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Volumn 125, Issue 4, 1999, Pages 649-657

Halobacterial rhodopsins

Author keywords

Bacterial rhodopsin; Bacteriorhodopsin; Evolution of bacterial rhodopsin; Halobacteria; Retinal protein

Indexed keywords

BACTERIORHODOPSIN; HALIDE; PROTON PUMP; RHODOPSIN;

EID: 0032961349     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022332     Document Type: Review
Times cited : (81)

References (58)
  • 1
    • 0015244599 scopus 로고
    • Structure of the purple membrane
    • Blaurock, A. and Stoeckenius, W. (1971) Structure of the purple membrane. Nat. New Biol. 233, 152-155
    • (1971) Nat. New Biol. , vol.233 , pp. 152-155
    • Blaurock, A.1    Stoeckenius, W.2
  • 2
    • 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. Nat. New Biol. 233, 149-152
    • (1971) Nat. New Biol. , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 4
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson, R. and Unwin, P.N.T. (1975) Three-dimensional model of purple membrane obtained by electron microscopy. Nature 257, 28-32
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 5
  • 7
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R.F. (1981) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132
    • (1981) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 8
    • 0010377880 scopus 로고
    • The antigenic structure and topography of bacteriorhodopsin in purple membranes as determined by interaction with monoclonal antibodies
    • Ovchinnikov, Y.A., Abdulaev, N.G., Vasilov, R.G., Vturina, I.Y., Kuryatov, A.B., and Kiselev, A.V. (1985) The antigenic structure and topography of bacteriorhodopsin in purple membranes as determined by interaction with monoclonal antibodies. FEBS Lett. 179, 343-350
    • (1985) FEBS Lett. , vol.179 , pp. 343-350
    • Ovchinnikov, Y.A.1    Abdulaev, N.G.2    Vasilov, R.G.3    Vturina, I.Y.4    Kuryatov, A.B.5    Kiselev, A.V.6
  • 9
    • 0002743109 scopus 로고
    • Evidence for the protonation of two internal carboxylic groups during the photocycle of bacteriorhodopsin. Investigation by kinetic infrared spectroscopy
    • Siebert, F., Mantele, W., and Kreutz, W. (1982) Evidence for the protonation of two internal carboxylic groups during the photocycle of bacteriorhodopsin. Investigation by kinetic infrared spectroscopy. FEBS Lett. 141, 82-87
    • (1982) FEBS Lett. , vol.141 , pp. 82-87
    • Siebert, F.1    Mantele, W.2    Kreutz, W.3
  • 10
    • 0023776215 scopus 로고
    • Fourie transform infrared techniques for probing membrane protein structure
    • Braiman, M.S. and Rothschild, K.J. (1988) Fourie transform infrared techniques for probing membrane protein structure. Annu. Rev. Biophys. Biophys. Chem. 17, 541-570
    • (1988) Annu. Rev. Biophys. Biophys. Chem. , vol.17 , pp. 541-570
    • Braiman, M.S.1    Rothschild, K.J.2
  • 11
    • 0024278712 scopus 로고
    • Bacteriorhodopsin, a membrane protein that uses light to translocate protons
    • Khorana, H.G. (1988) Bacteriorhodopsin, a membrane protein that uses light to translocate protons. J. Biol. Chem. 263, 7439-7442
    • (1988) J. Biol. Chem. , vol.263 , pp. 7439-7442
    • Khorana, H.G.1
  • 12
    • 0027526352 scopus 로고
    • Mechanism of light-dependent protontranslocation by bacteriorhodopsin
    • Krebs, M.P. and Khorana, H.G. (1993) Mechanism of light-dependent protontranslocation by bacteriorhodopsin. J. Bacteriol. 175, 1555-1560
    • (1993) J. Bacteriol. , vol.175 , pp. 1555-1560
