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Volumn 1807, Issue 9, 2011, Pages 1133-1142

The Na+-translocating F1FO-ATPase from the halophilic, alkalithermophile Natranaerobius thermophilus

Author keywords

Alkalithermophile; ATPase; Epsilon subunit; Halophile; Natranaerobius thermophilus

Indexed keywords

ADENOSINE TRIPHOSPHATE; ENZYME INHIBITOR; IONOPHORE; MAGNESIUM ION; MONENSIN; N,N' DICYLOHEXYLCARBODIIMIDE; POTASSIUM ION; PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SODIUM; UNCLASSIFIED DRUG;

EID: 79960556381     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.05.001     Document Type: Article
Times cited : (16)

References (56)
  • 1
    • 0029909791 scopus 로고    scopus 로고
    • The intracellular pH of Clostridium paradoxum, an anaerobic, alkaliphilic, and thermophilic bacterium
    • G. Cook, J. Russell, A. Reichert, and J. Wiegel The intracellular pH of Clostridium paradoxum, an anaerobic, alkaliphilic, and thermophilic bacterium Appl. Environ. Microbiol. 62 1996 4576 4579 (Pubitemid 26399458)
    • (1996) Applied and Environmental Microbiology , vol.62 , Issue.12 , pp. 4576-4579
    • Cook, G.M.1    Russell, J.B.2    Reichert, A.3    Wiegel, J.4
  • 2
    • 33745882947 scopus 로고    scopus 로고
    • o-ATPase from the thermoalkaliphilic bacterium Clostridium paradoxum
    • DOI 10.1128/JB.00128-06
    • o-ATPase from the thermoalkaliphilic bacterium Clostridium paradoxum J. Bacteriol. 188 2006 5045 5054 (Pubitemid 44051471)
    • (2006) Journal of Bacteriology , vol.188 , Issue.14 , pp. 5045-5054
    • Ferguson, S.A.1    Keis, S.2    Cook, G.M.3
  • 3
    • 49149125126 scopus 로고    scopus 로고
    • Sulfolobales
    • M. Dworkin, S. Falkow, E. Rosenberg, K.-H. Schleifer, E. Stackebrandt, Springer New York
    • H. Huber, and D. Prangishvili Sulfolobales M. Dworkin, S. Falkow, E. Rosenberg, K.-H. Schleifer, E. Stackebrandt, The Prokaryotes: Archaea. Bacteria: Firmicutes, Actinomycetes vol. 3 2006 Springer New York 23 51
    • (2006) The Prokaryotes: Archaea. Bacteria: Firmicutes, Actinomycetes , vol.3 VOL. , pp. 23-51
    • Huber, H.1    Prangishvili, D.2
  • 4
    • 0037207875 scopus 로고    scopus 로고
    • Bioenergetic properties of the thermoalkailphilic Bacillus sp. strain TA2.A1
    • DOI 10.1128/JB.185.2.461-465.2003
    • K. Olsson, S. Keis, H.W. Morgan, P. Dimroth, and G.M. Cook Bioenergetic properties of the thermoalkaliphilic Bacillus sp. strain TA2.A1 J. Bacteriol. 185 2003 461 465 (Pubitemid 36070471)
    • (2003) Journal of Bacteriology , vol.185 , Issue.2 , pp. 461-465
    • Olsson, K.1    Keis, S.2    Morgan, H.W.3    Dimroth, P.4    Cook, G.M.5
  • 5
    • 0032964959 scopus 로고    scopus 로고
    • Sodium-dependent glutamate uptake by an alkaliphilic, thermophilic bacillus strain, ta2.A1
    • C.J. Peddie, G.M. Cook, and H.W. Morgan Sodium-dependent glutamate uptake by an alkaliphilic, thermophilic Bacillus strain, TA2.A1 J. Bacteriol. 181 1999 3172 3177 (Pubitemid 29236923)
    • (1999) Journal of Bacteriology , vol.181 , Issue.10 , pp. 3172-3177
    • Peddie, C.J.1    Cook, G.M.2    Morgan, H.W.3
  • 7
    • 0028806517 scopus 로고
