메뉴 건너뛰기




Volumn 180, Issue 13, 1998, Pages 3448-3452

The A1A0 ATPase from Methanosarcina mazei: Cloning of the 5'end of the aha operon encoding the membrane domain and expression of the proteolipid in a membrane-bound form in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; A1A0 ATPASE, METHANOSARCINA MAZEI; ARCHAEAL PROTEIN; PROTEOLIPID; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; RECOMBINANT PROTEIN;

EID: 0031595840     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.13.3448-3452.1998     Document Type: Article
Times cited : (30)

References (36)
  • 1
    • 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) J. Bacteriol. , vol.176 , pp. 2543-2550
    • Becher, B.1    Müller, V.2
  • 3
    • 0027301416 scopus 로고
    • Characterization of a membrane-associated ATPase from Methanococcus voltae, a methanogenic member of the Archaea
    • Chen, W., and J. Koniskv. 1993. Characterization of a membrane-associated ATPase from Methanococcus voltae, a methanogenic member of the Archaea. J. Bacteriol. 175:5677-5682.
    • (1993) J. Bacteriol. , vol.175 , pp. 5677-5682
    • Chen, W.1    Koniskv, J.2
  • 4
    • 0024961968 scopus 로고
    • A gene encoding the proteolipid subunit of Sulfolobus acidocaldarius ATPase complex
    • Denda, K., J. Konishi, T. Oshima, T. Date, and M. Yoshida. 1989. A gene encoding the proteolipid subunit of Sulfolobus acidocaldarius ATPase complex. J. Biol. Chem. 264:7119-7121.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7119-7121
    • Denda, K.1    Konishi, J.2    Oshima, T.3    Date, T.4    Yoshida, M.5
  • 5
    • 0029967858 scopus 로고    scopus 로고
    • Pathways of energy conservation in methanogenic Archaea
    • Deppenmeier, U., V. Müller, and G. Gottschalk. 1996. Pathways of energy conservation in methanogenic Archaea. Arch. Microbiol. 165:149-163.
    • (1996) Arch. Microbiol. , vol.165 , pp. 149-163
    • Deppenmeier, U.1    Müller, V.2    Gottschalk, G.3
  • 6
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis program for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis program for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 7
    • 0025877156 scopus 로고
    • 0 ATP synthase definded by random oligonucleotide-primed mutagenesis
    • 0 ATP synthase definded by random oligonucleotide-primed mutagenesis. J. Bacteriol. 173:2639-2643.
    • (1991) J. Bacteriol. , vol.173 , pp. 2639-2643
    • Fraga, D.1    Fillingame, R.H.2
  • 8
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 9
    • 0345194051 scopus 로고
    • Utilization of trimethylamine and other methyl compounds and methane formation by Methanosarcina barken
    • Hippe, H., D. Caspari, K. Fiebig, and G. Gottschalk. 1979. Utilization of trimethylamine and other methyl compounds and methane formation by Methanosarcina barken. Proc. Natl. Acad. Sci. USA 76:494-498
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 494-498
    • Hippe, H.1    Caspari, D.2    Fiebig, K.3    Gottschalk, G.4
  • 10
    • 0031570319 scopus 로고    scopus 로고
    • Identification of proteolipid from an extremely halophilic archaeon, Halobacterium salinarum, as an N,N'-dicyclohexyl-carbodiimide binding subunit of ATP synthase
    • Ihara, K., S. Watanabe, K. Sugimura, and Y. Mukohata. 1997. Identification of proteolipid from an extremely halophilic archaeon, Halobacterium salinarum, as an N,N'-dicyclohexyl-carbodiimide binding subunit of ATP synthase. Arch. Biochem. Biophys. 341:267-272.
    • (1997) Arch. Biochem. Biophys. , vol.341 , pp. 267-272
    • Ihara, K.1    Watanabe, S.2    Sugimura, K.3    Mukohata, Y.4
  • 11
    • 0029928926 scopus 로고    scopus 로고
    • +-pump activity in inverted vesicles of Methanosarcina mazei Gö1 and characterization of membrane ATPase
    • +-pump activity in inverted vesicles of Methanosarcina mazei Gö1 and characterization of membrane ATPase. J. Bacteriol. 178:2424-2426.
