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Volumn 21, Issue 1, 1998, Pages 12-22

F- and V-ATPases in the genus Thermus and related species

Author keywords

F ATPases; Horizontal gene transfer; Meiothermus chliarophilus; Prokaryotic evolution; Thermus aquaticus; Thermus filiformis; Thermus scotoductus; Thermus thermophilus; V ATPases

Indexed keywords

ADENOSINE TRIPHOSPHATASE; AZIDE; BACTERIAL ENZYME; ENZYME ANTIBODY; MEMBRANE ENZYME; NITRATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; RNA 16S;

EID: 0031953610     PISSN: 07232020     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0723-2020(98)80003-9     Document Type: Article
Times cited : (10)

References (68)
  • 1
    • 0023917654 scopus 로고
    • A malachite green procedure for orthophosphate determination and its use in alkaline phosphate-based enzyme immunoassay
    • BAYKOV, A. A., EVTUSHENKO, O. A., AVAEBA, S. M.: A malachite green procedure for orthophosphate determination and its use in alkaline phosphate-based enzyme immunoassay. Anal. Biochem. 171, 266-270 (1988).
    • (1988) Anal. Biochem. , vol.171 , pp. 266-270
    • Baykov, A.A.1    Evtushenko, O.A.2    Avaeba, S.M.3
  • 2
    • 0028181851 scopus 로고
    • 0-ATP synthase in membrane vesicles of the archaeon Methanosarcina mazei GÖ1
    • 0-ATP synthase in membrane vesicles of the archaeon Methanosarcina mazei GÖ1. J. Bacteriol. 176, 2543-2550 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 2543-2550
    • Becher, B.1    Müller, V.2
  • 3
    • 0018973343 scopus 로고
    • 2+-activated adenosine triphosphatase of Escherichia coli
    • 2+-activated adenosine triphosphatase of Escherichia coli. Eur. J. Biochem. 106, 495-503 (1980).
    • (1980) Eur. J. Biochem. , vol.106 , pp. 495-503
    • Bragg, P.D.1    Hou, C.2
  • 5
    • 0028239826 scopus 로고
    • Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen
    • CASTRESANA, J., LÜBBEN, M., SARASTE, M., HIGGINS, D. G.: Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen. EMBO J. 13, 2516-2525 (1994).
    • (1994) EMBO J. , vol.13 , pp. 2516-2525
    • Castresana, J.1    Lübben, M.2    Saraste, M.3    Higgins, D.G.4
  • 6
    • 0018306932 scopus 로고
    • The proton-translocating adenosine triphosphatase of the obligately anaerobic bacterium Clostridium pasteurianum. 1. ATP phosphohydrolase activity
    • CLARKE, D. J., FULLER, F. M., MORRIS, J. G.: The proton-translocating adenosine triphosphatase of the obligately anaerobic bacterium Clostridium pasteurianum. 1. ATP phosphohydrolase activity. Eur. J. Biochem. 98, 597-612 (1979).
    • (1979) Eur. J. Biochem. , vol.98 , pp. 597-612
    • Clarke, D.J.1    Fuller, F.M.2    Morris, J.G.3
  • 7
    • 0025117401 scopus 로고
    • 0 ATPases and synthases
    • 0 ATPases and synthases. FEBS Lett. 259, 227-229 (1990).
    • (1990) FEBS Lett. , vol.259 , pp. 227-229
    • Cross, R.L.1    Taiz, L.2
  • 10
    • 0001764602 scopus 로고
    • + transporting ATP synthases
    • Bacterial Energetics. (T. A. KRULWICH, ed.) San Diego, Academic Press
    • + transporting ATP synthases, pp. 345-391. In: Bacterial Energetics. (T. A. KRULWICH, ed.) The Bacteria, Vol. XII, San Diego, Academic Press 1990.
    • (1990) The Bacteria , vol.12 , pp. 345-391
    • Fillingame, R.H.1
  • 11
    • 0024389333 scopus 로고
    • Structure and function of vacuolar class of ATP-driven proton pumps
    • FORGAC, M.: Structure and function of vacuolar class of ATP-driven proton pumps. Physiol. Rev. 69, 765-796 (1989).
