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Volumn 427, Issue 2, 2015, Pages 341-349

Light-induced helix movements in channelrhodopsin-2

Author keywords

Channelrhodopsin; Conformational changes; Electron cryo microscopy; Light gated ion channel; Microbial rhodopsin

Indexed keywords

BACTERIORHODOPSIN; CATION CHANNEL; CHANNELRHODOPSIN 2; DIMER; LIGAND GATED ION CHANNEL; MUTANT PROTEIN; UNCLASSIFIED DRUG; CALCIUM CHANNEL; RHODOPSIN; VEGETABLE PROTEIN;

EID: 84920812197     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.11.004     Document Type: Article
Times cited : (40)

References (50)
  • 2
    • 84897114580 scopus 로고    scopus 로고
    • Of ion pumps, sensors and channels - Perspectives on microbial rhodopsins between science and history
    • Grote M, Engelhard M, Hegemann P. Of ion pumps, sensors and channels - perspectives on microbial rhodopsins between science and history. Biochim Biophys Acta 2014;1837:533-45.
    • (2014) Biochim Biophys Acta , vol.1837 , pp. 533-545
    • Grote, M.1    Engelhard, M.2    Hegemann, P.3
  • 4
    • 84897113407 scopus 로고    scopus 로고
    • Channelrhodopsin unchained: Structure and mechanism of a light-gated cation channel
    • Lórenz-Fonfría VA, Heberle J. Channelrhodopsin unchained: structure and mechanism of a light-gated cation channel. Biochim Biophys Acta 2014;1837:626-42.
    • (2014) Biochim Biophys Acta , vol.1837 , pp. 626-642
    • Lórenz-Fonfría, V.A.1    Heberle, J.2
  • 5
    • 79959873914 scopus 로고    scopus 로고
    • The development and application of optogenetics
    • Fenno L, Yizhar O, Deisseroth K. The development and application of optogenetics. Annu Rev Neurosci 2011;34:389-412.
    • (2011) Annu Rev Neurosci , vol.34 , pp. 389-412
    • Fenno, L.1    Yizhar, O.2    Deisseroth, K.3
  • 6
    • 80054030842 scopus 로고    scopus 로고
    • Optogenetic control of cells and circuits
    • Miesenböck G. Optogenetic control of cells and circuits. Annu Rev Cell Dev Biol 2011;27:731-58.
    • (2011) Annu Rev Cell Dev Biol , vol.27 , pp. 731-758
    • Miesenböck, G.1
  • 7
    • 0027439826 scopus 로고
    • Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin
    • Subramaniam S, Gerstein M, Oesterhelt D, Henderson R. Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO J 1993;12:1-8.
    • (1993) EMBO J , vol.12 , pp. 1-8
    • Subramaniam, S.1    Gerstein, M.2    Oesterhelt, D.3    Henderson, R.4
  • 8
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin N. Acetylcholine receptor channel imaged in the open state. Nature 1995;373:37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 9
    • 84939194225 scopus 로고    scopus 로고
    • pH- and sodium-induced changes in a sodium/proton antiporter
    • Paulino C, Kühlbrandt W. pH- and sodium-induced changes in a sodium/proton antiporter. eLife 2013;3:e01412-2.
    • (2013) eLife , vol.3 , pp. e01412-e01412
    • Paulino, C.1    Kühlbrandt, W.2
  • 11
    • 75349085542 scopus 로고    scopus 로고
    • Structural guidance of the photocycle of channelrhodopsin-2 by an interhelical hydrogen bond
    • Bamann C, Gueta R, Kleinlogel S, Nagel G, Bamberg E. Structural guidance of the photocycle of channelrhodopsin-2 by an interhelical hydrogen bond. Biochemistry 2010;49:267-78.
    • (2010) Biochemistry , vol.49 , pp. 267-278
    • Bamann, C.1    Gueta, R.2    Kleinlogel, S.3    Nagel, G.4    Bamberg, E.5
  • 12
    • 81055155876 scopus 로고    scopus 로고
    • Projection structure of channelrhodopsin-2 at 6 A˚ resolution by electron crystallography
    • Müller M, Bamann C, Bamberg E, Kühlbrandt W. Projection structure of channelrhodopsin-2 at 6 A˚ resolution by electron crystallography. J Mol Biol 2011;414:86-95.
    • (2011) J Mol Biol , vol.414 , pp. 86-95
    • Müller, M.1    Bamann, C.2    Bamberg, E.3    Kühlbrandt, W.4
  • 14
    • 84857478497 scopus 로고    scopus 로고
    • In channelrhodopsin-2 Glu-90 is crucial for ion selectivity and is deprotonated during the photocycle
