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

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.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0009-2CD6-5 Version Permalink: https://hdl.handle.net/21.11116/0000-0009-2CD7-4
Genre: Journal Article

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 Creators:
Ruffert, Karelia1, Author           
Himmel, Bettina1, 2, Author           
Lall, Deepti1, Author           
Bamann, Christian2, Author           
Bamberg, Ernst2, Author           
Betz, Heinrich1, Author           
Eulenburg, Volker1, Author           
Affiliations:
1Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society, ou_2461704              
2Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              

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Free keywords: Channelrhodopsin 2; Photocurrent; Cation channel; Amphipathic helix; Ion selectivity; Voltage-clamp recording
 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.

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Language(s): eng - English
 Dates: 2011-05-302011-06-122011-07-15
 Publication Status: Issued
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bbrc.2011.06.024
PMID: 21683688
 Degree: -

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Title: Biochemical and Biophysical Research Communications
  Other : Biochem. Biophys. Res. Commun.
Source Genre: Journal
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Publ. Info: Orlando, Fla. : Academic Press
Pages: - Volume / Issue: 410 (4) Sequence Number: - Start / End Page: 737 - 743 Identifier: ISSN: 0006-291X
CoNE: https://pure.mpg.de/cone/journals/resource/954922652205_1