    • (1996) J. Bacteriol. , vol.178 , pp. 2424-2426
    • Inatomi, K.1
  • 12
    • 0022501645 scopus 로고
    • Characterization and purification of the membranebound ATPase of the archaebacterium Methanosarcina barken
    • Inatomi, K. I. 1986. Characterization and purification of the membranebound ATPase of the archaebacterium Methanosarcina barken. J. Bacteriol. 167:837-841.
    • (1986) J. Bacteriol. , vol.167 , pp. 837-841
    • Inatomi, K.I.1
  • 13
    • 0027470998 scopus 로고
    • Membrane ATPase from the aceticlastic methanogen Methanothrix thermophila
    • Inatomi, K. I., Y. Kamagata, and K. Nakamura. 1993. Membrane ATPase from the aceticlastic methanogen Methanothrix thermophila. J. Bacteriol. 175:80-84.
    • (1993) J. Bacteriol. , vol.175 , pp. 80-84
    • Inatomi, K.I.1    Kamagata, Y.2    Nakamura, K.3
  • 14
    • 0024401450 scopus 로고
    • Dicyclohexylcarbodiimidebinding protein is a subunit of the Methanosarcina barken ATPase complex
    • Inatomi, K. I., M. Maeda, and M. Futai. 1989. Dicyclohexylcarbodiimidebinding protein is a subunit of the Methanosarcina barken ATPase complex. Biochem. Biophys. Res. Commun. 162:1585-1590.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 1585-1590
    • Inatomi, K.I.1    Maeda, M.2    Futai, M.3
  • 16
    • 0021736478 scopus 로고
    • In vivo evidence for the role of the ε subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli
    • Klionsky, D. J., W. S. A. Brusilow, and R. D. Simoni. 1984. In vivo evidence for the role of the ε subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli. J. Bacteriol. 160:1055-1060.
    • (1984) J. Bacteriol. , vol.160 , pp. 1055-1060
    • Klionsky, D.J.1    Brusilow, W.S.A.2    Simoni, R.D.3
  • 18
    • 0022021846 scopus 로고
    • Translational initiation frequency of atp genes from Escherichia coli: Identification of an intercistronic sequence that enhances translation
    • McCarthy, J. E. G., H. U. Schairer, and W. Sebald. 1985. Translational initiation frequency of atp genes from Escherichia coli: identification of an intercistronic sequence that enhances translation. EMBO J. 4:519-526.
    • (1985) EMBO J. , vol.4 , pp. 519-526
    • McCarthy, J.E.G.1    Schairer, H.U.2    Sebald, W.3
  • 19
    • 0001203042 scopus 로고
    • Bioenergetics of methanogenesis
    • J. G. Ferry (ed.), Chapman & Hall, New York, N.Y.
    • Müller, V., M. Blaut, and G. Gottschalk. 1993. Bioenergetics of methanogenesis, p. 360-406. In J. G. Ferry (ed.), Methanogenesis. Chapman & Hall, New York, N.Y.
    • (1993) Methanogenesis , pp. 360-406
    • Müller, V.1    Blaut, M.2    Gottschalk, G.3
  • 20
    • 0026563170 scopus 로고
    • Evolution of organellar proton-ATPases
    • Nelson, N. 1992. Evolution of organellar proton-ATPases. Biochim. Biophys. Acta 1100:109-124.
