메뉴 건너뛰기




Volumn 269, Issue 2, 2007, Pages 301-308

Isolation and characterization of an amiloride-resistant mutant of Methanothermobacter thermautotrophicus possessing a defective Na +/H+ antiport

Author keywords

Archaea; ATP synthesis; Methanogen; Sodium proton exchange

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMILORIDE; POTASSIUM ION; SODIUM ION; SODIUM PROTON EXCHANGE PROTEIN; TETRACHLORSALAN;

EID: 33947362001     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2007.00655.x     Document Type: Article
Times cited : (13)

References (33)
  • 1
    • 0028181851 scopus 로고
    • 0-ATP synthase in membrane vesicles of the archaeon Methanosarcina mazei Go1
    • 0-ATP synthase in membrane vesicles of the archaeon Methanosarcina mazei Go1. J Bacteriol 176: 2543-2550.
    • (1994) J Bacteriol , vol.176 , pp. 2543-2550
    • Becher, B.1    Müller, V.2
  • 2
    • 1642356650 scopus 로고    scopus 로고
    • Isolation and characterization of an uncoupler-resistant mutant of Methanothermobacter thermautotrophicus
    • Čuboňová L, Šurín S, Majerník A & Šmigán P (2004) Isolation and characterization of an uncoupler-resistant mutant of Methanothermobacter thermautotrophicus. FEMS Microbiol Lett 233: 23-28.
    • (2004) FEMS Microbiol Lett , vol.233 , pp. 23-28
    • Čuboňová, L.1    Šurín, S.2    Majerník, A.3    Šmigán, P.4
  • 3
    • 0036357283 scopus 로고    scopus 로고
    • The unique biochemistry of methanogenesis
    • Deppenmeier U (2002) The unique biochemistry of methanogenesis. Prog Nucleic Acid Res Mol Biol 71: 223-283.
    • (2002) Prog Nucleic Acid Res Mol Biol , vol.71 , pp. 223-283
    • Deppenmeier, U.1
  • 4
    • 0025189332 scopus 로고
    • 2-dependent heterodisulfide reductase in methanogenic bacterium strain gol and Methanolobus tindarius
    • 2-dependent heterodisulfide reductase in methanogenic bacterium strain gol and Methanolobus tindarius. FEBS Lett 261: 199-203.
    • (1990) FEBS Lett , vol.261 , pp. 199-203
    • Deppenmeier, U.1    Blaut, M.2    Mahlmann, A.3    Gottschalk, G.4
  • 5
    • 0037220138 scopus 로고    scopus 로고
    • Bioenergetics of the formyl-methanofuran dehydrogenase and heterodisulfide reductase reactions in Methanothermobacter thermautotrophicus
    • de Poorter LM, Geerts WG, Theuvenet AP & Keltjens JT (2003) Bioenergetics of the formyl-methanofuran dehydrogenase and heterodisulfide reductase reactions in Methanothermobacter thermautotrophicus. Eur J Biochem 270: 66-75.
    • (2003) Eur J Biochem , vol.270 , pp. 66-75
    • de Poorter, L.M.1    Geerts, W.G.2    Theuvenet, A.P.3    Keltjens, J.T.4
  • 6
    • 0035342616 scopus 로고    scopus 로고
    • The Na(+)-translocating methyltransferase complex from methanogenic archaea
    • Gottschalk G & Thauer RK (2001) The Na(+)-translocating methyltransferase complex from methanogenic archaea. Biochim Biophys Acta 1505: 28-36.
    • (2001) Biochim Biophys Acta , vol.1505 , pp. 28-36
    • Gottschalk, G.1    Thauer, R.K.2
  • 7
    • 0034835047 scopus 로고    scopus 로고
    • Sodium ion cycle in bacterial pathogens: Evidence from cross-genome comparisons
    • table of contents
    • Häse CC, Fedorova ND, Galperin MY & Dibrov PA (2001) Sodium ion cycle in bacterial pathogens: evidence from cross-genome comparisons. Microbiol Mol Biol Rev 65: 353-370, table of contents.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 353-370
    • Häse, C.C.1    Fedorova, N.D.2    Galperin, M.Y.3    Dibrov, P.A.4
  • 8
