메뉴 건너뛰기




Volumn 5, Issue 1, 2001, Pages 61-69

Random sequence analysis of genomic DNA of an anaerobic, thermophilic, halophilic bacterium, Halothermothrix orenii

Author keywords

Codon bias; Genomic sequence; Halophile; Halothermothrix orenii; Sucrose phosphate synthase; Thermophile; V ATPase

Indexed keywords

AMINO ACID; GLUCOSYLTRANSFERASE; HYDROGENASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SODIUM CHLORIDE; SUCROSE PHOSPHATE SYNTHASE; SUCROSE-PHOSPHATE SYNTHASE;

EID: 0035259225     PISSN: 14310651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s007920000174     Document Type: Article
Times cited : (28)

References (26)
  • 2
    • 0029994972 scopus 로고    scopus 로고
    • Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: Enzyme purification, characterisation and N-terminal sequence
    • Bonete MJ, Pire C, Lorca FI, Comacho ML (1996) Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: enzyme purification, characterisation and N-terminal sequence. FEBS Lett 383(3):227-229
    • (1996) FEBS Lett , vol.383 , Issue.3 , pp. 227-229
    • Bonete, M.J.1    Pire, C.2    Lorca, F.I.3    Comacho, M.L.4
  • 3
    • 0028810373 scopus 로고
    • Isocitrate dehydrogenases from Haloferax volcanii and Sulfulobus solfataricus: Enzyme purification, characterisation and N-terminal sequence
    • Camacho ML, Brown RA, Bonete MJ, Danson MJ, Hough DW (1995) Isocitrate dehydrogenases from Haloferax volcanii and Sulfulobus solfataricus: enzyme purification, characterisation and N-terminal sequence. FEMS Microbiol Lett 134(1):85-90
    • (1995) FEMS Microbiol Lett , vol.134 , Issue.1 , pp. 85-90
    • Camacho, M.L.1    Brown, R.A.2    Bonete, M.J.3    Danson, M.J.4    Hough, D.W.5
  • 4
    • 0028322130 scopus 로고
    • Isolation and characterization of Halothermothrix orenii gen. nov., sp. nov., a halophilic, thermophilic, fermentative, strictly anaerobic bacterium
    • Cayol JL, Ollivier B, Patel BKC, Prensier G, Guezennec J, Garcia JL (1994) Isolation and characterization of Halothermothrix orenii gen. nov., sp. nov., a halophilic, thermophilic, fermentative, strictly anaerobic bacterium. Int J Syst Bacteriol 44(3):534-540
    • (1994) Int J Syst Bacteriol , vol.44 , Issue.3 , pp. 534-540
    • Cayol, J.L.1    Ollivier, B.2    Patel, B.K.C.3    Prensier, G.4    Guezennec, J.5    Garcia, J.L.6
  • 5
    • 0034105986 scopus 로고    scopus 로고
    • Thermohalobacter berrensis gen. nov., sp. nov., a thermophilic, strictly halophilic bacterium from a solar saltern
    • Cayol JL, Ducerf S, Patel BK, Garcia JL, Thomas P, Ollivier B (2000) Thermohalobacter berrensis gen. nov., sp. nov., a thermophilic, strictly halophilic bacterium from a solar saltern. Int J Syst Evol Microbiol 50(pt 2):559-564
    • (2000) Int J Syst Evol Microbiol , vol.50 , Issue.2 PART , pp. 559-564
    • Cayol, J.L.1    Ducerf, S.2    Patel, B.K.3    Garcia, J.L.4    Thomas, P.5    Ollivier, B.6
  • 6
    • 0032440388 scopus 로고    scopus 로고
    • Sucrose-phosphate synthase from Synechocystis sp. strain PCC 6803: Identification of the spsA gene and characterisation of the enzyme expressed in Escherichia coli
    • Curatti L, Folco E, Desplats P, Abratti G, Limones V, Herrera-Estrella L, Salerno G (1998) Sucrose-phosphate synthase from Synechocystis sp. strain PCC 6803: identification of the spsA gene and characterisation of the enzyme expressed in Escherichia coli. J Bacteriol 180(24):6776-6779
