodopsin from Klebsormidium nitens

Fig. 3

a Schematic drawing of KnChR with amino acid sequence between 284 and 294. b–e Photocurrent traces of KnChR-397 (no mutation), mutant variants- R287A, -R291A, and -R287A/R291A respectively. Blue bars indicate light application (480 nm, 12.3 mW/mm2). Membrane voltage was clamped from at −90 to +50 mV by 20 mV steps. Standard solutions were used (See “Methods”). f, g Comparison of time constants and peak current amplitude. The membrane voltage was clamped at −70 mV. N = 9 (WT-397), 6 (E285A), 7 (R287A), 6 (K289A), 6 (R291A), 6 (E293A), 6 (R287A/R291A), and 7 (WT-272). h I-V relationship of KnChR-397 (red)(N = 9), -R287A (blue)(N = 7), -R291A (green)(N = 6), and –R287A/R291A (yellow)(N = 6). Data were presented as the mean ± SEM. i Schematic drawing of interaction between the 7-TM domain and the cytoplasmic region in KnChR.

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