    • Eisenhauer K, Kuhne J, Ritter E, Berndt A, Wolf S, Freier E, et al. In channelrhodopsin-2 Glu-90 is crucial for ion selectivity and is deprotonated during the photocycle. J Biol Chem 2012;287:6904-11.
    • (2012) J Biol Chem , vol.287 , pp. 6904-6911
    • Eisenhauer, K.1    Kuhne, J.2    Ritter, E.3    Berndt, A.4    Wolf, S.5    Freier, E.6
  • 17
    • 84877578341 scopus 로고    scopus 로고
    • Towards an understanding of channelrhodopsin function: Simulations lead to novel insights of the channel mechanism
    • Watanabe HC, Welke K, Sindhikara DJ, Hegemann P, Elstner M. Towards an understanding of channelrhodopsin function: simulations lead to novel insights of the channel mechanism. J Mol Biol 2013;425:1795-814.
    • (2013) J Mol Biol , vol.425 , pp. 1795-1814
    • Watanabe, H.C.1    Welke, K.2    Sindhikara, D.J.3    Hegemann, P.4    Elstner, M.5
  • 18
    • 61649104837 scopus 로고    scopus 로고
    • Photocurrent attenuation by a single polar-to-nonpolar point mutation of channelrhodopsin-2
    • Sugiyama Y, Wang H, Hikima T, Sato M, Kuroda J, Takahashi T, et al. Photocurrent attenuation by a single polar-to-nonpolar point mutation of channelrhodopsin-2. Photochem Photobiol Sci 2009;8:328-36.
    • (2009) Photochem Photobiol Sci , vol.8 , pp. 328-336
    • Sugiyama, Y.1    Wang, H.2    Hikima, T.3    Sato, M.4    Kuroda, J.5    Takahashi, T.6
  • 19
    • 80052461748 scopus 로고    scopus 로고
    • Rectification of the channelrhodopsin early conductance
    • Gradmann D, Berndt A, Schneider F, Hegemann P. Rectification of the channelrhodopsin early conductance. Biophys J 2011;101:1057-68.
    • (2011) Biophys J , vol.101 , pp. 1057-1068
    • Gradmann, D.1    Berndt, A.2    Schneider, F.3    Hegemann, P.4
  • 20
    • 79960338849 scopus 로고    scopus 로고
    • 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. Glutamate residue 90 in the predicted transmembrane domain 2 is crucial for cation flux through channelrhodopsin 2. Biochem Biophys Res Commun 2011;410:737-43.
    • (2011) Biochem Biophys Res Commun , vol.410 , pp. 737-743
    • Ruffert, K.1    Himmel, B.2    Lall, D.3    Bamann, C.4    Bamberg, E.5    Betz, H.6
  • 21
    • 84899528517 scopus 로고    scopus 로고
    • Structureguided transformation of channelrhodopsin into a light-activated chloride channel
    • Berndt A, Lee SY, Ramakrishnan C, Deisseroth K. Structureguided transformation of channelrhodopsin into a light-activated chloride channel. Science 2014;344:420-4.
    • (2014) Science , vol.344 , pp. 420-424
    • Berndt, A.1    Lee, S.Y.2    Ramakrishnan, C.3    Deisseroth, K.4
  • 23
    • 58049216319 scopus 로고    scopus 로고
    • Monitoring light-induced structural changes of channelrho-dopsin-2 by UV-visible and Fourier transform infrared spectroscopy
    • Ritter E, Stehfest K, Berndt A, Hegemann P, Bartl FJ. Monitoring light-induced structural changes of channelrho-dopsin-2 by UV-visible and Fourier transform infrared spectroscopy. J Biochem 2008;283:35033-41.
    • (2008) J Biochem , vol.283 , pp. 35033-35041
    • Ritter, E.1    Stehfest, K.2    Berndt, A.3    Hegemann, P.4    Bartl, F.J.5
  • 26
    • 84884906995 scopus 로고    scopus 로고
    • Structural differences between the closed and open states of channelrhodopsin-2 as observed by EPR spectroscopy
    • Krause N, Engelhard C, Heberle J, Schlesinger R, Bittl R. Structural differences between the closed and open states of channelrhodopsin-2 as observed by EPR spectroscopy. FEBS Lett 2013;587:3309-13.
    • (2013) FEBS Lett , vol.587 , pp. 3309-3313
    • Krause, N.1    Engelhard, C.2    Heberle, J.3    Schlesinger, R.4    Bittl, R.5
  • 27
    • 0035016932 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin
    • Radzwill N, Gerwert K, Steinhoff HJ. Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin. Biophys J 2001;80:2856-66.
    • (2001) Biophys J , vol.80 , pp. 2856-2866
    • Radzwill, N.1    Gerwert, K.2    Steinhoff, H.J.3
  • 28
    • 0035943457 scopus 로고    scopus 로고
