메뉴 건너뛰기




Volumn 44, Issue 39, 2005, Pages 12923-12931

Disassembling and bleaching of chloride-free pharaonis halorhodopsin by octyl-β-glucoside

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BLEACHING; PH EFFECTS;

EID: 25444496709     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0511235     Document Type: Article
Times cited : (10)

References (43)
  • 1
    • 0034519206 scopus 로고    scopus 로고
    • Retinylidene proteins: Structures and functions from archaea to humans
    • Spudich, J. L., Yang, C. S., Jung, K. H., and Spudich, E. N. (2000) Retinylidene proteins: Structures and functions from archaea to humans, Annu. Rev. Cell Dev. Biol. 16, 365-392.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 365-392
    • Spudich, J.L.1    Yang, C.S.2    Jung, K.H.3    Spudich, E.N.4
  • 2
    • 0034872196 scopus 로고    scopus 로고
    • Can we identify the forces that drive the folding of integral membrane proteins?
    • Booth, P. J., Templer, R. H., Curran, A. R., and Allen, S. J. (2001) Can we identify the forces that drive the folding of integral membrane proteins? Biochem. Soc. Trans. 29, 408-413.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 408-413
    • Booth, P.J.1    Templer, R.H.2    Curran, A.R.3    Allen, S.J.4
  • 3
    • 0342484454 scopus 로고    scopus 로고
    • Analogies between halorhodopsin and bacteriorhodopsin
    • Váró, G. (2000) Analogies between halorhodopsin and bacteriorhodopsin, Biophys. Biochem. Acta 1460, 220-229.
    • (2000) Biophys. Biochem. Acta , vol.1460 , pp. 220-229
    • Váró, G.1
  • 4
    • 0025304015 scopus 로고
    • Halorhodopsin, a light-driven electrogenic chloride-transport system
    • Lanyi, J. K. (1990) Halorhodopsin, a light-driven electrogenic chloride-transport system, Physiol. Rev. 70, 319-330.
    • (1990) Physiol. Rev. , vol.70 , pp. 319-330
    • Lanyi, J.K.1
  • 5
    • 0018834616 scopus 로고
    • ATP synthesis linked to light-dependent proton uptake in a rad mutant strain of Halobacterium lacking bacteriorhodopsin
    • Matsuno-Yagi, A., and Mukohata, Y. (1980) ATP synthesis linked to light-dependent proton uptake in a rad 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
  • 6
    • 0028869129 scopus 로고
    • Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 1. The photochemical cycle
    • Váró, G., Brown, L. S., Sasaki, H., Kandori, H., Maeda, A., Needleman, R., and Lanyi, J. K. (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, H.3    Kandori, H.4    Maeda, A.5    Needleman, R.6    Lanyi, J.K.7
  • 7
    • 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., Needleman, R., and Lanyi, J. K. (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
  • 8
    • 0026463771 scopus 로고
    • Properties and the primary structure of a new halorhodopsin from halobacterial strain mex
    • Otomo, J., Tomioka, H., and Sasabe, H. (1992) Properties and the primary structure of a new halorhodopsin from halobacterial strain mex, Biochim. Biophys. Acta 1112, 7-13.
    • (1992) Biochim. Biophys. Acta , vol.1112 , pp. 7-13
    • Otomo, J.1    Tomioka, H.2    Sasabe, H.3
  • 9
    • 0027167779 scopus 로고
    • Bacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate Halobacterium sp. strain SG1: Three new members of a growing family
    • Soppa, J., Duschl, J., and Oesterhelt, D. (1993) Bacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate Halobacterium sp. strain SG1: Three new members of a growing family, J. Bacteriol. 175, 2720-2726.