    • (1998) J Bacteriol , vol.180 , Issue.24 , pp. 6776-6779
    • Curatti, L.1    Folco, E.2    Desplats, P.3    Abratti, G.4    Limones, V.5    Herrera-Estrella, L.6    Salerno, G.7
  • 7
    • 0033135158 scopus 로고    scopus 로고
    • The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center
    • Garcin E, Vernede X, Hatchikian EC, Volbeda A, Frey M, Fontecilla-Camps JC (1999) The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Struct Fold Des 7(5):557-566
    • (1999) Struct Fold des , vol.7 , Issue.5 , pp. 557-566
    • Garcin, E.1    Vernede, X.2    Hatchikian, E.C.3    Volbeda, A.4    Frey, M.5    Fontecilla-Camps, J.C.6
  • 8
    • 0024792641 scopus 로고
    • MacConkey agar as an alternative to X-gal in the detection of recombinant plasmids
    • Jennings MP, Beacham IR (1989) MacConkey agar as an alternative to X-gal in the detection of recombinant plasmids. Biotechniques 7(10):1082
    • (1989) Biotechniques , vol.7 , Issue.10 , pp. 1082
    • Jennings, M.P.1    Beacham, I.R.2
  • 9
    • 0032190206 scopus 로고    scopus 로고
    • + stimulated V-type ATPase in the membrane of a facultatively anaerobic and halophilic alkaliphile
    • + stimulated V-type ATPase in the membrane of a facultatively anaerobic and halophilic alkaliphile. FEMS Microbiol Lett 167:57-61
    • (1998) FEMS Microbiol Lett , vol.167 , pp. 57-61
    • Kaieda, N.1    Wakagi, T.2    Koyama, N.3
  • 10
    • 0017388369 scopus 로고
    • Thermophilic character of enzymes from extreme halophilic bacteria
    • Keradjopoulos D, Holldorf AW (1977) Thermophilic character of enzymes from extreme halophilic bacteria. FEMS Microbiol Lett 1:179-182
    • (1977) FEMS Microbiol Lett , vol.1 , pp. 179-182
    • Keradjopoulos, D.1    Holldorf, A.W.2
  • 12
    • 0016139829 scopus 로고
    • Salt dependent properties of proteins from extremely halophilic bacteria
    • Lanyi JK (1974) Salt dependent properties of proteins from extremely halophilic bacteria. Bacteriol Rev 38(3):272-290
    • (1974) Bacteriol Rev , vol.38 , Issue.3 , pp. 272-290
    • Lanyi, J.K.1
  • 13
    • 0033136352 scopus 로고    scopus 로고
    • Cloning and expression of a prokaryotic sucrose-phosphate synthase gene from the cyanobacterium Synechocystis sp. PCC 6803
    • Lunn JE, Price GD, Furbank RT (1999) Cloning and expression of a prokaryotic sucrose-phosphate synthase gene from the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol Biol 40:297-305
    • (1999) Plant Mol Biol , vol.40 , pp. 297-305
    • Lunn, J.E.1    Price, G.D.2    Furbank, R.T.3
  • 14
  • 15
    • 0033152499 scopus 로고    scopus 로고
    • Thermophilic and halophilic extremophiles
    • Madigan MT, Oren A (1999) Thermophilic and halophilic extremophiles. Curr Opin Microbiol 2:265-269
    • (1999) Curr Opin Microbiol , vol.2 , pp. 265-269
    • Madigan, M.T.1    Oren, A.2
  • 16
    • 0023433415 scopus 로고
    • The primary structure of the ribosomal A-protein (L12) from the halophilic eubacterium Haloanaerobium praevalens
    • Matheson AT, Louie KA, Tak BD, Zuker M (1987) The primary structure of the ribosomal A-protein (L12) from the halophilic eubacterium Haloanaerobium praevalens. Biochimie (Paris) 69(10):1013-1020
    • (1987) Biochimie (Paris) , vol.69 , Issue.10 , pp. 1013-1020
