메뉴 건너뛰기




Volumn 83, Issue 2, 2007, Pages 293-302

Interaction of the halobacterial transducer to a halorhodopsin mutant engineered so as to bind the transducer: Cl- circulation within the extracellular channel

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEAL PROTEIN; CAROTENOID; CHLORIDE; HALORHODOPSIN; HTRII PROTEIN, NATRONOBACTERIUM PHARAONIS; PHOTOTAXIS RECEPTOR SENSORY RHODOPSIN II, NATRONOBACTERIUM PHARAONIS; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 34247272464     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/2006-06-09-RA-916     Document Type: Conference Paper
Times cited : (33)

References (48)
  • 1
    • 0018834616 scopus 로고
    • ATP synthesis linked to light-dependent proton uptake in a red mutant strain of Halobacterium lacking bacteriorhodopsin
    • Matsuno-Yagi, A. and Y. Mukohata (1980) ATP synthesis linked to light-dependent proton uptake in a red mutant strain of Halobacterium lacking bacteriorhodopsin. Arch. Biochem. Biophys. 199, 297-303.
    • (1980) Arch. Biochem. Biophys , vol.199 , pp. 297-303
    • Matsuno-Yagi, A.1    Mukohata, Y.2
  • 2
    • 0342484454 scopus 로고    scopus 로고
    • Analogy between halorhodopsin and bacteriorhodopsin
    • Váró, G. (2000) Analogy between halorhodopsin and bacteriorhodopsin. Biochim. Biophys. Acta 1460, 220-229.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 220-229
    • Váró, G.1
  • 3
    • 0036667739 scopus 로고    scopus 로고
    • Halorhodopsin: Light-driven ion pumping made simple?
    • Essen, L. O (2002) Halorhodopsin: Light-driven ion pumping made simple? Curr. Opin. Struct. Biol. 12, 516-522.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 516-522
    • Essen, L.O.1
  • 5
    • 0032987196 scopus 로고    scopus 로고
    • Closing in on bacteriorhodopsin: Progress in understanding the molecule
    • Haupts, U., J. Tittor and D. Oesterhelt (1999) Closing in on bacteriorhodopsin: Progress in understanding the molecule. Annu. Rev. Biophys. Biomol. Struct. 28, 367-399.
    • (1999) Annu. Rev. Biophys. Biomol. Struct , vol.28 , pp. 367-399
    • Haupts, U.1    Tittor, J.2    Oesterhelt, D.3
  • 6
    • 0021756564 scopus 로고
    • Mechanism of color discrimination by a bacterial sensory rhodopsin
    • Spudich, J. L. and R. A. Bogomolni (1984) Mechanism of color 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
  • 7
    • 0020841103 scopus 로고
    • Photochemistry of two rhodopsin-like pigments in bacteriorhodopsin-free mutant of Halobacterium halobium
    • Hazemoto, N., N. Kamo, Y. Terayama, Y. Kobatake and M. Tsuda (1983) Photochemistry of two rhodopsin-like pigments in bacteriorhodopsin-free mutant of Halobacterium halobium. Biophys. J. 44, 59-64.
    • (1983) Biophys. J , vol.44 , pp. 59-64
    • Hazemoto, N.1    Kamo, N.2    Terayama, Y.3    Kobatake, Y.4    Tsuda, M.5
  • 8
    • 0021873222 scopus 로고
    • A photosystem other than PS370 also mediates the negative phototaxis of Halobacterium halobium
    • Takahashi, T., H. Tomioka, N. Kamo and Y. Kobatake (1985) A photosystem other than PS370 also mediates the negative phototaxis of Halobacterium halobium. FEMS Microbiol. Lett. 28, 161-164.
    • (1985) FEMS Microbiol. Lett , vol.28 , pp. 161-164
    • Takahashi, T.1    Tomioka, H.2    Kamo, N.3    Kobatake, Y.4
  • 9
    • 0022442116 scopus 로고
    • Flash spectrophotometric identification of a 4th rhodopsin-like pigment in halobacterium halobium
    • Tomioka, H., T. Takahashi, N. Kamo and Y. Kobatake (1986) Flash spectrophotometric identification of a 4th rhodopsin-like pigment in halobacterium halobium. Biochem. Biophys. Res. Commun. 139, 389-395.