    • (1989) Physiol. Rev. , vol.69 , pp. 765-796
    • Forgac, M.1
  • 12
    • 0027056143 scopus 로고
    • The nature of the last universal ancestor and the root of the tree of life, still open questions
    • FORTERRE, P., BENACHENHOU-LAHFA, N., CONFALONIERI, F., DUGUET, M., ELIE, C., LABEDAN, B.: The nature of the last universal ancestor and the root of the tree of life, still open questions. BioSystems 28, 15-32 (1993).
    • (1993) BioSystems , vol.28 , pp. 15-32
    • Forterre, P.1    Benachenhou-Lahfa, N.2    Confalonieri, F.3    Duguet, M.4    Elie, C.5    Labedan, B.6
  • 14
    • 0020570950 scopus 로고
    • 1): Biochemical and molecular approaches
    • 1): Biochemical and molecular approaches. Microbiol. Rev. 47, 285-312 (1983).
    • (1983) Microbiol. Rev. , vol.47 , pp. 285-312
    • Futai, M.1    Kanazawa, H.2
  • 16
    • 0031281692 scopus 로고    scopus 로고
    • Western blot of stained proteins from dried polyacrylamide gels
    • GRUBER, C., STAN-LOTTER, H.: Western blot of stained proteins from dried polyacrylamide gels. Anal. Biochem. 253, 125-127 (1997).
    • (1997) Anal. Biochem. , vol.253 , pp. 125-127
    • Gruber, C.1    Stan-Lotter, H.2
  • 17
    • 0024287134 scopus 로고
    • Sequence of the genes for the β and ε subunits of the ATP synthase of Bacillus megaterium QM B1551
    • HAWTHORNE, C. A., BRUSILOW, W. S.: Sequence of the genes for the β and ε subunits of the ATP synthase of Bacillus megaterium QM B1551. Biochem. Biophys. Res. Commun. 151, 926-931 (1988).
    • (1988) Biochem. Biophys. Res. Commun. , vol.151 , pp. 926-931
    • Hawthorne, C.A.1    Brusilow, W.S.2
  • 18
    • 0027738868 scopus 로고
    • Horizontal transfer of ATPase genes - The tree of life becomes a net of life
    • HILARIO, E., GOGARTEN, J. P.: Horizontal transfer of ATPase genes - the tree of life becomes a net of life. BioSystems 31, 111-119 (1993).
    • (1993) BioSystems , vol.31 , pp. 111-119
    • Hilario, E.1    Gogarten, J.P.2
  • 21
    • 0025822726 scopus 로고
    • The ATP synthase of Halobacterium salinarium (halobium) is an archaebacterial type as revealed from the amino acid sequences of its two major subunits
    • IHARA, K., MUKOHATA, Y.: The ATP synthase of Halobacterium salinarium (halobium) is an archaebacterial type as revealed from the amino acid sequences of its two major subunits. Arch. Biochem. Biophys. 286, 111-116 (1991).
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 111-116
    • Ihara, K.1    Mukohata, Y.2
  • 22
    • 0022559027 scopus 로고
    • 1-ATPase from Clostridium thermoaceticum
    • 1-ATPase from Clostridium thermoaceticum. J. Bacteriol. 165, 252-257 (1986).
    • (1986) J. Bacteriol. , vol.165 , pp. 252-257
    • Ivey, D.M.1    Ljungdahl, L.G.2
  • 23
    • 0025991196 scopus 로고
    • Organization and nucleotide sequence of the atp genes encoding the ATP synthase from alkaliphilic Bacillus firmus OF4
    • IVEY, D. M., KRULWICH, T. A.: Organization and nucleotide sequence of the atp genes encoding the ATP synthase from alkaliphilic Bacillus firmus OF4. Mol. Gen. Genet. 229, 292-300 (1991).
    • (1991) Mol. Gen. Genet. , vol.229 , pp. 292-300
    • Ivey, D.M.1    Krulwich, T.A.2
  • 24
    • 0000732090 scopus 로고
    • Evolution of protein molecules
    • (H. N. MUNRO ed.) New York, Academic Press
    • JUKES, T. H., CANTOR, C. R.: Evolution of protein molecules, pp. 21-132. In: Mammalian Protein Metabolism (H. N. MUNRO ed.) New York, Academic Press 1969.