    • (1992) Biochim. Biophys. Acta , vol.1100 , pp. 109-124
    • Nelson, N.1
  • 21
    • 0028238357 scopus 로고
    • Alternative mRNA splicing generates tissue-specific isoforms of 116-kDa polypeptide of vacuolar proton pump
    • Peng, S. B., B. P. Crider, X.-S. Xie, and D. K. Stone. 1994. Alternative mRNA splicing generates tissue-specific isoforms of 116-kDa polypeptide of vacuolar proton pump. J. Biol. Chem. 269:17262-17266.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17262-17266
    • Peng, S.B.1    Crider, B.P.2    Xie, X.-S.3    Stone, D.K.4
  • 24
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:369-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 369-379
    • Schägger, H.1    Von Jagow, G.2
  • 25
    • 0023254924 scopus 로고
    • Inducible expression vectors incorporating the Escherichia coli atpE translational initiation region
    • Schauder, B., H. Blöcker, R. Frank, and J. E. G. McCarthy. 1987. Inducible expression vectors incorporating the Escherichia coli atpE translational initiation region. Gene 52:279-283.
    • (1987) Gene , vol.52 , pp. 279-283
    • Schauder, B.1    Blöcker, H.2    Frank, R.3    McCarthy, J.E.G.4
  • 26
    • 0025096973 scopus 로고
    • Chemiosmotic energy conservation and the membrane ATPase of Methanolobus tindarius
    • Scheel, E., and G. Schäfer. 1990. Chemiosmotic energy conservation and the membrane ATPase of Methanolobus tindarius. Eur. J. Biochem. 187:727-735.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 727-735
    • Scheel, E.1    Schäfer, G.2
  • 30
    • 0023571657 scopus 로고
    • High-copy-number and low-copy-number plasmid vectors for lacZα-complementation and chloramphenicol-resistance selection
    • Takeshita, S., M. Sato, M. Toba, W. Masahashi, and T. Hashimoto-Gotoh. 1987. High-copy-number and low-copy-number plasmid vectors for lacZα-complementation and chloramphenicol-resistance selection. Gene 61:63-74.
    • (1987) Gene , vol.61 , pp. 63-74
    • Takeshita, S.1    Sato, M.2    Toba, M.3    Masahashi, W.4    Hashimoto-Gotoh, T.5
  • 31
    • 0014055981 scopus 로고
    • Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol
    • Tanaka, S., S. A. Lerner, and E. C. C. Lin. 1967. Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol. J. Bacteriol. 93:642-648.
    • (1967) J. Bacteriol. , vol.93 , pp. 642-648
    • Tanaka, S.1    Lerner, S.A.2    Lin, E.C.C.3
  • 32
    • 0023275830 scopus 로고
    • A family of yeast expression vectors containing the phage f1 intergenic region
    • Vernet, T., D. Dignard, and D. Y. Thomas. 1987. A family of yeast expression vectors containing the phage f1 intergenic region. Gene 52:225-233.
    • (1987) Gene , vol.52 , pp. 225-233
    • Vernet, T.1    Dignard, D.2    Thomas, D.Y.3
  • 33
    • 0021756359 scopus 로고
    • The une operon. Nucleotide sequence, regulation and structure of ATP-synthase
    • Walker, J. E., M. Saraste, and N. J. Gay. 1984. The une operon. Nucleotide sequence, regulation and structure of ATP-synthase. Biochim. Biophys. Acta 768:164-200.
    • (1984) Biochim. Biophys. Acta , vol.768 , pp. 164-200
    • Walker, J.E.1    Saraste, M.2    Gay, N.J.3
  • 34
    • 15144351674 scopus 로고
    • Ph.D. thesis. University of Göttingen, Göttingen, Germany
    • Wilms, R. 1992. Ph.D. thesis. University of Göttingen, Göttingen, Germany.
    • (1992)
    • Wilms, R.1
  • 36
    • 0025362525 scopus 로고
    • Role of vacuolar acidification in protein sorting and zymogen activation: A genetic analysis of the yeast vacuolar proton-translocating ATPase
    • Yamashiro, C. T., P. M. Kane, D. F. Wolczyk, R. A. Preston, and T. H. Stevens. 1990. Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase. Mol. Cell. Biol. 10:3737-3749.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3737-3749
    • Yamashiro, C.T.1    Kane, P.M.2    Wolczyk, D.F.3    Preston, R.A.4    Stevens, T.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.