    • Krebs, M.P.1    Khorana, H.G.2
  • 15
    • 0031583474 scopus 로고    scopus 로고
    • Chloride and proton transport in bacteriorhodopsin mutant D85T: Different modes of ion translocation in a retinal protein
    • Tittor, J., Haupt, U., Haupt, C., Oesterhelt, D., Becker, A., and Bamberg, E. (1997) Chloride and proton transport in bacteriorhodopsin mutant D85T: different modes of ion translocation in a retinal protein. J. Mol. Biol. 271, 405-416
    • (1997) J. Mol. Biol. , vol.271 , pp. 405-416
    • Tittor, J.1    Haupt, U.2    Haupt, C.3    Oesterhelt, D.4    Becker, A.5    Bamberg, E.6
  • 16
    • 0027317263 scopus 로고
    • The photochemical reactions of sensory rhodopsin I are altered by its transducer
    • Spudich, E.N. and Spudich, J.L. (1993) The photochemical reactions of sensory rhodopsin I are altered by its transducer. J. Biol. Chem. 268, 16095-16097
    • (1993) J. Biol. Chem. , vol.268 , pp. 16095-16097
    • Spudich, E.N.1    Spudich, J.L.2
  • 17
    • 0027967379 scopus 로고
    • Protein-protein interaction converts a proton pump into a sensory receptor
    • Spudich, J.L. (1994) Protein-protein interaction converts a proton pump into a sensory receptor. Cell 79, 747-750
    • (1994) Cell , vol.79 , pp. 747-750
    • Spudich, J.L.1
  • 18
    • 0031021374 scopus 로고    scopus 로고
    • General concept for ion translocation by halobacterial retinal proteins: The isomerization/switch/transfer (IST) model
    • Haupts, U., Tittor, J., Bamberg, E., and Oesterhelt, D. (1997) General concept for ion translocation by halobacterial retinal proteins: The isomerization/switch/transfer (IST) model. Biochemistry 36, 2-7
    • (1997) Biochemistry , vol.36 , pp. 2-7
    • Haupts, U.1    Tittor, J.2    Bamberg, E.3    Oesterhelt, D.4
  • 19
    • 0015969754 scopus 로고
    • Reconstitution of purple membrane vesicles catalyzing light-driven proton uptake and adenosine triphosphate formation
    • Racker, E. and Stoeckenius, W. (1974) Reconstitution of purple membrane vesicles catalyzing light-driven proton uptake and adenosine triphosphate formation. J. Biol. Chem. 249, 662-663
    • (1974) J. Biol. Chem. , vol.249 , pp. 662-663
    • Racker, E.1    Stoeckenius, W.2
  • 20
    • 0017694434 scopus 로고
    • Two possible roles of bacteriorhodopsin; a comparative study of strains of Halobacterium halobium differing in pigmentation
    • Matsuno-Yagi, A. and Mukohata, Y. (1977) Two possible roles of bacteriorhodopsin; a comparative study of strains of Halobacterium halobium differing in pigmentation. Biochem. Biophys. Res. Commun. 78, 237-243
    • (1977) Biochem. Biophys. Res. Commun. , vol.78 , pp. 237-243
    • Matsuno-Yagi, A.1    Mukohata, Y.2
  • 21
    • 0018834616 scopus 로고
    • ATP synthesis linked to light-dependent proton uptake in a red mutant of Halobacterium lacking bacteriorhodopsin
    • Matsuno-Yagi, A. and Mukohata, Y. (1980) ATP synthesis linked to light-dependent proton uptake in a red mutant 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
  • 22
    • 0021319996 scopus 로고
    • Bacterio-opsin mRNA in wild-type and bacterio-opsin-deficient Halobacterium halobium strains
    • DasSarma, S., RajBhandary, U., and Khorana, H.G. (1984) Bacterio-opsin mRNA in wild-type and bacterio-opsin-deficient Halobacterium halobium strains. Proc. Natl. Acad. Sci. USA 81, 125-129
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 125-129
    • DasSarma, S.1    RajBhandary, U.2    Khorana, H.G.3
  • 23
    • 0022658302 scopus 로고