    • Crystal structure of sensory rhodopsin II at 2.4 angstroms: Insights into color tuning and transducer interaction
    • Luecke H. Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction. Science (New York NY) 2001;293:1499-503.
    • (2001) Science (New York NY) , vol.293 , pp. 1499-1503
    • Luecke, H.1
  • 29
    • 0035477798 scopus 로고    scopus 로고
    • Structural insights into the early steps of receptor-transducer signal transfer in archaeal phototaxis
    • Wegener AA, Klare JP, Engelhard M, Steinhoff HJ. Structural insights into the early steps of receptor-transducer signal transfer in archaeal phototaxis. EMBO J 2001;20:5312-9.
    • (2001) EMBO J , vol.20 , pp. 5312-5319
    • Wegener, A.A.1    Klare, J.P.2    Engelhard, M.3    Steinhoff, H.J.4
  • 30
    • 0034714097 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helix F in spinlabelled Pharaonis sensory rhodopsin II
    • Wegener AA, Chizhov I, Engelhard M, Steinhoff HJ. Time-resolved detection of transient movement of helix F in spinlabelled Pharaonis sensory rhodopsin II. J Mol Biol 2000;301:881-91.
    • (2000) J Mol Biol , vol.301 , pp. 881-891
    • Wegener, A.A.1    Chizhov, I.2    Engelhard, M.3    Steinhoff, H.J.4
  • 31
    • 80052964367 scopus 로고    scopus 로고
    • Active state of sensory rhodopsin II: Structural determinants for signal transfer and proton pumping
    • Gushchin I, Reshetnyak A, Borshchevskiy V, Ishchenko A, Round E, Grudinin S, et al. Active state of sensory rhodopsin II: structural determinants for signal transfer and proton pumping. J Mol Biol 2011;412:591-600.
    • (2011) J Mol Biol , vol.412 , pp. 591-600
    • Gushchin, I.1    Reshetnyak, A.2    Borshchevskiy, V.3    Ishchenko, A.4    Round, E.5    Grudinin, S.6
  • 32
    • 84872823342 scopus 로고    scopus 로고
    • Large deformation of helix F during the photoreaction cycle of Pharaonis halorhodopsin in complex with azide
    • Nakanishi T, Kanada S, Murakami M, Ihara K, Kouyama T. Large deformation of helix F during the photoreaction cycle of Pharaonis halorhodopsin in complex with azide. Biophys J 2013;104:377-85.
    • (2013) Biophys J , vol.104 , pp. 377-385
    • Nakanishi, T.1    Kanada, S.2    Murakami, M.3    Ihara, K.4    Kouyama, T.5
  • 33
    • 33644771099 scopus 로고    scopus 로고
    • Development of the signal in sensory rhodopsin and its transfer to the cognate transducer
    • Moukhametzianov R, Klare JP, Efremov R, Baeken C, Göppner A, Labahn J, et al. Development of the signal in sensory rhodopsin and its transfer to the cognate transducer. Nature 2006;440:115-9.
    • (2006) Nature , vol.440 , pp. 115-119
    • Moukhametzianov, R.1    Klare, J.P.2    Efremov, R.3    Baeken, C.4    Göppner, A.5    Labahn, J.6
  • 34
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • Subramaniam S, Henderson R. Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature 2000;406:653-7.
    • (2000) Nature , vol.406 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 36
    • 37349092335 scopus 로고    scopus 로고
    • Spectral characteristics of the photocycle of channelrhodopsin-2 and its implication for channel function
    • Bamann C, Kirsch T, Nagel G, Bamberg E. Spectral characteristics of the photocycle of channelrhodopsin-2 and its implication for channel function. J Mol Biol 2008;375:686-94.
    • (2008) J Mol Biol , vol.375 , pp. 686-694
    • Bamann, C.1    Kirsch, T.2    Nagel, G.3    Bamberg, E.4
  • 37
    • 84876229081 scopus 로고    scopus 로고
    • Light-dark adaptation of channelrhodopsin C128T mutant
    • Ritter E, Piwowarski P, Hegemann P, Bartl FJ. Light-dark adaptation of channelrhodopsin C128T mutant. J Biol Chem 2013;288:10451-8.
    • (2013) J Biol Chem , vol.288 , pp. 10451-10458
    • Ritter, E.1    Piwowarski, P.2    Hegemann, P.3    Bartl, F.J.4
  • 38
    • 77952304469 scopus 로고    scopus 로고
    • The branched photocycle of the slow-cycling channelrhodopsin-2 mutant C128T
