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Glutamate residue 90 in the predicted transmembrane domain 2 is crucial for cation flux through channelrhodopsin 2

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Ruffert,  Karelia
Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society;

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Himmel,  Bettina
Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society;
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Lall,  Deepti
Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society;

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Bamann,  Christian
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Bamberg,  Ernst
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Betz,  Heinrich
Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society;

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Eulenburg,  Volker
Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society;

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Citation

Ruffert, K., Himmel, B., Lall, D., Bamann, C., Bamberg, E., Betz, H., et al. (2011). Glutamate residue 90 in the predicted transmembrane domain 2 is crucial for cation flux through channelrhodopsin 2. Biochemical and Biophysical Research Communications, 410(4), 737-743. doi:10.1016/j.bbrc.2011.06.024.


Cite as: https://hdl.handle.net/21.11116/0000-0009-2CD6-5
Abstract
Channelrhodopsin 2 (ChR2) is a microbial-type rhodopsin with a putative heptahelical structure that binds all-trans-retinal. Blue light illumination of ChR2 activates an intrinsic leak channel conductive for cations. Sequence comparison of ChR2 with the related ChR1 protein revealed a cluster of charged amino acids within the predicted transmembrane domain 2 (TM2), which includes glutamates E90, E97 and E101. Charge inversion substitutions of these residues significantly altered ChR2 function as revealed by two-electrode voltage-clamp recordings of light-induced currents from Xenopus laevis oocytes expressing the respective mutant proteins. Specifically, replacement of E90 by lysine or alanine resulted in differential effects on H+- and Na+-mediated currents. Our results are consistent with this glutamate side chain within the proposed TM2 contributing to ion flux through and the cation selectivity of ChR2.