    • ATP synthesis in cell envelope vesicles of Halobacterium halobium driven by membrane potential and/or base-acid transition
    • Mukohata, Y., Isoyama, M., and Fuke, A. (1986) ATP synthesis in cell envelope vesicles of Halobacterium halobium driven by membrane potential and/or base-acid transition. J. Biochem. 99, 1-8
    • (1986) J. Biochem. , vol.99 , pp. 1-8
    • Mukohata, Y.1    Isoyama, M.2    Fuke, A.3
  • 24
    • 0043217193 scopus 로고
    • Photophosphorylation in Halobacterium halobium
    • Danon, A. and Stoeckenius, W. (1974) Photophosphorylation in Halobacterium halobium. Proc. Natl. Acad. Sci. USA 71, 1234-1238
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 1234-1238
    • Danon, A.1    Stoeckenius, W.2
  • 25
    • 84912298248 scopus 로고
    • Light-induced proton uptake and ATP synthesis by bacteriorhodopsin-depleted Halobacterium
    • Morishita, H. and Masui, M., eds., Business Centr. Acad. Soc. Japan, Tokyo
    • Mukohata, Y., Matsuno-Yagi, A., and Kaji, Y. (1980) Light-induced proton uptake and ATP synthesis by bacteriorhodopsin-depleted Halobacterium in Saline Environment (Morishita, H. and Masui, M., eds.) pp. 31-37, Business Centr. Acad. Soc. Japan, Tokyo
    • (1980) Saline Environment , pp. 31-37
    • Mukohata, Y.1    Matsuno-Yagi, A.2    Kaji, Y.3
  • 26
    • 0019477123 scopus 로고
    • Light-induced membrane potential increase, ATP synthesis and proton uptake in Halobacterium halobium R1mR catalysed by halorhodopsin; effects of N,N′-dicyclohexylcarbodiimide, triphenyltin chloride and 3,5-di-tert-butyl-4-hydroxybenzylydene-malononitrile (SF6847)
    • Mukohata, Y. and Kaji, Y. (1981) Light-induced membrane potential increase, ATP synthesis and proton uptake in Halobacterium halobium R1mR catalysed by halorhodopsin; effects of N,N′-dicyclohexylcarbodiimide, triphenyltin chloride and 3,5-di-tert-butyl-4-hydroxybenzylydene-malononitrile (SF6847). Arch. Biochem. Biophys. 206, 72-76
    • (1981) Arch. Biochem. Biophys. , vol.206 , pp. 72-76
    • Mukohata, Y.1    Kaji, Y.2
  • 27
    • 0018787587 scopus 로고
    • Proton movements in response to a light-driven electrogenic pump for sodium ions in Halobacterium halobium membranes
    • Greene, R.V. and Lanyi, J.K. (1979) Proton movements in response to a light-driven electrogenic pump for sodium ions in Halobacterium halobium membranes. J. Biol. Chem. 254, 10986-10994
    • (1979) J. Biol. Chem. , vol.254 , pp. 10986-10994
    • Greene, R.V.1    Lanyi, J.K.2
  • 28
    • 0018644949 scopus 로고
    • Characterization of the light-driven sodium pump of Halobacterium halobium
    • MacDonald, R., Greene, R.V., Clark, R.D., and Lindley, E.V. (1979) Characterization of the light-driven sodium pump of Halobacterium halobium. J. Biol. Chem. 254, 11831-11838
    • (1979) J. Biol. Chem. , vol.254 , pp. 11831-11838
    • MacDonald, R.1    Greene, R.V.2    Clark, R.D.3    Lindley, E.V.4
  • 29
    • 0020479529 scopus 로고
    • Halorhodopsin is a light-driven chloride pump
    • Shobert, B. and Lanyi, J.K. (1981) Halorhodopsin is a light-driven chloride pump. J. Biol. Chem. 257, 10306-10313
    • (1981) J. Biol. Chem. , vol.257 , pp. 10306-10313
    • Shobert, B.1    Lanyi, J.K.2
  • 30
    • 0344932378 scopus 로고
    • The ATP synthase in extremely halophilic archaebacteria and its relatives
    • Mukohata, Y., ed., Academic Press, Tokyo
    • Mukohata, Y., Ihara, K., Yoshida, M., and Sugiyama, Y. (1991) The ATP synthase in extremely halophilic archaebacteria and its relatives in New Era of Bioenergetics (Mukohata, Y., ed.) pp. 169-196, Academic Press, Tokyo