    • (1993) J. Bacteriol. , vol.175 , pp. 2720-2726
    • Soppa, J.1    Duschl, J.2    Oesterhelt, D.3
  • 10
    • 0033534585 scopus 로고    scopus 로고
    • Evolution of the archaeal rhodopsins: Evolution rate changes by gene duplication and functional differentiation
    • Ihara, K., Umemura, T., Katagiri, I., Kitajima-Ihara, T., Sugiyama, Y., Kimura, Y., and Mukohata, Y. (1999) Evolution of the archaeal rhodopsins: Evolution rate changes by gene duplication and functional differentiation, J. Mol. Biol. 285, 163-174.
    • (1999) J. Mol. Biol. , vol.285 , pp. 163-174
    • Ihara, K.1    Umemura, T.2    Katagiri, I.3    Kitajima-Ihara, T.4    Sugiyama, Y.5    Kimura, Y.6    Mukohata, Y.7
  • 11
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 a resolution
    • Kolbe, M., Besir, H., Essen, L. O., and Oesterhelt, D. (2000) Structure of the light-driven chloride pump halorhodopsin at 1.8 A 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
  • 12
    • 0025064073 scopus 로고
    • Properties and photochemistry of a halorhodopsin from the haloalkalophile, Natronobacterium pharaonis
    • Duschl, A., Lanyi, J. K., and Zimányi, L. (1990) Properties and photochemistry of a halorhodopsin from the haloalkalophile, Natronobacterium pharaonis, J. Biol. Chem. 265, 1261-1267.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1261-1267
    • Duschl, A.1    Lanyi, J.K.2    Zimányi, L.3
  • 13
    • 0031583910 scopus 로고    scopus 로고
    • Functional expression of pharaonis phoborhcdopsin in Escherichia coli
    • Shimono, K., Iwamoto, M., Sumi, M., and Kamo, N. (1997) Functional expression of pharaonis phoborhcdopsin in Escherichia coli, FEBS Lett. 420, 54-56.
    • (1997) FEBS Lett. , vol.420 , pp. 54-56
    • Shimono, K.1    Iwamoto, M.2    Sumi, M.3    Kamo, N.4
  • 14
    • 0032963356 scopus 로고    scopus 로고
    • Purification of histidine tagged bacteriorhodopsin, pharaonis halorhodopsin, and pharaonis sensory rhodopsin II functionally expressed in Escherichia coli
    • Hohenfeld, I. P., Wegener, A. A., and Engelhard, M. (1999) Purification of histidine tagged bacteriorhodopsin, pharaonis halorhodopsin, and pharaonis sensory rhodopsin II functionally expressed in Escherichia coli, FEBS Lett. 442, 198-202.
    • (1999) FEBS Lett. , vol.442 , pp. 198-202
    • Hohenfeld, I.P.1    Wegener, A.A.2    Engelhard, M.3
  • 15
    • 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., Kanamori, T., Kamo, N., Demura, M., and Nitta, K. (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
  • 16
    • 0038692912 scopus 로고    scopus 로고
    • Ser-130 of Natronobacterium pharaonis halorhodopsin is important for the chloride binding
    • Sato, M., Kikukawa, T., Araiso, T., Okita, H., Shimono, K., Kamo, N., Demura, M., and Nitta, K. (2003) Ser-130 of Natronobacterium pharaonis halorhodopsin is important for the chloride binding, Biophys. Chem. 104, 209-216.
    • (2003) Biophys. Chem. , vol.104 , pp. 209-216
    • Sato, M.1    Kikukawa, T.2    Araiso, T.3    Okita, H.4    Shimono, K.5    Kamo, N.6    Demura, M.7    Nitta, K.8
  • 17
    • 0042821607 scopus 로고    scopus 로고
    • Roles of Ser130 and Thr126 in chloride binding and photocycle of pharaonis halorhodopsin
    • Sato, M., Kikukawa, T., Araiso, T., Okita, H., Shimono, K., Kamo, N., Demura, M., and Nitta, K. (2003) Roles of Ser130 and Thr126 in chloride binding and photocycle of pharaonis halorhodopsin, J. Biochem. 134, 151-158.