    • (1969) Mammalian Protein Metabolism , pp. 21-132
    • Jukes, T.H.1    Cantor, C.R.2
  • 26
    • 0028596970 scopus 로고
    • +-ATPase from Enterococcus hirae
    • +-ATPase from Enterococcus hirae. J. Biochem. 116, 1302-1308 (1994).
    • (1994) J. Biochem. , vol.116 , pp. 1302-1308
    • Kakinuma, Y.1    Igarashi, K.2
  • 27
    • 0020383106 scopus 로고
    • Nucleotide sequence of the genes for β and ε subunits of proton-translocating ATPase from Escherichia coli
    • KANAZAWA, H., KAYANO, T., KIYASU, T., FUTAI, M.: Nucleotide sequence of the genes for β and ε subunits of proton-translocating ATPase from Escherichia coli. Biochem. Biophys. Res. Commun. 105, 1257-1264 (1982).
    • (1982) Biochem. Biophys. Res. Commun. , vol.105 , pp. 1257-1264
    • Kanazawa, H.1    Kayano, T.2    Kiyasu, T.3    Futai, M.4
  • 30
    • 0022448655 scopus 로고
    • Genetic transformation of the extreme thermophile Thermus thermophilus and other Thermus spp.
    • KOYAMA, Y., HOSHINO, T., TOMIZUKA, N., FURUKAWA, K.: Genetic transformation of the extreme thermophile Thermus thermophilus and other Thermus spp. J. Bacteriol. 166, 338-340 (1986).
    • (1986) J. Bacteriol. , vol.166 , pp. 338-340
    • Koyama, Y.1    Hoshino, T.2    Tomizuka, N.3    Furukawa, K.4
  • 31
    • 0028287844 scopus 로고
    • 1994. Thermus scotoductus, sp. nov., a pigment-producing thermophilic bacterium from hot tap water in Iceland and including Thermus sp. X-1
    • KRISTJANSSON, J. K., HJÖRLEIFSDOTTIR, S., MARTEINSSON, V. T., ALFREDSSON, G. A.: 1994. Thermus scotoductus, sp. nov., a pigment-producing thermophilic bacterium from hot tap water in Iceland and including Thermus sp. X-1. Syst. Appl. Microbiol. 17, 44-50 (1994).
    • (1994) Syst. Appl. Microbiol. , vol.17 , pp. 44-50
    • Kristjansson, J.K.1    Hjörleifsdottir, S.2    Marteinsson, V.T.3    Alfredsson, G.A.4
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • LAEMMLI, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685 (1970).
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
  • 35
    • 0018338129 scopus 로고
    • Preparation of the soluble ATPase from mitochondria, chloroplasts and bacteria by the chloroform technique
    • LINNETT, P. E., MITCHELL, A. D., PARTIS, M. D., BEECHEY, R. B.: Preparation of the soluble ATPase from mitochondria, chloroplasts and bacteria by the chloroform technique. Methods Enzymol. 55, 337-343 (1979).
    • (1979) Methods Enzymol. , vol.55 , pp. 337-343
    • Linnett, P.E.1    Mitchell, A.D.2    Partis, M.D.3    Beechey, R.B.4
  • 39
    • 0026563170 scopus 로고
    • Evolution of organellar proton-ATPases
    • NELSON, N.: Evolution of organellar proton-ATPases. Biochem. Biophys. Acta 1100, 109-124 (1992).
    • (1992) Biochem. Biophys. Acta , vol.1100 , pp. 109-124
    • Nelson, N.1
  • 40
    • 0002547924 scopus 로고
    • Molecular and cellular biology of F- and V-ATPases
    • (N. NELSON, ed.) New York, Berlin, Springer Verlag
    • NELSON, N.: Molecular and cellular biology of F- and V-ATPases, pp. 1-27. In: Organellar proton ATPases. (N. NELSON, ed.) New York, Berlin, Springer Verlag 1995.