    • 0025187801 scopus 로고
    • Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)
    • Hedderich R, Berkessel A &Thauer RK (1990) Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg). Eur J Biochem 193: 255-261.
    • (1990) Eur J Biochem , vol.193 , pp. 255-261
    • Hedderich, R.1    Berkessel, A.2    Thauer, R.K.3
  • 9
    • 0033545947 scopus 로고    scopus 로고
    • Mutations conferring resistance to phenamil and amiloride, inhibitors of sodium-driven motility of Vibrio parahaemolyticus
    • Jaques S, Kim YK & McCarter LL (1999) Mutations conferring resistance to phenamil and amiloride, inhibitors of sodium-driven motility of Vibrio parahaemolyticus. Proc Natl Acad Sci USA 96: 5740-5745.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5740-5745
    • Jaques, S.1    Kim, Y.K.2    McCarter, L.L.3
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 17144454389 scopus 로고    scopus 로고
    • Biochemical analysis of neomycin-resistance in the methanoarchaeon Methanothermobacter thermautotrophicus and some implications for energetic processes in this strain
    • Majerník A, Čuboňová L, Polák P, Šmigáň P & Greksák M (2003) Biochemical analysis of neomycin-resistance in the methanoarchaeon Methanothermobacter thermautotrophicus and some implications for energetic processes in this strain. Anaerobe 9: 31-38.
    • (2003) Anaerobe , vol.9 , pp. 31-38
    • Majerník, A.1    Čuboňová, L.2    Polák, P.3    Šmigáň, P.4    Greksák, M.5
  • 14
    • 2542487925 scopus 로고    scopus 로고
    • 0 ATPases: From multimeric to monomeric rotors comprising 6-13 ion binding sites
    • 0 ATPases: from multimeric to monomeric rotors comprising 6-13 ion binding sites. J Bioenerg Biomembr 36: 115-125.
    • (2004) J Bioenerg Biomembr , vol.36 , pp. 115-125
    • Müller, V.1
  • 15
    • 0024289450 scopus 로고
    • Electron-transport- driven sodium extrusion during methanogenesis from formaldehyde and molecular hydrogen by Methanosarcina barkeri
    • Müller V, Winner C & Gottschalk G (1988) Electron-transport- driven sodium extrusion during methanogenesis from formaldehyde and molecular hydrogen by Methanosarcina barkeri. Eur J Biochem 178: 519-525.
    • (1988) Eur J Biochem , vol.178 , pp. 519-525
    • Müller, V.1    Winner, C.2    Gottschalk, G.3
  • 18
    • 0001580628 scopus 로고
    • Sodium dependence of methane formation in methanogenic bacteria
    • Perski HJ, Schönheit P & Thauer RK (1982) Sodium dependence of methane formation in methanogenic bacteria. FEBS Lett 143: 323-326.
    • (1982) FEBS Lett , vol.143 , pp. 323-326
    • Perski, H.J.1    Schönheit, P.2    Thauer, R.K.3
  • 19
    • 0034567462 scopus 로고    scopus 로고
    • The membrane potential of Methanobacterium thermoautotrophicum under different external conditions
    • Polák P, Šmigáň P & Greksák M (2000) The membrane potential of Methanobacterium thermoautotrophicum under different external conditions. Folia Microbiologica 45: 107-113.
    • (2000) Folia Microbiologica , vol.45 , pp. 107-113
    • Polák, P.1    Šmigáň, P.2    Greksák, M.3
  • 20
    • 32444451427 scopus 로고    scopus 로고
    • 2 assimilation in the archaeon Methanococcus maripaludis
    • 2 assimilation in the archaeon Methanococcus maripaludis. J Bacteriol 188: 1373-1380.
    • (2006) J Bacteriol , vol.188 , pp. 1373-1380
    • Porat, I.1    Kim, W.2    Hendrickson, E.L.3
  • 21
    • 0035808978 scopus 로고    scopus 로고
