Channelrhodopsins of Volvox carteri are photochromic proteins that are specifically expressed in somatic cells under control of light, temperature and the sex-inducer

Kianianmomeni A, Stehfest K, Nematollahi G, Hegemann P, Hallmann A (2009)
Plant Physiol. 151(1): 347-366.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
Abstract / Bemerkung
Channelrhodopsins are light-gated ion channels involved in the photoresponses of microalgae. Here, we describe the characterization of two channelrhodopsins, Volvox channelrhodopsin-1 (VChR1) and VChR2, from the multicellular green alga Volvox carteri. Both are encoded by nuclear single copy genes and are highly expressed in the small biflagellated somatic cells but not in the asexual reproductive cells (gonidia). Expression of both VChRs increases after cell cleavage and peaks after completion of embryogenesis, when the biosynthesis of the extracellular matrix begins. Likewise, expression of both transcripts increases after addition of the sex-inducer protein, but VChR2 is induced much more than VChR1. The expression of VChR1 is specifically promoted by extended dark periods, and heat stress reduces predominantly VChR1 expression. Expression of both VChRs increased under low light conditions, whereas cold stress and wounding reduced expression. Both VChRs were spectroscopically studied in their purified recombinant forms. VChR2 is similar to the ChR2 counterpart from Chlamydomonas reinhardtii with respect to its absorption maximum ( 460 nm) and photocycle dynamics. In contrast, VChR1 absorbs maximally at 540 nm at low pH (D540), shifting to 500 nm at high pH (D500). Flash photolysis experiments showed that after light excitation, the D540 dark state bleaches and at least two photoproducts, P600 and P500, are sequentially populated during the photocycle. We hypothesize that VChR2 is a general photoreceptor that is responsible for the avoidance of blue light and might play a key role in sexual development, whereas VChR1 is the main phototaxis photoreceptor under vegetative conditions, as it is more specifically adapted to environmental conditions and the developmental stages of Volvox.
Erscheinungsjahr
Zeitschriftentitel
Plant Physiol.
Band
151
Zeitschriftennummer
1
Seite
347-366
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eISSN
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Kianianmomeni A, Stehfest K, Nematollahi G, Hegemann P, Hallmann A. Channelrhodopsins of Volvox carteri are photochromic proteins that are specifically expressed in somatic cells under control of light, temperature and the sex-inducer. Plant Physiol. 2009;151(1):347-366.
Kianianmomeni, A., Stehfest, K., Nematollahi, G., Hegemann, P., & Hallmann, A. (2009). Channelrhodopsins of Volvox carteri are photochromic proteins that are specifically expressed in somatic cells under control of light, temperature and the sex-inducer. Plant Physiol., 151(1), 347-366. doi:10.1104/pp.109.143297
Kianianmomeni, A., Stehfest, K., Nematollahi, G., Hegemann, P., and Hallmann, A. (2009). Channelrhodopsins of Volvox carteri are photochromic proteins that are specifically expressed in somatic cells under control of light, temperature and the sex-inducer. Plant Physiol. 151, 347-366.
Kianianmomeni, A., et al., 2009. Channelrhodopsins of Volvox carteri are photochromic proteins that are specifically expressed in somatic cells under control of light, temperature and the sex-inducer. Plant Physiol., 151(1), p 347-366.
A. Kianianmomeni, et al., “Channelrhodopsins of Volvox carteri are photochromic proteins that are specifically expressed in somatic cells under control of light, temperature and the sex-inducer”, Plant Physiol., vol. 151, 2009, pp. 347-366.
Kianianmomeni, A., Stehfest, K., Nematollahi, G., Hegemann, P., Hallmann, A.: Channelrhodopsins of Volvox carteri are photochromic proteins that are specifically expressed in somatic cells under control of light, temperature and the sex-inducer. Plant Physiol. 151, 347-366 (2009).
Kianianmomeni, Arash, Stehfest, K., Nematollahi, Ghazaleh, Hegemann, P., and Hallmann, Armin. “Channelrhodopsins of Volvox carteri are photochromic proteins that are specifically expressed in somatic cells under control of light, temperature and the sex-inducer”. Plant Physiol. 151.1 (2009): 347-366.