    • (1995) Organellar Proton ATPases , pp. 1-27
    • Nelson, N.1
  • 42
    • 0029863893 scopus 로고    scopus 로고
    • Transfer of Thermus ruber (LOGINOVA et al. 1984), Thermus silvanus (TENREIRO et al. 1995), Thermus chliarophilus (TENREIRO et al. 1995), to Meiothermus gen. nov. as Meiothermus ruber comb, nov., Meiothermus silvanus comb, nov., Meiothermus chliarophilus comb. nov., respectively and emendation of the genus Thermus
    • NOBRE, M. F., TRÜPER, H. G., DA COSTA, M. S.: Transfer of Thermus ruber (LOGINOVA et al. 1984), Thermus silvanus (TENREIRO et al. 1995), Thermus chliarophilus (TENREIRO et al. 1995), to Meiothermus gen. nov. as Meiothermus ruber comb, nov., Meiothermus silvanus comb, nov., Meiothermus chliarophilus comb. nov., respectively and emendation of the genus Thermus. Int. J. Syst, Bacteriol. 46, 604-606 (1996).
    • (1996) Int. J. Syst, Bacteriol. , vol.46 , pp. 604-606
    • Nobre, M.F.1    Trüper, H.G.2    Da Costa, M.S.3
  • 44
    • 0001294549 scopus 로고
    • Genes and genetic manipulation in Thermus thermophilus
    • Thermus Species (R. J. SHARP, R. A. D. WILLIAMS, eds.) Plenum Press, London
    • OSHIMA, T.: Genes and genetic manipulation in Thermus thermophilus, pp. 185-205. In: Thermus Species (R. J. SHARP, R. A. D. WILLIAMS, eds.) Biotechnology Handbooks series, Plenum Press, London 1995.
    • (1995) Biotechnology Handbooks Series , pp. 185-205
    • Oshima, T.1
  • 45
    • 33646830005 scopus 로고
    • Ion motive ATPases. I. Ubiquity, properties and significance to cell function
    • PEDERSEN, P. L., CARAFOLI, E.: Ion motive ATPases. I. Ubiquity, properties and significance to cell function. Trends Biochem. Sci. 12, 146-150 (1987).
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 146-150
    • Pedersen, P.L.1    Carafoli, E.2
  • 46
    • 0000728066 scopus 로고
    • 16S rDNA analysis of Spirochaeta thermophila: Position and implications for the systematics of the order Spirochaetales
    • RAINEY, F. A., DORSCH, M., MORGAN, H. W., STACKEBRANDT, E.: 16S rDNA analysis of Spirochaeta thermophila: position and implications for the systematics of the order Spirochaetales. Syst. Appl. Microbiol. 16, 224-226 (1992).
    • (1992) Syst. Appl. Microbiol. , vol.16 , pp. 224-226
    • Rainey, F.A.1    Dorsch, M.2    Morgan, H.W.3    Stackebrandt, E.4
  • 47
    • 0027363870 scopus 로고
    • 16S rDNA analysis reveals phylogenetic diversity among the polysaccharolytic clostridia
    • RAINEY, F. A., STACKEBRANDT, E.: 16S rDNA analysis reveals phylogenetic diversity among the polysaccharolytic clostridia. FEMS Microbiol. Lett. 113, 125-128 (1993).
    • (1993) FEMS Microbiol. Lett. , vol.113 , pp. 125-128
    • Rainey, F.A.1    Stackebrandt, E.2
  • 50
    • 0023375195 scopus 로고
    • The neighbour-joining method: A new method for reconstructing phylogenetic trees
    • SAITOU, N., MEI, M.: The neighbour-joining method: A new method for reconstructing phylogenetic trees. Molecular Biol. Evol. 4, 406-425 (1987).
    • (1987) Molecular Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Mei, M.2
  • 51
    • 0024568225 scopus 로고
    • Confidence limits on phylogenetics: The bootstrap revisited
    • SANDERSON, M. J.: Confidence limits on phylogenetics: the bootstrap revisited. Cladistics 5, 113-129 (1989).
    • (1989) Cladistics , vol.5 , pp. 113-129
    • Sanderson, M.J.1
  • 52
    • 0024817092 scopus 로고
    • Numerical taxonomy of Thermus isolates from hot springs in Portugal
    • SANTOS, M. A., WILLIAMS, R. A. D., DA COSTA, M. S.: Numerical taxonomy of Thermus isolates from hot springs in Portugal. Syst. Appl. Microbiol. 12, 310-315 (1989).
    • (1989) Syst. Appl. Microbiol. , vol.12 , pp. 310-315
    • Santos, M.A.1    Williams, R.A.D.2    Da Costa, M.S.3
  • 54
    • 0025338413 scopus 로고
    • The proton-translocating ATPase of Escherichia coli
    • SENIOR, A. E.: The proton-translocating ATPase of Escherichia coli. Annu. Rev. Biophys. Biophys. Chem. 19, 7-41 (1990).