    • (1986) Biochem. Biophys. Res. Commun , vol.139 , pp. 389-395
    • Tomioka, H.1    Takahashi, T.2    Kamo, N.3    Kobatake, Y.4
  • 10
    • 0035498353 scopus 로고    scopus 로고
    • Photochemistry and photoinduced proton-transfer by pharaonis phoborhodopsin
    • Kamo, N., K. Shimono, M. Iwamoto and Y. Sudo (2001) Photochemistry and photoinduced proton-transfer by pharaonis phoborhodopsin. Biochemistry (Mosc) 66, 1277-1282.
    • (2001) Biochemistry (Mosc) , vol.66 , pp. 1277-1282
    • Kamo, N.1    Shimono, K.2    Iwamoto, M.3    Sudo, Y.4
  • 11
    • 0035943457 scopus 로고    scopus 로고
    • Crystal structure of sensory rhodopsin II at 2.4 angstroms: Insights into color tuning and transducer interaction
    • Luecke, H., B. Schobert, J. K. Lanyi, E. N. Spudich and 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.
    • (2001) Science , vol.293 , pp. 1499-1503
    • Luecke, H.1    Schobert, B.2    Lanyi, J.K.3    Spudich, E.N.4    Spudich, J.L.5
  • 12
    • 0030906654 scopus 로고    scopus 로고
    • Molecular mechanism of photosignaling by archaeal sensory rhodopsins
    • Hoff, W. D., K. H. Jung and J. L. Spudich (1997) Molecular mechanism of photosignaling by archaeal sensory rhodopsins. Annu. Rev. Biophys. Biomol. Struct. 26, 223-258.
    • (1997) Annu. Rev. Biophys. Biomol. Struct , vol.26 , pp. 223-258
    • Hoff, W.D.1    Jung, K.H.2    Spudich, J.L.3
  • 13
    • 14344254083 scopus 로고    scopus 로고
    • Molecular mechanism of protein-protein interaction of pharaonis phoborhodopsin?transducer and photosignal transfer reaction by the complex
    • Sudo, Y., H. Kandori and N. Kamo (2004) Molecular mechanism of protein-protein interaction of pharaonis phoborhodopsin?transducer and photosignal transfer reaction by the complex. Recent Res. Devel. Biophys. 3, 1-16.
    • (2004) Recent Res. Devel. Biophys , vol.3 , pp. 1-16
    • Sudo, Y.1    Kandori, H.2    Kamo, N.3
  • 14
    • 0033514438 scopus 로고    scopus 로고
    • The specificity of interaction of archaeal transducers with their cognate sensory rhodopsins is determined by their transmembrane helices
    • Zhang, X. N., J. Zhu and J. L. Spudich (1999) The specificity of interaction of archaeal transducers with their cognate sensory rhodopsins is determined by their transmembrane helices. Proc. Natl Acad. Sci. USA 96, 857-862.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 857-862
    • Zhang, X.N.1    Zhu, J.2    Spudich, J.L.3
  • 15
    • 0342624740 scopus 로고    scopus 로고
    • Deletion analysis of the che operon in the archaeon Halobacterium salinarium
    • Rudolph, J. and D. Oesterhelt (1996) Deletion analysis of the che operon in the archaeon Halobacterium salinarium. J. Mol. Biol. 258, 548-554.
    • (1996) J. Mol. Biol , vol.258 , pp. 548-554
    • Rudolph, J.1    Oesterhelt, D.2
  • 17
    • 0031455398 scopus 로고    scopus 로고
    • The two-component signaling pathway of bacterial chemotaxis: A molecular view of signal transduction by receptors, kinases, and adaptation enzymes
    • Falke, J. J., R. B. Bass, S. L. Butler, S. A. Chervitz and M. A. Danielson (1997) The two-component signaling pathway of bacterial chemotaxis: A molecular view of signal transduction by receptors, kinases, and adaptation enzymes. Annu. Rev. Cell Dev. Biol. 13, 457-512.