    • (1991) New Era of Bioenergetics , pp. 169-196
    • Mukohata, Y.1    Ihara, K.2    Yoshida, M.3    Sugiyama, Y.4
  • 31
    • 0020841103 scopus 로고
    • Photochemistry of two-rhodopsinlike pigments in bacteriorhodopsin-free mutant of Halobacterium halobium
    • Hazemoto, N., Kamo, N., Terayama, Y., Kobatake, Y., and Tsuda, M. (1983) Photochemistry of two-rhodopsinlike 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
  • 33
    • 0000373165 scopus 로고
    • Identification of a third rhodopsin-like pigment in phototactic Halobacterium halobium
    • Bogomolni, R. and Spudich, J.L. (1982) Identification of a third rhodopsin-like pigment in phototactic Halobacterium halobium. Proc. Natl. Acad. Sci. USA 79, 6250-6254
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6250-6254
    • Bogomolni, R.1    Spudich, J.L.2
  • 34
    • 0016842838 scopus 로고
    • Two photosystems controlling behavioural responses of Halobacterium halobium
    • Hildebrandt, E. and Dencher, N. (1975) Two photosystems controlling behavioural responses of Halobacterium halobium. Nature 257, 46-48
    • (1975) Nature , vol.257 , pp. 46-48
    • Hildebrandt, E.1    Dencher, N.2
  • 35
    • 0021873222 scopus 로고
    • A photosystem other than PS370 also mediates the negative phototaxis of Halobacterium halobium
    • Takahashi, T., Tomioka, H., Kamo, N., and Kobatake, Y. (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
  • 36
    • 0022790908 scopus 로고
    • Color discrimination in halobacteria: Spectroscopic characterization of a second sensory receptor covering the blue-green region of the spectrum
    • Wolff, E.K., Bogomolni, R.A., Scherrer, P., Hess, B., and Stoeckenius, W. (1986) Color discrimination in halobacteria: spectroscopic characterization of a second sensory receptor covering the blue-green region of the spectrum. Proc. Natl. Acad. Sci. USA 83, 7272-7276
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7272-7276
    • Wolff, E.K.1    Bogomolni, R.A.2    Scherrer, P.3    Hess, B.4    Stoeckenius, W.5
  • 37
    • 0023926733 scopus 로고
    • An Australian halobacterium contains a novel proton pump retinal protein: Archaerhodopsin
    • Mukohata, Y., Sugiyama, Y., Ihara, K., and Yoshida, M. (1988) An Australian halobacterium contains a novel proton pump retinal protein: Archaerhodopsin. Biochem. Biophys. Res. Commun. 151, 1339-1345
    • (1988) Biochem. Biophys. Res. Commun. , vol.151 , pp. 1339-1345
    • Mukohata, Y.1    Sugiyama, Y.2    Ihara, K.3    Yoshida, M.4
  • 38
    • 0024849644 scopus 로고
    • Isolation of a gene that encodes a new retinal protein, archaerhodopsin, from Halobacterium sp. aus-1
    • Sugiyama, Y., Maeda, M., Futai, M., and Mukohata, Y. (1989) Isolation of a gene that encodes a new retinal protein, archaerhodopsin, from Halobacterium sp. aus-1. J. Biol. Chem. 264, 20859-20862
    • (1989) J. Biol. Chem. , vol.264 , pp. 20859-20862
    • Sugiyama, Y.1    Maeda, M.2    Futai, M.3    Mukohata, Y.4
  • 39
    • 0025157188 scopus 로고
    • The primary structure of a halorhodopsin from Natronobacterium pharaonis. Structural, functional and evolutionary implications for bacterial rhodopsins and halorhodopsins
    • Lanyi, J.K., Duschl, A., Hatfield, G.W., May, K., and Oesterhelt, D. (1990) The primary structure of a halorhodopsin from Natronobacterium pharaonis. Structural, functional and evolutionary implications for bacterial rhodopsins and halorhodopsins. J. Biol. Chem. 265, 1253-1260
