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Volumn 100, Issue 9, 2011, Pages 2178-2183

Sensory rhodopsin-I as a bidirectional switch: Opposite conformational changes from the same photoisomerization

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EID: 79956297602     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.03.026     Document Type: Article
Times cited : (7)

References (30)
  • 1
    • 55849091415 scopus 로고    scopus 로고
    • A Schiff base connectivity switch in sensory rhodopsin signaling
    • Sineshchekov, O. A., J. Sasaki,..., J. L. Spudich. 2008. A Schiff base connectivity switch in sensory rhodopsin signaling. Proc. Natl. Acad. Sci. USA. 105:16159-16164.
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 16159-16164
    • Sineshchekov, O.A.1    Sasaki, J.2    Spudich, J.L.3
  • 2
    • 77955255169 scopus 로고    scopus 로고
    • Attractant and repellent signaling conformers of sensory rhodopsin-transducer complexes
    • Sineshchekov, O. A., J. Sasaki,..., J. L. Spudich. 2010. Attractant and repellent signaling conformers of sensory rhodopsin-transducer complexes. Biochemistry. 49:6696-6704.
    • (2010) Biochemistry. , vol.49 , pp. 6696-6704
    • Sineshchekov, O.A.1    Sasaki, J.2    Spudich, J.L.3
  • 3
    • 79956329881 scopus 로고    scopus 로고
    • Opposite displacement of helix F in attractant and repellent signaling by sensory rhodopsin-Htr complexes
    • In press
    • Sasaki, J., A. L. Tsai, and J. L. Spudich. 2011. Opposite displacement of helix F in attractant and repellent signaling by sensory rhodopsin-Htr complexes. J. Biol. Chem., In press.
    • (2011) J. Biol. Chem.
    • Sasaki, J.1    Tsai, A.L.2    Spudich, J.L.3
  • 4
    • 0021756564 scopus 로고
    • Mechanism of colour discrimination by a bacterial sensory rhodopsin
    • Spudich, J. L., and R. A. Bogomolni. 1984. Mechanism of colour discrimination by a bacterial sensory rhodopsin. Nature. 312:509-513.
    • (1984) Nature. , vol.312 , pp. 509-513
    • Spudich, J.L.1    Bogomolni, R.A.2
  • 5
    • 0031021374 scopus 로고    scopus 로고
    • General concept for ion translocation by halobacterial retinal proteins: The isomerization/switch/transfer (IST) model
    • DOI 10.1021/bi962014g
    • Haupts, U., J. Tittor,..., D. Oesterhelt. 1997. General concept for ion translocation by halobacterial retinal proteins: the isomerization/switch/ transfer (IST) model. Biochemistry. 36:2-7. (Pubitemid 27024671)
    • (1997) Biochemistry , vol.36 , Issue.1 , pp. 2-7
    • Haupts, U.1    Tittor, J.2    Bamberg, E.3    Oesterhelt, D.4
  • 6
    • 0036821737 scopus 로고    scopus 로고
    • Internal water molecules of archaeal rhodopsins (review)
    • DOI 10.1080/0968768021000035069
    • Furutani, Y., and H. Kandori. 2002. Internal water molecules of archaeal rhodopsins (Review). Mol. Membr. Biol. 19:257-265 (Review). (Pubitemid 36090786)
    • (2002) Molecular Membrane Biology , vol.19 , Issue.4 , pp. 257-265
    • Furutani, Y.1    Kandori, H.2
  • 7
    • 44449102270 scopus 로고    scopus 로고
    • Microbial rhodopsins: Scaffolds for ion pumps, channels, and sensors
    • Klare, J. P., I. Chizhov, and M. Engelhard. 2008. Microbial rhodopsins: scaffolds for ion pumps, channels, and sensors. Results Probl. Cell Differ. 45:73-122.
    • (2008) Results Probl. Cell Differ. , vol.45 , pp. 73-122
    • Klare, J.P.1    Chizhov, I.2    Engelhard, M.3
  • 8
    • 49749116145 scopus 로고    scopus 로고
    • Signal transfer in haloarchaeal sensory rhodopsin-transducer complexes
    • Sasaki, J., and J. L. Spudich. 2008. Signal transfer in haloarchaeal sensory rhodopsin-transducer complexes. Photochem. Photobiol. 84:863-868.
    • (2008) Photochem. Photobiol. , vol.84 , pp. 863-868
    • Sasaki, J.1    Spudich, J.L.2
  • 10
    • 0028126444 scopus 로고
    • Sensory rhodopsin I photocycle intermediate SRI380 contains 13-cis retinal bound via an unprotonated Schiff base
    • Haupts, U., W. Eisfeld,..., D. Oesterhelt. 1994. Sensory rhodopsin I photocycle intermediate SRI380 contains 13-cis retinal bound via an unprotonated Schiff base. FEBS Lett. 356:25-29.