    • (1997) Annu. Rev. Cell Dev. Biol , vol.13 , pp. 457-512
    • Falke, J.J.1    Bass, R.B.2    Butler, S.L.3    Chervitz, S.A.4    Danielson, M.A.5
  • 19
    • 33644827372 scopus 로고    scopus 로고
    • Importance of specific hydrogen bonds of archaeal rhodopsins for the binding to the transducer protein
    • Sudo, Y., M. Yamabi, S. Kato, C. Hasegawa, M. Iwamoto, K. Shimono and N. Kamo (2006) Importance of specific hydrogen bonds of archaeal rhodopsins for the binding to the transducer protein. J. Mol. Biol. 357, 1274-1282.
    • (2006) J. Mol. Biol , vol.357 , pp. 1274-1282
    • Sudo, Y.1    Yamabi, M.2    Kato, S.3    Hasegawa, C.4    Iwamoto, M.5    Shimono, K.6    Kamo, N.7
  • 20
    • 0035470682 scopus 로고    scopus 로고
    • Pharaonis phoborhodopsin binds to its cognate truncated transducer even in the presence of a detergent with a 1:1 stoichiometry
    • Sudo, Y., M. Iwamoto, K. Shimono and N. Kamo (2001) Pharaonis phoborhodopsin binds to its cognate truncated transducer even in the presence of a detergent with a 1:1 stoichiometry. Photochem. Photobiol. 74, 489-494.
    • (2001) Photochem. Photobiol , vol.74 , pp. 489-494
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Kamo, N.4
  • 21
    • 15444378199 scopus 로고    scopus 로고
    • Role of putative anion-binding sites in cytoplasmic and extracellular channels of Natronomonas pharaonis halorhodopsin
    • Sato, M., M. Kubo, T. Aizawa, N. Kamo, T. Kikukawa, K. Nitta and M. Demura (2005) Role of putative anion-binding sites in cytoplasmic and extracellular channels of Natronomonas pharaonis halorhodopsin. Biochemistry 44, 4775-4784.
    • (2005) Biochemistry , vol.44 , pp. 4775-4784
    • Sato, M.1    Kubo, M.2    Aizawa, T.3    Kamo, N.4    Kikukawa, T.5    Nitta, K.6    Demura, M.7
  • 22
    • 0344413602 scopus 로고    scopus 로고
    • Interaction of Natronomonas pharaonis phoborhodopsin (sensory rhodopsin II) with its cognate transducer probed by increase in the thermal stability
    • Sudo, Y., M. Yamabi, M. Iwamoto, K. Shimono and N. Kamo (2003) Interaction of Natronomonas pharaonis phoborhodopsin (sensory rhodopsin II) with its cognate transducer probed by increase in the thermal stability. Photochem. Photobiol. 78, 511-516.
    • (2003) Photochem. Photobiol , vol.78 , pp. 511-516
    • Sudo, Y.1    Yamabi, M.2    Iwamoto, M.3    Shimono, K.4    Kamo, N.5
  • 23
    • 1842778906 scopus 로고    scopus 로고
    • Functional identification of SLC5A8, a tumor suppressor downregulated in colon cancer, as a Na(+)-coupled transporter for short-chain fatty acids
    • Miyauchi, S., E. Gopal, Y. J. Fei and V. Ganapathy (2004) Functional identification of SLC5A8, a tumor suppressor downregulated in colon cancer, as a Na(+)-coupled transporter for short-chain fatty acids. J. Biol. Chem. 279, 13293-13296.
    • (2004) J. Biol. Chem , vol.279 , pp. 13293-13296
    • Miyauchi, S.1    Gopal, E.2    Fei, Y.J.3    Ganapathy, V.4
  • 25
    • 0034874537 scopus 로고    scopus 로고
    • Temperature and halide dependence of the photocycle of halorhodopsin from Natronobacterium pharaonis
    • Chizhov, I. and M. Engelhard (2001) Temperature and halide dependence of the photocycle of halorhodopsin from Natronobacterium pharaonis. Biophys. J. 81, 1600-1612.
    • (2001) Biophys. J , vol.81 , pp. 1600-1612
    • Chizhov, I.1    Engelhard, M.2
  • 28
    • 0342979867 scopus 로고    scopus 로고
    • Sensory rhodopsin II from the halo-alkaliphilic Natronobacterium pharaonis: Light-activated proton transfer reactions
    • Schmies, G., B. Lüttenberg, I. Chizhov, M. Engelhard, A. Becker and E. Bamberg (2000) Sensory rhodopsin II from the halo-alkaliphilic Natronobacterium pharaonis: Light-activated proton transfer reactions. Biophys. J. 78, 967-976.