    • Picrophilus gen. nov., fam. nov.: A novel aerobic, heterotrophic, thermoacidophilic genus and family comprising archaea capable of growth around pH 0
    • C. Schleper, G. Puehler, I. Holz, A. Gambacorta, D. Janekovic, U. Santarius, H. Klenk, and W. Zillig Picrophilus gen. nov., fam. nov.: a novel aerobic, heterotrophic, thermoacidophilic genus and family comprising archaea capable of growth around pH 0 J. Bacteriol. 177 1995 7050 7059
    • (1995) J. Bacteriol. , vol.177 , pp. 7050-7059
    • Schleper, C.1    Puehler, G.2    Holz, I.3    Gambacorta, A.4    Janekovic, D.5    Santarius, U.6    Klenk, H.7    Zillig, W.8
  • 8
    • 11144313963 scopus 로고
    • Thermoplasma acidophilum and Thermoplasma volcanium sp. nov., from solfatara fields
    • A. Segerer, T.A. Langworthy, and K.O. Stetter Thermoplasma acidophilum and Thermoplasma volcanium sp. nov., from solfatara fields Syst. Appl. Microbiol. 10 1988 161 171
    • (1988) Syst. Appl. Microbiol. , vol.10 , pp. 161-171
    • Segerer, A.1    Langworthy, T.A.2    Stetter, K.O.3
  • 9
    • 41349118342 scopus 로고    scopus 로고
    • Life at extreme limits: The anaerobic halophilic alkalithermophiles
    • DOI 10.1196/annals.1419.028, Incredible Anaerobes From Physiology to Genomics to Fuels
    • N.M. Mesbah, and J. Wiegel Life at extreme limits: the anaerobic halophilic alkalithermophiles J. Wiegel, M.W.W. Adams, R. Maier, The Incredible Anaerobes: From Physiology to Genomics to Fuels 2008 Annals of the New York Academy of Sciences New York 44 57 (Pubitemid 351451169)
    • (2008) Annals of the New York Academy of Sciences , vol.1125 , pp. 44-57
    • Mesbah, N.M.1    Wiegel, J.2
  • 10
    • 36549017617 scopus 로고    scopus 로고
    • Natranaerobius thermophilus gen. nov., sp. nov., a holophilic, alkalithermophilic bacterium from soda lakes of the Wadi An Natrun, Egypt, and proposal of Natranaerobiaceae fam. nov. and Natranaerobiales ord. nov
    • DOI 10.1099/ijs.0.65068-0
    • N.M. Mesbah, D.B. Hedrick, A.D. Peacock, M. Rohde, and J. Wiegel Natranaerobius thermophilus gen. nov. sp. nov., a halophilic, alkalithermophilic bacterium from soda lakes of the Wadi An Natrun, Egypt, and proposal of Natranaerobiaceae fam. nov. and Natranaerobiales ord. nov. Int. J. Syst. Evol. Microbiol. 57 2007 2507 2512 (Pubitemid 350187410)
    • (2007) International Journal of Systematic and Evolutionary Microbiology , vol.57 , Issue.11 , pp. 2507-2512
    • Mesbah, N.M.1    Hedrick, D.B.2    Peacock, A.D.3    Rohde, M.4    Wiegel, J.5
  • 11
    • 72449203758 scopus 로고    scopus 로고
    • Biodiversity of poly-extremophilic bacteria: Does combining the extremes of high salt, alkaline pH and elevated temperature approach a physico-chemical boundary for life?
    • K.J. Bowers, N.M. Mesbah, and J. Wiegel Biodiversity of poly-extremophilic bacteria: does combining the extremes of high salt, alkaline pH and elevated temperature approach a physico-chemical boundary for life? Saline Systems 5 2009 9
    • (2009) Saline Systems , vol.5 , pp. 9
    • Bowers, K.J.1    Mesbah, N.M.2    Wiegel, J.3
  • 13
    • 0002772862 scopus 로고    scopus 로고
    • Sodium stress