    • (1990) J. Biol. Chem. , vol.265 , pp. 1253-1260
    • Lanyi, J.K.1    Duschl, A.2    Hatfield, G.W.3    May, K.4    Oesterhelt, D.5
  • 40
    • 0026563018 scopus 로고
    • Bacterial rhodopsins of newly isolated halobacteria
    • Otomo, J., Tomioka, H., and Sasabe, H. (1992) Bacterial rhodopsins of newly isolated halobacteria. J. Gen. Microbiol. 138, 1027-1037
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1027-1037
    • Otomo, J.1    Tomioka, H.2    Sasabe, H.3
  • 41
    • 0031022623 scopus 로고    scopus 로고
    • Haloarcula argentinensis sp. nov. and Haloarcula mukohataei sp. nov., two new extremely halophilic archaea collected in Argentina
    • Ihara, K., Watanabe, S., and Tamura, T. (1997) Haloarcula argentinensis sp. nov. and Haloarcula mukohataei sp. nov., two new extremely halophilic archaea collected in Argentina. Int. J. Syst. Bacteriol. 47, 73-77
    • (1997) Int. J. Syst. Bacteriol. , vol.47 , pp. 73-77
    • Ihara, K.1    Watanabe, S.2    Tamura, T.3
  • 42
    • 0027995550 scopus 로고
    • The novel ion pump rhodopsins from both the bacteriorhodopsin and archaerhodopsin families/tribes
    • Tateno, M., Ihara, K., and Mukohata, Y. (1994) The novel ion pump rhodopsins from both the bacteriorhodopsin and archaerhodopsin families/tribes. Arch. Biochem. Biophys. 315, 127-132
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 127-132
    • Tateno, M.1    Ihara, K.2    Mukohata, Y.3
  • 44
    • 0028204916 scopus 로고
    • Comparative studies on ion pumps of the bacterial rhodopsin family
    • Mukohata, Y. (1994) Comparative studies on ion pumps of the bacterial rhodopsin family. Biophys. Chem. 50, 191-201
    • (1994) Biophys. Chem. , vol.50 , pp. 191-201
    • Mukohata, Y.1
  • 45
    • 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
  • 46
    • 0029894473 scopus 로고    scopus 로고
    • Influence exercised by histidine-95 on chloride transport and the photocycle in halorhodopsin
    • Otomo, J. (1996) Influence exercised by histidine-95 on chloride transport and the photocycle in halorhodopsin. Biochemistry 35, 6684-6689
    • (1996) Biochemistry , vol.35 , pp. 6684-6689
    • Otomo, J.1
  • 47
    • 0025856631 scopus 로고
    • Archaerhodopsin-2, from Halobacterium sp. aus-2 further reveals essential amino acid residues for light-driven proton pumps
    • Uegaki, K., Sugiyama, Y., and Mukohata, Y. (1991) Archaerhodopsin-2, from Halobacterium sp. aus-2 further reveals essential amino acid residues for light-driven proton pumps. Arch. Biochem. Biophys. 286, 107-110
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 107-110
    • Uegaki, K.1    Sugiyama, Y.2    Mukohata, Y.3
  • 48
    • 84908825648 scopus 로고
    • Comparative studies on bacteriorhodopsin-type pumps: Basic physicochemical data for proton pumps
    • Structures and Functions of Retinal Proteins (Rigaud, J.L., ed.), John Libbey Eurotext, Montrouge, France
    • Mukohata, Y., Ihara, K., Miyashita, Y., Amemiya, T., Taguchi, T., Tateno, M., and Sugiyama, Y. (1992) Comparative studies on bacteriorhodopsin-type pumps: basic physicochemical data for proton pumps in Structures and Functions of Retinal Proteins (Rigaud, J.L., ed.) Colloque INSERM (1992) 221, 101-104, John Libbey Eurotext, Montrouge, France
    • (1992) Colloque INSERM (1992) , vol.221 , pp. 101-104
    • Mukohata, Y.1    Ihara, K.2    Miyashita, Y.3    Amemiya, T.4    Taguchi, T.5    Tateno, M.6    Sugiyama, Y.7
  • 49
    • 0028016119 scopus 로고
    • Met-145 is a key residue in the dark adaptation of bacteriorhodopsin homologs