    • (2000) Biophys. J , vol.78 , pp. 967-976
    • Schmies, G.1    Lüttenberg, B.2    Chizhov, I.3    Engelhard, M.4    Becker, A.5    Bamberg, E.6
  • 29
    • 0035852672 scopus 로고    scopus 로고
    • Electrophysiological characterization of specific interactions between bacterial sensory rhodopsins and their transducers
    • Schmies, G., M. Engelhard, P. G. Wood, G. Nagel and E. Bamberg (2001) Electrophysiological characterization of specific interactions between bacterial sensory rhodopsins and their transducers. Proc. Natl Acad. Sci. USA 98, 1555-1559.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 1555-1559
    • Schmies, G.1    Engelhard, M.2    Wood, P.G.3    Nagel, G.4    Bamberg, E.5
  • 32
    • 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, K. Shimono, M. Sumi and 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.
    • (2001) Biophys. J , vol.80 , pp. 916-922
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Sumi, M.4    Kamo, N.5
  • 33
    • 0028869129 scopus 로고
    • Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 1. The photochemical cycle
    • Váró , G., L. S. Brown, J. Sasaki, H. Kandori, A. Maeda, R. Needleman and J. K. Lanyi (1995) Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 1. The photochemical cycle. Biochemistry 34, 14490-14499.
    • (1995) Biochemistry , vol.34 , pp. 14490-14499
    • Váró, G.1    Brown, L.S.2    Sasaki, J.3    Kandori, H.4    Maeda, A.5    Needleman, R.6    Lanyi, J.K.7
  • 34
    • 0037133298 scopus 로고    scopus 로고
    • Stopped-flow analysis on anion binding to blue-form halorhodopsin from Natronobacterium pharaonis: Comparison with the anion-uptake process during the photocycle
    • Sato, M., T. Kanamori, N. Kamo, M. Demura and K. Nitta (2002) Stopped-flow analysis on anion binding to blue-form halorhodopsin from Natronobacterium pharaonis: Comparison with the anion-uptake process during the photocycle. Biochemistry 41, 2452-2458.
    • (2002) Biochemistry , vol.41 , pp. 2452-2458
    • Sato, M.1    Kanamori, T.2    Kamo, N.3    Demura, M.4    Nitta, K.5
  • 35
    • 0024968421 scopus 로고
    • Transient spectroscopy of bacterial rhodopsins with an optical multichannel analyzer. 2. Effects of anions on the halorhodopsin photocycle
    • Zimanyi, L. and J. K. Lanyi (1989) Transient spectroscopy of bacterial rhodopsins with an optical multichannel analyzer. 2. Effects of anions on the halorhodopsin photocycle. Biochemistry 28, 5172-5179.
    • (1989) Biochemistry , vol.28 , pp. 5172-5179
    • Zimanyi, L.1    Lanyi, J.K.2
  • 36
    • 0027050450 scopus 로고
    • Resonance Raman study of halorhodopsin photocycle kinetics, chromophore structure, and chloride-pumping mechanism
    • Ames, J. B., J. Raap, J. Lugtenburg and R. A. Mathies (1992) Resonance Raman study of halorhodopsin photocycle kinetics, chromophore structure, and chloride-pumping mechanism. Biochemistry 31, 12546-12554.
    • (1992) Biochemistry , vol.31 , pp. 12546-12554
    • Ames, J.B.1    Raap, J.2    Lugtenburg, J.3    Mathies, R.A.4
  • 37
    • 0028808334 scopus 로고
    • Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 2. Chloride release and uptake, protein conformation change, and thermodynamics
    • Váró , G., R. Needleman and J. K. Lanyi (1995) Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 2. Chloride release and uptake, protein conformation change, and thermodynamics. Biochemistry 34, 14500-14507.
    • (1995) Biochemistry , vol.34 , pp. 14500-14507
    • Váró, G.1    Needleman, R.2    Lanyi, J.K.3
  • 38
    • 0034075676 scopus 로고    scopus 로고
    • Charge motions during the photocycle of pharaonis halorhodopsin
    • Ludmann, K., G. Ibron, J. K. Lanyi and G. Váró (2000) Charge motions during the photocycle of pharaonis halorhodopsin. Biophys. J. 78, 959-966.