    • G. Storz, R. Hengge-Aronis, ASM Press Washington D.C.
    • E. Padan, and T.A. Krulwich Sodium stress G. Storz, R. Hengge-Aronis, Bacterial Stress Responses 2000 ASM Press Washington D.C. 117 130
    • (2000) Bacterial Stress Responses , pp. 117-130
    • Padan, E.1    Krulwich, T.A.2
  • 14
    • 36549083287 scopus 로고    scopus 로고
    • Isolation, cultivation and characterization of alkalithermophiles
    • F.A. Rainey, A. Oren, Elsevier London
    • N.M. Mesbah, and J. Wiegel Isolation, cultivation and characterization of alkalithermophiles F.A. Rainey, A. Oren, Methods in Microbiology Volume 35: Extremophilic Microorganisms vol. 38 2006 Elsevier London 451 468
    • (2006) Methods in Microbiology Volume 35: Extremophilic Microorganisms , vol.38 VOL. , pp. 451-468
    • Mesbah, N.M.1    Wiegel, J.2
  • 15
    • 0032143255 scopus 로고    scopus 로고
    • Anaerobic alkalithermophiles, a novel group of extremophiles
    • DOI 10.1007/s007920050068
    • J. Wiegel Anaerobic alkalithermophiles, a novel group of extremophiles Extremophiles 2 1998 257 267 (Pubitemid 28408007)
    • (1998) Extremophiles , vol.2 , Issue.3 , pp. 257-267
    • Wiegel, J.1
  • 17
    • 70349932063 scopus 로고    scopus 로고
    • Cation/proton antiporter complements of bacteria: Why so large and diverse?
    • T.A. Krulwich, D.B. Hicks, and M. Ito Cation/proton antiporter complements of bacteria: why so large and diverse? Mol. Microbiol. 74 2009 257 260
    • (2009) Mol. Microbiol. , vol.74 , pp. 257-260
    • Krulwich, T.A.1    Hicks, D.B.2    Ito, M.3
  • 18
  • 22
    • 0034737965 scopus 로고    scopus 로고
    • ATP synthase: What we know about ATP hydrolysis and what we do not know about ATP synthesis
    • DOI 10.1016/S0005-2728(00)00082-7, PII S0005272800000827
    • J. Weber, and A.E. Senior ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis Biochim. Biophys. Acta 1458 2000 300 309 (Pubitemid 30320713)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1458 , Issue.2-3 , pp. 300-309
    • Weber, J.1    Senior, A.E.2
  • 23
    • 0141789637 scopus 로고    scopus 로고
    • Surviving the acid test: Responses of gram-positive bacteria to low pH
    • DOI 10.1128/MMBR.67.3.429-453.2003
    • P.D. Cotter, and C. Hill Surviving the acid test: responses of Gram-positive bacteria to low pH Microbiol. Mol. Biol. Rev. 67 2003 429 453 (Pubitemid 37122528)
    • (2003) Microbiology and Molecular Biology Reviews , vol.67 , Issue.3 , pp. 429-453
    • Cotter, P.D.1    Hill, C.2
  • 24
    • 0000871115 scopus 로고
    • The effect of sulfur compounds on the growth of the halophilic homoacetic bacterium Acetohalobium arabaticum
    • V.V. Kevbrin, and G.A. Zavarzin The effect of sulfur compounds on the growth of the halophilic homoacetic bacterium Acetohalobium arabaticum Microbiologia 61 1992 812 817
    • (1992) Microbiologia , vol.61 , pp. 812-817
    • Kevbrin, V.V.1    Zavarzin, G.A.2
  • 25
    • 10644224511 scopus 로고
    • Formation of methane by bacterial extracts
    • E.A. Wolin, M.J. Wolin, and R.S. Wolfe Formation of methane by bacterial extracts J. Biol. Chem. 238 1963 2882 2886