    • (1994) FEBS Lett. , vol.356 , pp. 25-29
    • Haupts, U.1    Eisfeld, W.2    Oesterhelt, D.3
  • 11
    • 0037177209 scopus 로고    scopus 로고
    • Demonstration of 2:2 stoichiometry in the functional SRI-HtrI signaling complex in Halobacterium membranes by gene fusion analysis
    • DOI 10.1021/bi015966h
    • Chen, X., and J. L. Spudich. 2002. Demonstration of 2:2 stoichiometry in the functional SRI-HtrI signaling complex in Halobacterium membranes by gene fusion analysis. Biochemistry. 41:3891-3896. (Pubitemid 34251028)
    • (2002) Biochemistry , vol.41 , Issue.12 , pp. 3891-3896
    • Chen, X.1    Spudich, J.L.2
  • 12
    • 40149094954 scopus 로고    scopus 로고
    • Structural changes of sensory rhodopsin I and its transducer protein are dependent on the protonated state of Asp76
    • DOI 10.1021/bi702050c
    • Furutani, Y., H. Takahashi,..., H. Kandori. 2008. Structural changes of sensory rhodopsin I and its transducer protein are dependent on the protonated state of Asp76. Biochemistry. 47:2875-2883. (Pubitemid 351328839)
    • (2008) Biochemistry , vol.47 , Issue.9 , pp. 2875-2883
    • Furutani, Y.1    Takahashi, H.2    Sasaki, J.3    Sudo, Y.4    Spudich, J.L.5    Kandori, H.6
  • 13
    • 61749098218 scopus 로고    scopus 로고
    • Proton release group of pharaonis phoborhodopsin revealed by ATR-FTIR spectroscopy
    • Kitade, Y., Y. Furutani,..., H. Kandori. 2009. Proton release group of pharaonis phoborhodopsin revealed by ATR-FTIR spectroscopy. Biochemistry. 48:1595-1603.
    • (2009) Biochemistry. , vol.48 , pp. 1595-1603
    • Kitade, Y.1    Furutani, Y.2    Kandori, H.3
  • 15
    • 0029900082 scopus 로고    scopus 로고
    • Protonatable residues at the cytoplasmic end of transmembrane helix-2 in the signal transducer HtrI control photochemistry and function of sensory rhodopsin I
    • DOI 10.1073/pnas.93.13.6557
    • Jung, K.-H., and J. L. Spudich. 1996. Protonatable residues at the cytoplasmic end of transmembrane helix-2 in the signal transducer HtrI control photochemistry and function of sensory rhodopsin I. Proc. Natl. Acad. Sci. USA. 93:6557-6561. (Pubitemid 26230346)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.13 , pp. 6557-6561
    • Jung, K.-H.1    Spudich, J.L.2
  • 16
    • 0029939690 scopus 로고    scopus 로고
    • Asp76 is the Schiff base counterion and proton acceptor in the proton-translocating form of sensory rhodopsin I
    • Rath, P., E. Spudich,..., K. J. Rothschild. 1996. Asp76 is the Schiff base counterion and proton acceptor in the proton-translocating form of sensory rhodopsin I. Biochemistry. 35:6690-6696.
    • (1996) Biochemistry. , vol.35 , pp. 6690-6696
    • Rath, P.1    Spudich, E.2    Rothschild, K.J.3
  • 17
    • 0034696409 scopus 로고    scopus 로고
    • 540 intermediate of sensory rhodopsin II: Asp73 is the Schiff base proton acceptor
    • DOI 10.1021/bi991676d
    • Bergo, V., E. N. Spudich,..., K. J. Rothschild. 2000. FTIR analysis of the SII540 intermediate of sensory rhodopsin II: Asp73 is the Schiff base proton acceptor. Biochemistry. 39:2823-2830. (Pubitemid 30159386)
    • (2000) Biochemistry , vol.39 , Issue.11 , pp. 2823-2830
    • Bergo, V.1    Spudich, E.N.2    Scott, K.L.3    Spudich, J.L.4    Rothschild, K.J.5
  • 19
    • 0029445538 scopus 로고
    • Rapid high-yield purification and liposome reconstitution of polyhistidine-tagged sensory rhodopsin I
    • Krebs, M. P., E. N. Spudich, and J. L. Spudich. 1995. Rapid high-yield purification and liposome reconstitution of polyhistidine-tagged sensory rhodopsin I. Protein Expr. Purif. 6:780-788.
    • (1995) Protein Expr. Purif. , vol.6 , pp. 780-788
    • Krebs, M.P.1    Spudich, E.N.2    Spudich, J.L.3
  • 20
    • 0024959624 scopus 로고
    • Bacteriorhodopsin's M412 intermediate contains a 13-cis, 14-s-trans, 15-anti-retinal Schiff base chromophore
    • Ames, J. B., S. P. Fodor,..., R. A. Mathies. 1989. Bacteriorhodopsin's M412 intermediate contains a 13-cis, 14-s-trans, 15-anti-retinal Schiff base chromophore. Biochemistry. 28:3681-3687.