    • (2003) J. Biochem. , vol.134 , pp. 151-158
    • Sato, M.1    Kikukawa, T.2    Araiso, T.3    Okita, H.4    Shimono, K.5    Kamo, N.6    Demura, M.7    Nitta, K.8
  • 19
    • 15444378199 scopus 로고    scopus 로고
    • Role of putative anion-binding sites in cytoplasmic and extracellular channels of Natronomonas pharaonis halorhodopsin
    • Sato, M., Kubo, M., Aizawa, T., Kamo, N., Kikukawa, T., Nitta, K., and Demura, M. (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
  • 20
    • 0000942888 scopus 로고    scopus 로고
    • Fourier transform Raman study of retinal isomeric composition and equilibration in halorhodopsin
    • Zimányi, L., and Lanyi, J. K. (1997) Fourier transform Raman study of retinal isomeric composition and equilibration in halorhodopsin, J. Phys. Chem. B 101, 1930-1933.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 1930-1933
    • Zimányi, L.1    Lanyi, J.K.2
  • 21
    • 0031282975 scopus 로고    scopus 로고
    • Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps
    • Lanyi, J. K. (1997) Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps, J. Biol. Chem. 272, 31209-31212.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31209-31212
    • Lanyi, J.K.1
  • 22
    • 0034716941 scopus 로고    scopus 로고
    • The final stages of folding of the membrane protein bacteriorhodopsin occur by kinetically indistinguishable parallel folding paths that are mediated by pH
    • Lu, H., and Booth, P. J. (2000) The final stages of folding of the membrane protein bacteriorhodopsin occur by kinetically indistinguishable parallel folding paths that are mediated by pH, J. Mol. Biol. 299, 233-243.
    • (2000) J. Mol. Biol. , vol.299 , pp. 233-243
    • Lu, H.1    Booth, P.J.2
  • 23
    • 1042302803 scopus 로고    scopus 로고
    • Inhomogeneous stability of bacteriorhodopsin in purple membrane against photobleaching at high temperature
    • Yokoyama, Y., Sonoyama, M., and Mitaku, S. (2004) Inhomogeneous stability of bacteriorhodopsin in purple membrane against photobleaching at high temperature, Proteins 54, 442-454.
    • (2004) Proteins , vol.54 , pp. 442-454
    • Yokoyama, Y.1    Sonoyama, M.2    Mitaku, S.3
  • 24
    • 0032871901 scopus 로고    scopus 로고
    • Light-induced denaturation of bacteriorhodopsin solubilized by octyl-β-glucoside
    • Mukai, Y., Kamo, N., and Mitaku, S. (1999) Light-induced denaturation of bacteriorhodopsin solubilized by octyl-β-glucoside, Protein Eng. 12, 755-759.
    • (1999) Protein Eng. , vol.12 , pp. 755-759
    • Mukai, Y.1    Kamo, N.2    Mitaku, S.3
  • 25
    • 25444529103 scopus 로고    scopus 로고
    • Photobleaching of bacteriorhodopsin solubilized with Triton X-100
    • in press
    • Sasaki, T., Sonoyama, N., Demura, M., and Mitaku, S. (2005) Photobleaching of bacteriorhodopsin solubilized with Triton X-100, Photochem. Photobiol., in press.
    • (2005) Photochem. Photobiol.
    • Sasaki, T.1    Sonoyama, N.2    Demura, M.3    Mitaku, S.4
  • 26
    • 0342932027 scopus 로고    scopus 로고
    • The oligomeric state of Bacillus thuringiensis Cry toxins in solution
    • Guereca, L., and Bravo, A. (1999) The oligomeric state of Bacillus thuringiensis Cry toxins in solution, Biochim. Biophys. Acta 1429, 342-350.
    • (1999) Biochim. Biophys. Acta , vol.1429 , pp. 342-350
    • Guereca, L.1    Bravo, A.2
  • 28
    • 0028286154 scopus 로고
    • Blue halorhodopsin from Natronobacterium pharaonis: Wavelength regulation by anions
    • Scharf, B., and Engelhard, M. (1994) Blue halorhodopsin from Natronobacterium pharaonis: Wavelength regulation by anions, Biochemistry 33, 6387-6393.
