메뉴 건너뛰기




Volumn 55, Issue 6, 2005, Pages 1681-1694

MpcT is the transducer for membrane potential changes in Halobacterium salinarum

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; BIOLOGICAL RESPONSE MODIFIER; HALORHODOPSIN;

EID: 13844257635     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2005.04516.x     Document Type: Article
Times cited : (40)

References (41)
  • 1
    • 0024618364 scopus 로고
    • Methyl-accepting taxis proteins in Halobacterium halobium
    • Alam, M., Lebert, M., Oesterhelt, D., and Hazelbauer, G. (1989) Methyl-accepting taxis proteins in Halobacterium halobium. EMBO J 8: 631-639.
    • (1989) EMBO J , vol.8 , pp. 631-639
    • Alam, M.1    Lebert, M.2    Oesterhelt, D.3    Hazelbauer, G.4
  • 3
    • 0026348180 scopus 로고
    • The proton pump bacteriorhodopsin is a photoreceptor for signal transduction in Halobacterium halobium
    • Bibikov, S.I., Grishanin, R.N., Marwan, W., Oesterhelt, D., and Skulachev, V.P. (1991) The proton pump bacteriorhodopsin is a photoreceptor for signal transduction in Halobacterium halobium. FEBS Lett 295: 223-226.
    • (1991) FEBS Lett , vol.295 , pp. 223-226
    • Bibikov, S.I.1    Grishanin, R.N.2    Marwan, W.3    Oesterhelt, D.4    Skulachev, V.P.5
  • 5
    • 0026502186 scopus 로고
    • Bacillus subtilis chemotaxis - A deviation from the Escherichia coli paradigm
    • Bischoff, D.S., and Ordal, G.W. (1992) Bacillus subtilis chemotaxis - a deviation from the Escherichia coli paradigm. Mol Microbiol 6: 23-28.
    • (1992) Mol Microbiol , vol.6 , pp. 23-28
    • Bischoff, D.S.1    Ordal, G.W.2
  • 6
    • 0018926910 scopus 로고
    • Multiple electrophoretic forms of methyl-accepting chemotaxis proteins generated by stimulus-elicited methylation in Escherichia coli
    • Boyd, A., and Simon, M.I. (1980) Multiple electrophoretic forms of methyl-accepting chemotaxis proteins generated by stimulus-elicited methylation in Escherichia coli. J Bacteriol 143: 809-815.
    • (1980) J Bacteriol , vol.143 , pp. 809-815
    • Boyd, A.1    Simon, M.I.2
  • 7
    • 0030903470 scopus 로고    scopus 로고
    • Primary structure and functional analysis of the soluble transducer protein HtrXI in the archaeon Halobacterium salinarium
    • Brooun, A., Zhang, W., and Alam, M. (1997) Primary structure and functional analysis of the soluble transducer protein HtrXI in the archaeon Halobacterium salinarium. J Bacteriol 179: 2963-2968.
    • (1997) J Bacteriol , vol.179 , pp. 2963-2968
    • Brooun, A.1    Zhang, W.2    Alam, M.3
  • 8
    • 0031944976 scopus 로고    scopus 로고
    • An archaeal aerotaxis transducer combines subunit I core structures of eukaryotic cytochrome c oxidase and eubacterial methyl-accepting chemotaxis proteins
    • Brooun, A., Bell, J., Freitas, T., Larsen, R.W., and Alam, M. (1998) An archaeal aerotaxis transducer combines subunit I core structures of eukaryotic cytochrome c oxidase and eubacterial methyl-accepting chemotaxis proteins. J Bacteriol 180: 1642-1646.
    • (1998) J Bacteriol , vol.180 , pp. 1642-1646
    • Brooun, A.1    Bell, J.2    Freitas, T.3    Larsen, R.W.4    Alam, M.5
  • 10
    • 0031929447 scopus 로고    scopus 로고
    • Sensory rhodopsin II transducer HtrII is also responsible for serine chemotaxis in the archaeon Halobacterium salinarum
    • Hou, S., Brooun, A., Yu, H.S., Freitas, T., and Alam, M. (1998) Sensory rhodopsin II transducer HtrII is also responsible for serine chemotaxis in the archaeon Halobacterium salinarum. J Bacteriol 180: 1600-1602.
    • (1998) J Bacteriol , vol.180 , pp. 1600-1602
    • Hou, S.1    Brooun, A.2    Yu, H.S.3    Freitas, T.4    Alam, M.5
  • 11
    • 0034598826 scopus 로고    scopus 로고
    • Myoglobin-like aerotaxis transducers in Archaea and Bacteria
    • Hou, S., Larsen, R.W., Boudko, D., Riley, C.W., Karatan, E., Zimmer, M., et al. (2000) Myoglobin-like aerotaxis transducers in Archaea and Bacteria. Nature 403: 540-544.