    • Matheson, A.T.1    Louie, K.A.2    Tak, B.D.3    Zuker, M.4
  • 17
    • 0022590625 scopus 로고
    • Intracellular salt concentrations of the anaerobic halophilic eubacteria Haloanaerobium praevalens and Halobacteroides halobious
    • Oren A (1986) Intracellular salt concentrations of the anaerobic halophilic eubacteria Haloanaerobium praevalens and Halobacteroides halobious. Can J Microbiol 32:4-9
    • (1986) Can J Microbiol , vol.32 , pp. 4-9
    • Oren, A.1
  • 18
    • 0021906874 scopus 로고
    • Fervidobacterium nodosum gen. nov., a new chemoorganotrophic caldoactive anaerobic bacterium
    • Patel BKC, Morgan HW, Daniel RM (1985a) Fervidobacterium nodosum gen. nov., a new chemoorganotrophic caldoactive anaerobic bacterium. Arch Microbiol 14:63-69
    • (1985) Arch Microbiol , vol.14 , pp. 63-69
    • Patel, B.K.C.1    Morgan, H.W.2    Daniel, R.M.3
  • 19
    • 0001307475 scopus 로고
    • A simple and efficient method for preparing anaerobic media
    • Patel BKC, Morgan HW, Daniel RM (1985b) A simple and efficient method for preparing anaerobic media. Biotechnol Lett 7:227-228
    • (1985) Biotechnol Lett , vol.7 , pp. 227-228
    • Patel, B.K.C.1    Morgan, H.W.2    Daniel, R.M.3
  • 20
    • 0024044384 scopus 로고
    • Effect of extreme salt concentrations on the physiology and biochemistry of Halobacteroides acetoethylicus
    • Rengpipat S, Lowe SE, Zeikus JG (1988) Effect of extreme salt concentrations on the physiology and biochemistry of Halobacteroides acetoethylicus. J Bacteriol 170(7):3065-3071
    • (1988) J Bacteriol , vol.170 , Issue.7 , pp. 3065-3071
    • Rengpipat, S.1    Lowe, S.E.2    Zeikus, J.G.3
  • 22
    • 0031578224 scopus 로고    scopus 로고
    • The stabilising residues and the functional domains in the hyperthermophilic V-ATPase of Desulfurococcus
    • Shibui H, Hamamoto T, Yohda M, Kagawa Y (1997) The stabilising residues and the functional domains in the hyperthermophilic V-ATPase of Desulfurococcus. Biochem Biophys Res Commun 234:341-345
    • (1997) Biochem Biophys Res Commun , vol.234 , pp. 341-345
    • Shibui, H.1    Hamamoto, T.2    Yohda, M.3    Kagawa, Y.4
  • 24
    • 0026039536 scopus 로고
    • Molecular cloning of the genes encoding the major two subunits of a eubacterial V-type ATPase from Thermus thermophilis
    • Tsutsumi S, Denda K, Yokoyama K, Oshima T, Date T, Yoshida M (1991) Molecular cloning of the genes encoding the major two subunits of a eubacterial V-type ATPase from Thermus thermophilis. Biochim Biophys Acta 1098:13-20
    • (1991) Biochim Biophys Acta , vol.1098 , pp. 13-20
    • Tsutsumi, S.1    Denda, K.2    Yokoyama, K.3    Oshima, T.4    Date, T.5    Yoshida, M.6
  • 25
    • 0032799575 scopus 로고    scopus 로고
    • The hyperthermophilic bacterium, Thermotoga maritima, contains an unusually complex iron-hydrogenase: Amino acid sequence analyses versus biochemical characterization
    • Verhagen MF, O'Rourke T, Adams MW (1999) The hyperthermophilic bacterium, Thermotoga maritima, contains an unusually complex iron-hydrogenase: amino acid sequence analyses versus biochemical characterization. Biochim Biophys Acta 1412(3):212-229
    • (1999) Biochim Biophys Acta , vol.1412 , Issue.3 , pp. 212-229
    • Verhagen, M.F.1    O'Rourke, T.2    Adams, M.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.