    • (1994) Biochemistry , vol.33 , pp. 6387-6393
    • Scharf, B.1    Engelhard, M.2
  • 29
    • 0026633609 scopus 로고
    • Singular value decomposition: Application to analysis of experimental data
    • Henry, E. R., and Hofrichter, J. (1992) Singular value decomposition: Application to analysis of experimental data, Methods Enzymol. 210, 129-193.
    • (1992) Methods Enzymol. , vol.210 , pp. 129-193
    • Henry, E.R.1    Hofrichter, J.2
  • 30
    • 0035576064 scopus 로고    scopus 로고
    • Environment around the chromophore in pharaonis phoborhodopsin: Mutation analysis of the retinal binding site
    • Shimono, K., Ikeura, Y., Sudo, Y., Iwamoto, M., and Kamo, N. (2001) Environment around the chromophore in pharaonis phoborhodopsin: Mutation analysis of the retinal binding site, Biophys. Biochem. Acta 1515, 92-100.
    • (2001) Biophys. Biochem. Acta , vol.1515 , pp. 92-100
    • Shimono, K.1    Ikeura, Y.2    Sudo, Y.3    Iwamoto, M.4    Kamo, N.5
  • 31
    • 25444453372 scopus 로고
    • High-performance liquid Chromatographic and spectroscopic characterization of stereoisomeric retinaloximes. Improvements in resolution and implication of the method
    • Tsukida, K., Ito, M., Tanaka, T., and Yagi, I. (1985) High-performance liquid Chromatographic and spectroscopic characterization of stereoisomeric retinaloximes. Improvements in resolution and implication of the method, J. Chromatogr. 331, 265-272.
    • (1985) J. Chromatogr. , vol.331 , pp. 265-272
    • Tsukida, K.1    Ito, M.2    Tanaka, T.3    Yagi, I.4
  • 32
    • 0034707088 scopus 로고    scopus 로고
    • The vesicle-to-micelle transition of phosphatidylcholine vesicles induced by nonionic detergents: Effects of sodium chloride, sucrose, and urea
    • Walter, A., Kuehl, G., Barnes, K., and VanderWaerdt, G. (2000) The vesicle-to-micelle transition of phosphatidylcholine vesicles induced by nonionic detergents: Effects of sodium chloride, sucrose, and urea, Biochim. Biophys. Acta 1508, 20-33.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 20-33
    • Walter, A.1    Kuehl, G.2    Barnes, K.3    Vanderwaerdt, G.4
  • 33
    • 0026581605 scopus 로고
    • Chromophore configuration of pharaonis phoborhodopsin and its isomerization on photon absorption
    • Imamoto, Y., Shichida, Y., Hirayama, J., Tomioka, H., Kamo, N., and Yoshizawa, T. (1992) Chromophore configuration of pharaonis phoborhodopsin and its isomerization on photon absorption, Biochemistry 31, 2523-2528.
    • (1992) Biochemistry , vol.31 , pp. 2523-2528
    • Imamoto, Y.1    Shichida, Y.2    Hirayama, J.3    Tomioka, H.4    Kamo, N.5    Yoshizawa, T.6
  • 34
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt, D., and Stoeckenius, W. (1971) Rhodopsin-like protein from the purple membrane of Halobacterium halobium, Nature 233, 149-152.
    • (1971) Nature , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 35
    • 5444220123 scopus 로고    scopus 로고
    • Abnormal micellar growth in sugar-based and ethoxylated nonionic surfactants and their mixtures in dilute regimes using analytical ultracentrifugation
    • Zhang, R., and Somasundaran, P. (2004) Abnormal micellar growth in sugar-based and ethoxylated nonionic surfactants and their mixtures in dilute regimes using analytical ultracentrifugation, Langmuir 20, 8552-8558.