    • (2000) Nature , vol.403 , pp. 540-544
    • Hou, S.1    Larsen, R.W.2    Boudko, D.3    Riley, C.W.4    Karatan, E.5    Zimmer, M.6
  • 13
    • 0033982051 scopus 로고    scopus 로고
    • BasT, a membrane-bound transducer protein for amino acid detection in Halobacterium salinarum
    • Kokoeva, M.V., and Oesterhelt, D. (2000) BasT, a membrane-bound transducer protein for amino acid detection in Halobacterium salinarum. Mol Microbiol 35: 647-656.
    • (2000) Mol Microbiol , vol.35 , pp. 647-656
    • Kokoeva, M.V.1    Oesterhelt, D.2
  • 14
    • 0037093395 scopus 로고    scopus 로고
    • A novel mode of sensory transduction in archaea: Binding protein-mediated chemotaxis towards osmoprotectants and amino acids
    • Kokoeva, M.V., Storch, K.-F., Klein, C., and Oesterhelt, D. (2002) A novel mode of sensory transduction in archaea: binding protein-mediated chemotaxis towards osmoprotectants and amino acids. EMBO J 21: 2312-2322.
    • (2002) EMBO J , vol.21 , pp. 2312-2322
    • Kokoeva, M.V.1    Storch, K.-F.2    Klein, C.3    Oesterhelt, D.4
  • 15
    • 0025114033 scopus 로고
    • Quantitation of photochromism of sensory rhodopsin-I by computerized tracking of Halobacterium halobium cells
    • Marwan, W., and Oesterhelt, D. (1990) Quantitation of photochromism of sensory rhodopsin-I by computerized tracking of Halobacterium halobium cells. J Mol Biol 215: 277285.
    • (1990) J Mol Biol , vol.215 , pp. 277285
    • Marwan, W.1    Oesterhelt, D.2
  • 16
    • 0025782272 scopus 로고
    • Light-induced release of the switch factor during photophobic responses of Halobacterium halobium
    • Marwan, W., and Oesterhelt, D. (1991) Light-induced release of the switch factor during photophobic responses of Halobacterium halobium. Naturwissenschaften 78: 127-129.
    • (1991) Naturwissenschaften , vol.78 , pp. 127-129
    • Marwan, W.1    Oesterhelt, D.2
  • 17
    • 0017195595 scopus 로고
    • Light-induced changes of the pH gradient and the membrane potential in H. halobium
    • Michel, H., and Oesterhelt, D. (1976) Light-induced changes of the pH gradient and the membrane potential in H. halobium. FEBS Lett 65: 175-178.
    • (1976) FEBS Lett , vol.65 , pp. 175-178
    • Michel, H.1    Oesterhelt, D.2
  • 18
    • 0019163814 scopus 로고
    • Electrochemical proton gradient across the cell-membrane of Halobacterium halobium: Effect of N,N′-dicyclohexylcarbodiimide, relation to intracellular adenosine-triphosphate, adenosine-diphosphate, and phosphate concentration, and influence of the potassium gradient
    • Michel, H., and Oesterhelt, D. (1980) Electrochemical proton gradient across the cell-membrane of Halobacterium halobium: effect of N,N′-dicyclohexylcarbodiimide, relation to intracellular adenosine-triphosphate, adenosine-diphosphate, and phosphate concentration, and influence of the potassium gradient. Biochemistry 19: 4607-4614.
    • (1980) Biochemistry , vol.19 , pp. 4607-4614
    • Michel, H.1    Oesterhelt, D.2
  • 19
    • 0026034427 scopus 로고
    • Arginine deiminase from Halobacterium salinarium - Purification and properties
    • Monstadt, G.M., and Holldorf, A.W. (1991) Arginine deiminase from Halobacterium salinarium - purification and properties. Biochem J 273: 739-745.
    • (1991) Biochem J , vol.273 , pp. 739-745
    • Monstadt, G.M.1    Holldorf, A.W.2
  • 20
    • 0019564647 scopus 로고
    • Light-induced ATP synthesis dependent on halorhodopsin-pH regulation
    • Mukohata, Y., and Kaji, Y. (1981) Light-induced ATP synthesis dependent on halorhodopsin-pH regulation. Arch Biochem Biophys 208: 615-617.