    • (2000) Biophys. J , vol.78 , pp. 959-966
    • Ludmann, K.1    Ibron, G.2    Lanyi, J.K.3    Váró, G.4
  • 39
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution
    • Kolbe, M., H. Besir, L. O. Essen and D. Oesterhelt (2000) Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution. Science 288, 1390-1396.
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3    Oesterhelt, D.4
  • 40
    • 0039355490 scopus 로고    scopus 로고
    • Specific arginine and threonine residues control anion binding and transport in the light driven chloride pump halorhodopsin
    • Rüdiger, M. and D. Oesterhelt (1997) Specific arginine and threonine residues control anion binding and transport in the light driven chloride pump halorhodopsin. EMBO J. 16, 3813-3821.
    • (1997) EMBO J , vol.16 , pp. 3813-3821
    • Rüdiger, M.1    Oesterhelt, D.2
  • 41
    • 0032992449 scopus 로고    scopus 로고
    • Time-resolved measurements of photovoltage generation by bacteriorhodopsin and halorhodopsin adsorbed on a thin polymer film
    • Muneyuki, E., C. Shibazaki, H. Ohtani, D. Okuno, M. Asaumi and T. Mogi (1999) Time-resolved measurements of photovoltage generation by bacteriorhodopsin and halorhodopsin adsorbed on a thin polymer film. J. Biochem. (Tokyo) 125, 270-276.
    • (1999) J. Biochem. (Tokyo) , vol.125 , pp. 270-276
    • Muneyuki, E.1    Shibazaki, C.2    Ohtani, H.3    Okuno, D.4    Asaumi, M.5    Mogi, T.6
  • 42
    • 24944531254 scopus 로고    scopus 로고
    • Hydrogen-bonding alterations of the protonated Schiff base and water molecule in the chloride pump of Natronobacterium pharaonis
    • Shibata, M., N. Muneda, T. Sasaki, K. Shimono, N. Kamo, M. Demura and H. Kandori (2005) Hydrogen-bonding alterations of the protonated Schiff base and water molecule in the chloride pump of Natronobacterium pharaonis. Biochemistry 44, 12279-12286.
    • (2005) Biochemistry , vol.44 , pp. 12279-12286
    • Shibata, M.1    Muneda, N.2    Sasaki, T.3    Shimono, K.4    Kamo, N.5    Demura, M.6    Kandori, H.7
  • 43
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • Subramaniam, S. and R. Henderson (2000) Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature 406, 653-657.
    • (2000) Nature , vol.406 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 44
    • 0342646933 scopus 로고    scopus 로고
    • Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin
    • Sass, H. J., G. Buldt, R. Gessenich, D. Hehn, D. Neff, R. Schlesinger, J. Berendzen and P. Ormos (2000) Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin. Nature 406, 649-653.
    • (2000) Nature , vol.406 , pp. 649-653
    • Sass, H.J.1    Buldt, G.2    Gessenich, R.3    Hehn, D.4    Neff, D.5    Schlesinger, R.6    Berendzen, J.7    Ormos, P.8
  • 45
    • 0034658269 scopus 로고    scopus 로고
    • Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography
    • Vonck, J. (2000) Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography. EMBO J. 19, 2152-2160.
    • (2000) EMBO J , vol.19 , pp. 2152-2160
    • Vonck, J.1
  • 46
    • 0035016932 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin
    • Radzwill, N., K. Gerwert and H. J. Steinhoff (2001) Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin. Biophys. J. 80, 2856-2866.
    • (2001) Biophys. J , vol.80 , pp. 2856-2866
    • Radzwill, N.1    Gerwert, K.2    Steinhoff, H.J.3
  • 47
    • 0036231588 scopus 로고    scopus 로고
    • Time-resolved X-ray diffraction reveals movement of F helix of D96N bacteriorhodopsin during M-MN transition at neutral pH
    • Oka, T., N. Yagi, F. Tokunaga and M. Kataoka (2002) Time-resolved X-ray diffraction reveals movement of F helix of D96N bacteriorhodopsin during M-MN transition at neutral pH. Biophys. J. 82, 2610-2616.
    • (2002) Biophys. J , vol.82 , pp. 2610-2616
    • Oka, T.1    Yagi, N.2    Tokunaga, F.3    Kataoka, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.