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 7-41
    • Senior, A.E.1
  • 56
    • 0029099451 scopus 로고
    • +-translocating ATPase in Methanobacterium thermoautotrophicum and their possible function under alkaline conditions
    • +-translocating ATPase in Methanobacterium thermoautotrophicum and their possible function under alkaline conditions. FEBS Lett. 371, 119-122 (1994).
    • (1994) FEBS Lett. , vol.371 , pp. 119-122
    • Smigan, P.1    Majernik, A.2    Polak, P.3    Hapala, I.4    Greksak, M.5
  • 57
    • 0023048899 scopus 로고
    • 1 ATPase of Escherichia coli and of the structural asymmetry of its β subunits
    • 1 ATPase of Escherichia coli and of the structural asymmetry of its β subunits. Eur. J. Biochem. 154, 321-327 (1986).
    • (1986) Eur. J. Biochem. , vol.154 , pp. 321-327
    • Stan-Lotter, H.1    Bragg, P.D.2
  • 59
    • 0029057969 scopus 로고
    • Nucleotide sequence of the ATPase A and B subunits of the halophilic archaebacterium Haloferax volcanii and characterization of the enzyme
    • STEINERT, K., KROTH-PANCIC, P. G., BICKEL-SANDKÖTTER, S.: Nucleotide sequence of the ATPase A and B subunits of the halophilic archaebacterium Haloferax volcanii and characterization of the enzyme. Biochim. Biophys. Acta 1249, 137-144 (1995).
    • (1995) Biochim. Biophys. Acta , vol.1249 , pp. 137-144
    • Steinert, K.1    Kroth-Pancic, P.G.2    Bickel-SANDKÖTTER, S.3
  • 62
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • THOMPSON, J. D., HIGGINS, D. G., GIBSON, T. J.: Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 63
    • 0017098799 scopus 로고
    • Halobacterium saccharovorum sp. nov., a carbohydrate-metabolizing, extremely halophilic bacterium
    • TOMLINSON, G. A., HOCHSTEIN, L. I.: Halobacterium saccharovorum sp. nov., a carbohydrate-metabolizing, extremely halophilic bacterium. Can. J. Microbiol. 22, 587-591 (1976).
    • (1976) Can. J. Microbiol. , vol.22 , pp. 587-591
    • Tomlinson, G.A.1    Hochstein, L.I.2
  • 64
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • TOWBIN, H., STAEHLIN, T., GORDON, J.: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354 (1979).
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehlin, T.2    Gordon, J.3
  • 65
    • 0026039536 scopus 로고
    • Molecular cloning of genes encoding major two subunits of a eubacterial V-type ATPase from Thermus thermophilus
    • TSUTSUMI, S., DENDA, K., YOKOYAMA, K., OSHIMA, T., DATE, T., YOSHIDA, M.: Molecular cloning of genes encoding major two subunits of a eubacterial V-type ATPase from Thermus thermophilus. Biochim. Biophys. Acta 1098, 13-20 (1991).
    • (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
  • 66
    • 0001853684 scopus 로고
    • The taxonomy and identification of Thermus
    • Thermus Species (R. J. SHARP, R. A. D. WILLIAMS, eds.) Plenum Press, London
    • WILLIAMS, R. A. D., SHARP, R.: The taxonomy and identification of Thermus, pp. 1-42. In: Thermus Species (R. J. SHARP, R. A. D. WILLIAMS, eds.) Biotechnology Handbooks series, Plenum Press, London 1995.
    • (1995) Biotechnology Handbooks Series , pp. 1-42
    • Williams, R.A.D.1    Sharp, R.2
  • 68
    • 0025695393 scopus 로고
    • Thermus thermophilus membrane-associated ATPase. Indication of a eubacterial V-type ATPase
    • YOKOYAMA, K., OSHIMA, T., YOSHIDA, M.: Thermus thermophilus membrane-associated ATPase. Indication of a eubacterial V-type ATPase. J. Biol. Chem. 265, 21946-21950 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 21946-21950
    • Yokoyama, K.1    Oshima, T.2    Yoshida, M.3


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