    • (1981) Arch Biochem Biophys , vol.208 , pp. 615-617
    • Mukohata, Y.1    Kaji, Y.2
  • 22
    • 0023644784 scopus 로고
    • Sites of covalent modification in Trg, a sensory transducer of Escherichia coli
    • Nowlin, D., Bollinger, J., and Hazelbauer, G. (1987) Sites of covalent modification in Trg, a sensory transducer of Escherichia coli. J Biol Chem 262: 6039-6045.
    • (1987) J Biol Chem , vol.262 , pp. 6039-6045
    • Nowlin, D.1    Bollinger, J.2    Hazelbauer, G.3
  • 23
    • 0032144042 scopus 로고    scopus 로고
    • The structure and mechanism of the family of retinal proteins from halophilic archaea
    • Oesterhelt, D. (1998) The structure and mechanism of the family of retinal proteins from halophilic archaea. Curr Opin Struct Biol 8: 489-500.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 489-500
    • Oesterhelt, D.1
  • 24
    • 0015908026 scopus 로고
    • Light inhibition of respiration in Halobacterium halobium
    • Oesterhelt, D., and Krippahl, G. (1973) Light inhibition of respiration in Halobacterium halobium. FEBS Lett 36: 72-76.
    • (1973) FEBS Lett , vol.36 , pp. 72-76
    • Oesterhelt, D.1    Krippahl, G.2
  • 25
    • 0020792146 scopus 로고
    • Phototropic growth of halobacteria and its use for isolation of photosynthetically-deficient mutants
    • Oesterhelt, D., and Krippahl, G. (1983) Phototropic growth of halobacteria and its use for isolation of photosynthetically-deficient mutants. Ann Microbiol (Inst Pasteur) 134B: 137-150.
    • (1983) Ann Microbiol (Inst Pasteur) , vol.134 B , pp. 137-150
    • Oesterhelt, D.1    Krippahl, G.2
  • 26
    • 0027954763 scopus 로고
    • The ecology of the extremely halophilic archaea
    • Oren, A. (1994) The ecology of the extremely halophilic archaea. FEMS Microbiol Rev 13: 415-439.
    • (1994) FEMS Microbiol Rev , vol.13 , pp. 415-439
    • Oren, A.1
  • 27
    • 0032853179 scopus 로고    scopus 로고
    • Identification of methylation sites and effects of phototaxis stimuli on transducer methylation in Halobacterium salinarum
    • Perazzona, B., and Spudich, J.L. (1999) Identification of methylation sites and effects of phototaxis stimuli on transducer methylation in Halobacterium salinarum. J Bacteriol 181: 5676-5683.
    • (1999) J Bacteriol , vol.181 , pp. 5676-5683
    • Perazzona, B.1    Spudich, J.L.2
  • 28
    • 19344376625 scopus 로고    scopus 로고
    • Design and diversity in bacterial chemotaxis: A comparative study in Escherichia coli and Bacillus subtilis
    • Rao, C.V., Kirby, J.R., and Arkin, A.P. (2004) Design and diversity in bacterial chemotaxis: a comparative study in Escherichia coli and Bacillus subtilis. PLoS Biol 2: 0239-0252.
    • (2004) PLoS Biol , vol.2 , pp. 0239-0252
    • Rao, C.V.1    Kirby, J.R.2    Arkin, A.P.3
  • 29
    • 0030883388 scopus 로고    scopus 로고
    • The Aer protein and the serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior
    • Rebbapragada, A., Johnson, M.S., Harding, G.P., Zuccarelli, A.J., Fletcher, H.M., Zhulin, I.B., and Taylor, B.L. (1997) The Aer protein and the serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior. Proc Natl Acad Sci USA 94: 10541-10546.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10541-10546
    • Rebbapragada, A.1    Johnson, M.S.2    Harding, G.P.3    Zuccarelli, A.J.4    Fletcher, H.M.5    Zhulin, I.B.6    Taylor, B.L.7
  • 30
    • 0342624740 scopus 로고    scopus 로고
    • Deletion analysis of the che operon in the archaeon Halobacterium salinarium
    • Rudolph, J., and Oesterhelt, D. (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
  • 32
    • 0029761908 scopus 로고    scopus 로고
    • Fermentative arginine degradation in Halobacterium salinarium (formerly Halobacterium halobium): Genes, gene products, and transcripts of the arcRACB gene cluster
    • Ruepp, A., and Soppa, J. (1996) Fermentative arginine degradation in Halobacterium salinarium (formerly Halobacterium halobium): genes, gene products, and transcripts of the arcRACB gene cluster. J Bacteriol 178: 4942-4947.