    • (2004) Langmuir , vol.20 , pp. 8552-8558
    • Zhang, R.1    Somasundaran, P.2
  • 36
    • 0024289165 scopus 로고
    • Functional reconstitution of halorhodopsin. Properties of halorhodopsin-containing proteoliposomes
    • Duschl, A., McCloskey, M. A., and Lanyi, J. K. (1988) Functional reconstitution of halorhodopsin. Properties of halorhodopsin-containing proteoliposomes, J. Biol. Chem. 263, 17016-17022.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17016-17022
    • Duschl, A.1    McCloskey, M.A.2    Lanyi, J.K.3
  • 37
    • 0020490831 scopus 로고
    • Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures
    • London, E., and Khorana, H. G. (1982) Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures, J. Biol. Chem. 257, 7003-7011.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7003-7011
    • London, E.1    Khorana, H.G.2
  • 38
    • 0026059269 scopus 로고
    • The retinylidene Schiff base counterion in bacteriorhodopsin
    • Marti, T., Rosselet, S. J., Otto, H., Heyn, M. P., and Khorana, H. G. (1991) The retinylidene Schiff base counterion in bacteriorhodopsin, J. Biol. Chem. 266, 18674-18683.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18674-18683
    • Marti, T.1    Rosselet, S.J.2    Otto, H.3    Heyn, M.P.4    Khorana, H.G.5
  • 39
    • 84985429318 scopus 로고
    • Light induced isomerisation, at acidic pH, initiates hydrolysis of bacteriorhodopsin to bacterio-opsin and 9-cis-retinal
    • Fischer, U. C., Towner, P., and Oesterhelt, D. (1981) Light induced isomerisation, at acidic pH, initiates hydrolysis of bacteriorhodopsin to bacterio-opsin and 9-cis-retinal, Photochem. Photobiol. 33, 529-537.
    • (1981) Photochem. Photobiol. , vol.33 , pp. 529-537
    • Fischer, U.C.1    Towner, P.2    Oesterhelt, D.3
  • 40
    • 0023505876 scopus 로고
    • Iso-halorhodopsin: A stable, 9-cis retinal containing photoproduct of halorhodopsin
    • Zimanyi, L., and Lanyi, J. K. (1987) Iso-halorhodopsin: A stable, 9-cis retinal containing photoproduct of halorhodopsin, Biophys. J. 52, 1007-1013.
    • (1987) Biophys. J. , vol.52 , pp. 1007-1013
    • Zimanyi, L.1    Lanyi, J.K.2
  • 41
    • 0022779687 scopus 로고
    • Resonance Raman study of the pink membrane photochemically prepared from the deionized blue membrane of H. halobium
    • Pande, C., Callender, R. H., Chang, C. H., and Ebrey, T. G. (1986) Resonance Raman study of the pink membrane photochemically prepared from the deionized blue membrane of H. halobium, Biophys. J. 50, 545-549.
    • (1986) Biophys. J. , vol.50 , pp. 545-549
    • Pande, C.1    Callender, R.H.2    Chang, C.H.3    Ebrey, T.G.4
  • 42
    • 0001386064 scopus 로고
    • Removal of methyl groups from retinal controls the activity of bacteriorhodopsin
    • Gaertner, W., Towner, P., Hopf, H., and Oesterhelt, D. (1983) Removal of methyl groups from retinal controls the activity of bacteriorhodopsin, Biochemistry 22, 2637-2644.
    • (1983) Biochemistry , vol.22 , pp. 2637-2644
    • Gaertner, W.1    Towner, P.2    Hopf, H.3    Oesterhelt, D.4
  • 43
    • 0030904764 scopus 로고    scopus 로고
    • Intermediates in the assembly of bacteriorhodopsin investigated by time-resolved absorption spectroscopy
    • Booth, P. J., and Farooq, A. (1997) Intermediates in the assembly of bacteriorhodopsin investigated by time-resolved absorption spectroscopy, Eur. J. Biochem. 246, 674-680.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 674-680
    • Booth, P.J.1    Farooq, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.