    • Ihara, K., Amemiya, T., Miyashita, Y., and Mukohata, Y. (1994) Met-145 is a key residue in the dark adaptation of bacteriorhodopsin homologs. Biophys. J. 67, 1187-1191
    • (1994) Biophys. J. , vol.67 , pp. 1187-1191
    • Ihara, K.1    Amemiya, T.2    Miyashita, Y.3    Mukohata, Y.4
  • 50
    • 0027218962 scopus 로고
    • Hydrophobic amino acids in the retinal-binding pocket of bacteriorhodopsin
    • Greenhalgh, D., Farrens, D.L., Subramaniam, S., and Khorana, G.H. (1993) Hydrophobic amino acids in the retinal-binding pocket of bacteriorhodopsin. J. Biol. Chem. 268, 20305-20311
    • (1993) J. Biol. Chem. , vol.268 , pp. 20305-20311
    • Greenhalgh, D.1    Farrens, D.L.2    Subramaniam, S.3    Khorana, G.H.4
  • 52
    • 0029081802 scopus 로고
    • Transfer of Halobacterium saccharovorum, Halobacterium sodomense, Halobacterium trapanicum NRC34021 and Halobacterium lacusprofundi to the genus Halorubrum gen. nov., Halorubrum saccharovorum comb. nov., Halorubrum sodomense comb, nov., Halorubrum trapanicum comb. nov., and Halorubrum lacusprofundi comv. nov.
    • McGeity, T.J. and Grant, W.D. (1995) Transfer of Halobacterium saccharovorum, Halobacterium sodomense, Halobacterium trapanicum NRC34021 and Halobacterium lacusprofundi to the genus Halorubrum gen. nov., Halorubrum saccharovorum comb. nov., Halorubrum sodomense comb, nov., Halorubrum trapanicum comb. nov., and Halorubrum lacusprofundi comv. nov. Syst. Appl. Microbiol. 18, 237-243
    • (1995) Syst. Appl. Microbiol. , vol.18 , pp. 237-243
    • McGeity, T.J.1    Grant, W.D.2
  • 54
    • 0027080728 scopus 로고
    • Primary structure of an archaebacterial transducer, a methyl-accepting protein associated with sensory rhodopsin I
    • Yao, V.J. and Spudich, J.L. (1992) Primary structure of an archaebacterial transducer, a methyl-accepting protein associated with sensory rhodopsin I. Proc. Natl. Acad. Sci. USA 89, 11915-11919
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11915-11919
    • Yao, V.J.1    Spudich, J.L.2
  • 55
    • 0028962369 scopus 로고
    • Chemotaxis and phototaxis require a Che histidine kinase in the archaeon Halobacterium salinarium
    • Rudolph, J. and Oesterhelt, D. (1995) Chemotaxis and phototaxis require a Che histidine kinase in the archaeon Halobacterium salinarium. EMBO J. 14, 667-673
    • (1995) EMBO J. , vol.14 , pp. 667-673
    • Rudolph, J.1    Oesterhelt, D.2
  • 56
    • 0000205409 scopus 로고
    • Signal transduction in bacterial chemotaxis
    • Spudich, J.L. and Saitir, B.H., eds., Wiley-Liss, New York
    • Eisenbach, M. (1991) Signal transduction in bacterial chemotaxis in Sensory Receptors and Signal Transduction (Spudich, J.L. and Saitir, B.H., eds.) pp. 137-208, Wiley-Liss, New York
    • (1991) Sensory Receptors and Signal Transduction , pp. 137-208
    • Eisenbach, M.1
  • 57
    • 0029758830 scopus 로고    scopus 로고
    • The primary structures of the Archaeon Halobacterium salinalium blue light receptor sensory rhodopsin II and its transducer, a methyl-accepting protein
    • Zhang, W., Brooun, A., Mueller, M.M., and Alam, M. (1996) The primary structures of the Archaeon Halobacterium salinalium blue light receptor sensory rhodopsin II and its transducer, a methyl-accepting protein. Proc. Natl. Acad. Sci. USA 93, 8230-8235
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8230-8235
    • Zhang, W.1    Brooun, A.2    Mueller, M.M.3    Alam, M.4
  • 58
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.