    • (1996) J Bacteriol , vol.178 , pp. 4942-4947
    • Ruepp, A.1    Soppa, J.2
  • 33
    • 0028965178 scopus 로고
    • The primary structure of sensory rhodopsin II: A member of an additional retinal protein subgroup is coexpressed with its transducer, the halobacterial transducer of rhodopsin II
    • Seidel, R., Scharf, B., Gautel, M., Kleine, K., Oesterhelt, D., and Engelhard, M. (1995) The primary structure of sensory rhodopsin II: a member of an additional retinal protein subgroup is coexpressed with its transducer, the halobacterial transducer of rhodopsin II. Proc Natl Acad Sci USA 92: 3036-3040.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3036-3040
    • Seidel, R.1    Scharf, B.2    Gautel, M.3    Kleine, K.4    Oesterhelt, D.5    Engelhard, M.6
  • 34
    • 0000621729 scopus 로고    scopus 로고
    • Chemotaxis
    • Neidhardt, R.C.I., Ingraham, J.L., Lin, E.G.C., Low, K.B., Magasanik, B., Reznikoff, W.S., et al., (eds). Washington, DC: American Society of Microbiology
    • Stock, J.B., and Surette, M.G. (1996) Chemotaxis. In Escherichia coli and Salmonella typhimurium: cellular and molecular biology. Vol. 1. Neidhardt, R.C.I., Ingraham, J.L., Lin, E.G.C., Low, K.B., Magasanik, B., Reznikoff, W.S., et al., (eds). Washington, DC: American Society of Microbiology, pp. 551-573.
    • (1996) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology , vol.1 , pp. 551-573
    • Stock, J.B.1    Surette, M.G.2
  • 35
    • 0033104510 scopus 로고    scopus 로고
    • Car: A cytoplasmic sensor responsible for arginine chemotaxis in Halobacterium salinarum
    • Storch, K.F., Rudolph, J., and Oesterhelt, D. (1999) Car: a cytoplasmic sensor responsible for arginine chemotaxis in Halobacterium salinarum. EMBO J 18: 1146-1158.
    • (1999) EMBO J , vol.18 , pp. 1146-1158
    • Storch, K.F.1    Rudolph, J.2    Oesterhelt, D.3
  • 36
    • 0032694979 scopus 로고    scopus 로고
    • Aerotaxis and other energy-sensing behaviour in bacteria
    • Taylor, B.L., Zhulin, I.B., and Johnson, M.S. (1999) Aerotaxis and other energy-sensing behaviour in bacteria. Annu Rev Microbiol 53: 103-128.
    • (1999) Annu Rev Microbiol , vol.53 , pp. 103-128
    • Taylor, B.L.1    Zhulin, I.B.2    Johnson, M.S.3
  • 37
    • 0017807533 scopus 로고
    • Potassium uniport and ATP synthesis in Halobacterium halobium
    • Wagner, G., Hartmann, R., and Oesterhelt, D. (1978) Potassium uniport and ATP synthesis in Halobacterium halobium. Eur J Biochem 89: 169-179.
    • (1978) Eur J Biochem , vol.89 , pp. 169-179
    • Wagner, G.1    Hartmann, R.2    Oesterhelt, D.3
  • 38
    • 0019847993 scopus 로고
    • Bioenergetic role of halorhodopsin in Halobacterium halobium cells
    • Wagner, G., Oesterhelt, D., Krippahl, G., and Lanyi, J.K. (1981) Bioenergetic role of halorhodopsin in Halobacterium halobium cells. FEBS Lett 131: 341-345.
    • (1981) FEBS Lett , vol.131 , pp. 341-345
    • Wagner, G.1    Oesterhelt, D.2    Krippahl, G.3    Lanyi, J.K.4
  • 39
    • 0035045569 scopus 로고    scopus 로고
    • Dissection of the functional and structural domains of phosphorelay histidine kinase A of Bacillus subtilis
    • Wang, L., Fabret, C., Kanamaru, K., Stephenson, K., Dartois, V., Perego, M., and Hoch, J.A. (2001) Dissection of the functional and structural domains of phosphorelay histidine kinase A of Bacillus subtilis. J Bacteriol 183: 2795-2802.
    • (2001) J Bacteriol , vol.183 , pp. 2795-2802
    • Wang, L.1    Fabret, C.2    Kanamaru, K.3    Stephenson, K.4    Dartois, V.5    Perego, M.6    Hoch, J.A.7
  • 40
    • 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
  • 41
    • 0029758830 scopus 로고    scopus 로고
    • The primary structures of the archaeon Halobacterium salinarium 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 salinarium 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.