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Bedbrook CN, Rice AJ, Yang KK, Ding X, Chen S, LeProust EM, Gradinaru V, Arnold FH., Proc Natl Acad Sci U S A 114(13), 2017
PMID: 28283661
The regulatory mechanism of ion permeation through a channelrhodopsin derived from Mesostigma viride (MvChR1).
Watanabe S, Ishizuka T, Hososhima S, Zamani A, Hoque MR, Yawo H., Photochem Photobiol Sci 15(3), 2016
PMID: 26853505
Biophysics of Channelrhodopsin.
Schneider F, Grimm C, Hegemann P., Annu Rev Biophys 44(), 2015
PMID: 26098512
Microbial rhodopsins of Halorubrum species isolated from Ejinoor salt lake in Inner Mongolia of China.
Chaoluomeng, Dai G, Kikukawa T, Ihara K, Iwasa T., Photochem Photobiol Sci 14(11), 2015
PMID: 26328780
Algal photoreceptors: in vivo functions and potential applications.
Kianianmomeni A, Hallmann A., Planta 239(1), 2014
PMID: 24081482
Photons and neurons.
Richter CP, Tan X., Hear Res 311(), 2014
PMID: 24709273
Involvement of glutamate 97 in ion influx through photo-activated channelrhodopsin-2.
Tanimoto S, Sugiyama Y, Takahashi T, Ishizuka T, Yawo H., Neurosci Res 75(1), 2013
PMID: 22664343
Intramolecular proton transfer in channelrhodopsins.
Sineshchekov OA, Govorunova EG, Wang J, Li H, Spudich JL., Biophys J 104(4), 2013
PMID: 23442959
Optogenetic manipulation of neural and non-neural functions.
Yawo H, Asano T, Sakai S, Ishizuka T., Dev Growth Differ 55(4), 2013
PMID: 23550617
Characterization of a highly efficient blue-shifted channelrhodopsin from the marine alga Platymonas subcordiformis.
Govorunova EG, Sineshchekov OA, Li H, Janz R, Spudich JL., J Biol Chem 288(41), 2013
PMID: 23995841
Diversity of Chlamydomonas channelrhodopsins.
Hou SY, Govorunova EG, Ntefidou M, Lane CE, Spudich EN, Sineshchekov OA, Spudich JL., Photochem Photobiol 88(1), 2012
PMID: 22044280
Color-tuned channelrhodopsins for multiwavelength optogenetics.
Prigge M, Schneider F, Tsunoda SP, Shilyansky C, Wietek J, Deisseroth K, Hegemann P., J Biol Chem 287(38), 2012
PMID: 22843694
New channelrhodopsin with a red-shifted spectrum and rapid kinetics from Mesostigma viride.
Govorunova EG, Spudich EN, Lane CE, Sineshchekov OA, Spudich JL., MBio 2(3), 2011
PMID: 21693637
The microbial opsin family of optogenetic tools.
Zhang F, Vierock J, Yizhar O, Fenno LE, Tsunoda S, Kianianmomeni A, Prigge M, Berndt A, Cushman J, Polle J, Magnuson J, Hegemann P, Deisseroth K., Cell 147(7), 2011
PMID: 22196724
Evolution of the channelrhodopsin photocycle model.
Stehfest K, Hegemann P., Chemphyschem 11(6), 2010
PMID: 20349494
Calcium channels in photosynthetic eukaryotes: implications for evolution of calcium-based signalling.
Verret F, Wheeler G, Taylor AR, Farnham G, Brownlee C., New Phytol 187(1), 2010
PMID: 20456068

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