    • (1989) Biochemistry. , vol.28 , pp. 3681-3687
    • Ames, J.B.1    Fodor, S.P.2    Mathies, R.A.3
  • 22
    • 0024280218 scopus 로고
    • Chromophore structure in bacteriorhodopsin's N intermediate: Implications for the protonpumping mechanism
    • Fodor, S. P., J. B. Ames,..., R. A. Mathies. 1988. Chromophore structure in bacteriorhodopsin's N intermediate: implications for the protonpumping mechanism. Biochemistry. 27:7097-7101.
    • (1988) Biochemistry. , vol.27 , pp. 7097-7101
    • Fodor, S.P.1    Ames, J.B.2    Mathies, R.A.3
  • 23
    • 33749557420 scopus 로고    scopus 로고
    • Microbial rhodopsins: Functional versatility and genetic mobility
    • DOI 10.1016/j.tim.2006.09.006, PII S0966842X06002307
    • Sharma, A. K., J. L. Spudich, and W. F. Doolittle. 2006. Microbial rhodopsins: functional versatility andgenetic mobility. Trends Microbiol. 14:463-469. (Pubitemid 44537809)
    • (2006) Trends in Microbiology , vol.14 , Issue.11 , pp. 463-469
    • Sharma, A.K.1    Spudich, J.L.2    Doolittle, W.F.3
  • 25
    • 0035142193 scopus 로고    scopus 로고
    • Photo-induced proton transport of pharaonis phoborhodopsin (sensory rhodopsin II) is ceased by association with the transducer
    • Sudo, Y., M. Iwamoto,..., N. Kamo. 2001. Photo-induced proton transport of pharaonis phoborhodopsin (sensory rhodopsin II) is ceased by association with the transducer. Biophys. J. 80:916-922. (Pubitemid 32128342)
    • (2001) Biophysical Journal , vol.80 , Issue.2 , pp. 916-922
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Sumi, M.4    Kamo, N.5
  • 26
    • 0031929447 scopus 로고    scopus 로고
    • Sensory rhodopsin II transducer HtrII is also responsible for serine chemotaxis in the archaeon Halobacterium salinarum
    • Hou, S., A. Brooun,..., M. Alam. 1998. Sensory rhodopsin II transducer HtrII is also responsible for serine chemotaxis in the archaeon Halobacterium salinarum. J. Bacteriol. 180:1600-1602. (Pubitemid 28125752)
    • (1998) Journal of Bacteriology , vol.180 , Issue.6 , pp. 1600-1602
    • Hou, S.1    Brooun, A.2    Yu, H.S.3    Freitas, T.4    Alam, M.5
  • 28
    • 0035943457 scopus 로고    scopus 로고
    • Crystal structure of sensory rhodopsin II at 2.4 angstroms: Insights into color tuning and transducer interaction
    • DOI 10.1126/science.1062977
    • Luecke, H., B. Schobert,..., J. L. Spudich. 2001. Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction. Science. 293:1499-1503. (Pubitemid 32801553)
    • (2001) Science , vol.293 , Issue.5534 , pp. 1499-1503
    • Luecke, H.1    Schobert, B.2    Lanyi, J.K.3    Spudich, E.N.4    Spudich, J.L.5
  • 29
    • 0034714097 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helix F in spin-labelled pharaonis sensory rhodopsin II
    • Wegener, A. A., I. Chizhov,..., H. J. Steinhoff. 2000. Time-resolved detection of transient movement of helix F in spin-labelled pharaonis sensory rhodopsin II. J. Mol. Biol. 301:881-891.
    • (2000) J. Mol. Biol. , vol.301 , pp. 881-891
    • Wegener, A.A.1    Chizhov, I.2    Steinhoff, H.J.3
  • 30
    • 34247243258 scopus 로고    scopus 로고
    • Analysis of light-induced conformational changes of Natronomonas pharaonis sensory rhodopsin II by time resolved electron paramagnetic resonance spectroscopy
    • DOI 10.1562/2006-07-05-RA-960
    • Bordignon, E., J. P. Klare,..., H. J. Steinhoff. 2007. Analysis of lightinduced conformational changes of Natronomonas pharaonis sensory rhodopsin II by time resolved electron paramagnetic resonance spectroscopy. Photochem. Photobiol. 83:263-272. (Pubitemid 46623047)
    • (2007) Photochemistry and Photobiology , vol.83 , Issue.2 , pp. 263-272
    • Bordignon, E.1    Klare, J.P.2    Holterhues, J.3    Martell, S.4    Krasnaberski, A.5    Engelhard, M.6    Steinhoff, H.-J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.