    • Selective extraction of subunit D of the Na(+)-translocating methyltransferase and subunit c of the A(1)A(0) ATPase from the cytoplasmic membrane of methanogenic archaea by chloroform/methanol and characterization of subunit c of Methanothermobacter thermoautotrophicus as a 16-kDa proteolipid
    • Ruppert C, Schmid R, Hedderich R & Müller V (2001) Selective extraction of subunit D of the Na(+)-translocating methyltransferase and subunit c of the A(1)A(0) ATPase from the cytoplasmic membrane of methanogenic archaea by chloroform/methanol and characterization of subunit c of Methanothermobacter thermoautotrophicus as a 16-kDa proteolipid. FEMS Microbiol Lett 195: 47-51.
    • (2001) FEMS Microbiol Lett , vol.195 , pp. 47-51
    • Ruppert, C.1    Schmid, R.2    Hedderich, R.3    Müller, V.4
  • 22
    • 0034045136 scopus 로고    scopus 로고
    • Purification and characterization of a membrane-bound hydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Sapra R, Verhagen MF & Adams MW (2000) Purification and characterization of a membrane-bound hydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol 182: 3423-3428.
    • (2000) J Bacteriol , vol.182 , pp. 3423-3428
    • Sapra, R.1    Verhagen, M.F.2    Adams, M.W.3
  • 23
    • 0037934657 scopus 로고    scopus 로고
    • A simple energy-conserving system: Proton reduction coupled to proton translocation
    • Sapra R, Bagramyan K & Adams MW (2003) A simple energy-conserving system: proton reduction coupled to proton translocation. Proc Natl Acad Sci USA 100: 7545-7550.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7545-7550
    • Sapra, R.1    Bagramyan, K.2    Adams, M.W.3
  • 25
    • 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 & von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 26
    • 0021020851 scopus 로고
    • ATP synthesis driven by potassium diffusion potential in Methanobacterium thermoautotrophicum is stimulated by sodium
    • Schönheit P & Perski HJ (1983) ATP synthesis driven by potassium diffusion potential in Methanobacterium thermoautotrophicum is stimulated by sodium. FEMS Microbiol Lett 20: 263-267.
    • (1983) FEMS Microbiol Lett , vol.20 , pp. 263-267
    • Schönheit, P.1    Perski, H.J.2
  • 28
    • 0021143022 scopus 로고
    • Effect of 2,4-dinitrophenol and ionophores on growth and methanogenesis in Methanobacterium thermoautotrophicum
    • Šmigáň P, Friederová A, Rusnák P & Greksák M (1984) Effect of 2,4-dinitrophenol and ionophores on growth and methanogenesis in Methanobacterium thermoautotrophicum. Folia Microbiol 29: 353-358.
    • (1984) Folia Microbiol , vol.29 , pp. 353-358
    • Šmigáň, P.1    Friederová, A.2    Rusnák, P.3    Greksák, M.4
  • 30
    • 0029099451 scopus 로고
    • +-translocating ATPases in Methanobacterium thermoautotrophicum and their possible function under alkaline conditions
    • +-translocating ATPases in Methanobacterium thermoautotrophicum and their possible function under alkaline conditions. FEBS Letters 371: 119-122.
    • (1995) FEBS Letters , vol.371 , pp. 119-122
    • Šmigáň, P.1    Majerník, A.2    Polák, P.3    Hapala, I.4    Greksák, M.5
  • 32
    • 0033568398 scopus 로고    scopus 로고
    • Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins
    • Tersteegen A & Hedderich R (1999) Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins. Eur J Biochem 264: 930-943.
    • (1999) Eur J Biochem , vol.264 , pp. 930-943
    • Tersteegen, A.1    Hedderich, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.