    • Stehfest K, Ritter E, Berndt A, Bartl F, Hegemann P. The branched photocycle of the slow-cycling channelrhodopsin-2 mutant C128T. J Mol Biol 2010;398:690-702.
    • (2010) J Mol Biol , vol.398 , pp. 690-702
    • Stehfest, K.1    Ritter, E.2    Berndt, A.3    Bartl, F.4    Hegemann, P.5
  • 39
    • 0348053809 scopus 로고
    • Preservation of membranes in anhydrobiotic organisms: The role of trehalose
    • Crowe JH, Crowe LM, Chapman D. Preservation of membranes in anhydrobiotic organisms: the role of trehalose. Science (New York NY) 1984;223:701-3.
    • (1984) Science (New York NY) , vol.223 , pp. 701-703
    • Crowe, J.H.1    Crowe, L.M.2    Chapman, D.3
  • 40
    • 0032695274 scopus 로고    scopus 로고
    • Trehalose embedding technique for high-resolution electron crystallography: Application to structural study on bacteriorhodopsin
    • Hirai TT, Murata KK, Mitsuoka KK, Kimura YY, Fujiyoshi YY. Trehalose embedding technique for high-resolution electron crystallography: application to structural study on bacteriorhodopsin. J Electron Microsc (Tokyo) 1998;48:653-8.
    • (1998) J Electron Microsc (Tokyo) , vol.48 , pp. 653-658
    • Hirai, T.T.1    Murata, K.K.2    Mitsuoka, K.K.3    Kimura, Y.Y.4    Fujiyoshi, Y.Y.5
  • 41
    • 58149477054 scopus 로고    scopus 로고
    • Effect of trehalose on protein structure
    • Jain NK, Roy I. Effect of trehalose on protein structure. Protein Sci 2008;18:24-36.
    • (2008) Protein Sci , vol.18 , pp. 24-36
    • Jain, N.K.1    Roy, I.2
  • 42
    • 0027408831 scopus 로고
    • Glucose alone does not completely hydrate bacteriorhodopsin in glucose-embedded purple membrane
    • Perkins GAG, Burkard FF, Liu EE, Glaeser RMR. Glucose alone does not completely hydrate bacteriorhodopsin in glucose-embedded purple membrane. J Microsc (Oxford) 1992;169:61-5.
    • (1992) J Microsc (Oxford) , vol.169 , pp. 61-65
    • Perkins, G.A.G.1    Burkard, F.F.2    Liu, E.E.3    Glaeser, R.M.R.4
  • 43
    • 33646155331 scopus 로고    scopus 로고
    • Enhancing functional production of G proteincoupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen
    • André N, Cherouati N, Prual C, Steffan T, Zeder-Lutz G, Magnin T, et al. Enhancing functional production of G proteincoupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen. Protein Sci 2006;15:1115-26.
    • (2006) Protein Sci , vol.15 , pp. 1115-1126
    • André, N.1    Cherouati, N.2    Prual, C.3    Steffan, T.4    Zeder-Lutz, G.5    Magnin, T.6
  • 44
    • 0026061928 scopus 로고
    • High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media
    • Kühlbrandt W, Wang D. High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media. J Mol Biol 1991;217:691-9.
    • (1991) J Mol Biol , vol.217 , pp. 691-699
    • Kühlbrandt, W.1    Wang, D.2
  • 46
    • 36049000626 scopus 로고    scopus 로고
    • 2dx-merge: Data management and merging for 2D crystal images
    • Gipson B, Zeng X, Stahlberg H. 2dx-merge: data management and merging for 2D crystal images. J Struct Biol 2007;160:375-84.
    • (2007) J Struct Biol , vol.160 , pp. 375-384
    • Gipson, B.1    Zeng, X.2    Stahlberg, H.3
  • 47
  • 49
    • 0028103275 scopus 로고
    • The CCP4 Suite - Programs for protein crystallography
    • Bailey S. The CCP4 Suite - programs for protein crystallography. Acta Crystallogr Sect D Biol Crystallogr 1994;50:760-3.
    • (1994) Acta Crystallogr Sect D Biol Crystallogr , vol.50 , pp. 760-763
    • Bailey, S.1
  • 50
    • 0028059991 scopus 로고
    • Analysis of electron microscope images and electron diffraction patterns of thin crystals of phi 29 connectors in ice
    • Valpuesta JM, Valpuesta JM, Carrascosa JL, Carrascosa JL, Henderson R, Henderson R. Analysis of electron microscope images and electron diffraction patterns of thin crystals of phi 29 connectors in ice. J Mol Biol 1994;240:281-7.
    • (1994) J Mol Biol , vol.240 , pp. 281-287
    • Valpuesta, J.M.1    Valpuesta, J.M.2    Carrascosa, J.L.3    Carrascosa, J.L.4    Henderson, R.5    Henderson, R.6


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