    • (1963) J. Biol. Chem. , vol.238 , pp. 2882-2886
    • Wolin, E.A.1    Wolin, M.J.2    Wolfe, R.S.3
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0028219162 scopus 로고
    • A simple modification of the Blum's silver stain method allows for 30 minute detection of proteins in polyacrylamide gels
    • M.V. Nesterenko, M. Tilley, and S.J. Upton A simple modification of the Blum's silver stain method allows for 30 minute detection of proteins in polyacrylamide gels J. Biochem. Biophys. Methods 28 1994 239 242
    • (1994) J. Biochem. Biophys. Methods , vol.28 , pp. 239-242
    • Nesterenko, M.V.1    Tilley, M.2    Upton, S.J.3
  • 29
    • 0032541971 scopus 로고    scopus 로고
    • Detergent-mediated reconstitution of membrane proteins
    • DOI 10.1021/bi981596u
    • J. Knol, K. Sjollema, and B. Poolman Detergent-mediated reconstitution of membrane proteins Biochemistry 37 1998 16410 16415 (Pubitemid 28536277)
    • (1998) Biochemistry , vol.37 , Issue.46 , pp. 16410-16415
    • Knol, J.1    Sjollema, K.2    Poolman, B.3
  • 30
    • 0015304036 scopus 로고
    • Membrane-bound adenosine triphosphatase of Escherichia coli
    • H. Kobayashi, and Y. Anraku Membrane-bound adenosine triphosphatase of Escherichia coli J. Biochem. Biophys. Methods 71 1972 387 399
    • (1972) J. Biochem. Biophys. Methods , vol.71 , pp. 387-399
    • Kobayashi, H.1    Anraku, Y.2
  • 31
    • 33846040629 scopus 로고    scopus 로고
    • TransportDB: A comprehensive database resource for cytoplasmic membrane transport systems and outer membrane channels
    • Q. Ren, K. Chen, and I.T. Paulsen TransportDB: a comprehensive database resource for cytoplasmic membrane transport systems and outer membrane channels Nucleic Acids Res. 35 2007 D274 D279
    • (2007) Nucleic Acids Res. , vol.35
    • Ren, Q.1    Chen, K.2    Paulsen, I.T.3
  • 33
    • 0032825378 scopus 로고    scopus 로고
    • 0-ATPase (atpBEFHAGDC) operon of Lactobacillus acidophilus by differential display: Gene structure, cloning and characterization
    • DOI 10.1046/j.1365-2958.1999.01557.x
    • o-ATPase (atpBEFHAGDC) operon of Lactobacillus acidophilus by differential display: gene structure, cloning and characterization Mol. Microbiol. 33 1999 1152 1161 (Pubitemid 29433621)
    • (1999) Molecular Microbiology , vol.33 , Issue.6 , pp. 1152-1161
    • Kullen, M.J.1    Klaenhammer, T.R.2
  • 34
    • 0042838028 scopus 로고    scopus 로고
    • o ATP synthase: Operon, composition, and some properties
    • DOI 10.1128/JB.185.18.5527-5535.2003
    • 0 ATP synthase: operon, composition and some properties J. Bacteriol. 185 2003 5527 5535 (Pubitemid 37082410)
    • (2003) Journal of Bacteriology , vol.185 , Issue.18 , pp. 5527-5535
    • Das, A.1    Ljungdahl, L.G.2
  • 38
    • 0021756359 scopus 로고
    • Teh unc operon: Nucleotide sequence, regulation, and structure of ATP synthase
    • J.E. Walker, M. Saraste, and N.J. Gay Teh unc operon: nucleotide sequence, regulation, and structure of ATP synthase Biochim. Biophys. Acta 768 1982 164 200
    • (1982) Biochim. Biophys. Acta , vol.768 , pp. 164-200
    • Walker, J.E.1    Saraste, M.2    Gay, N.J.3
  • 40
  • 43
    • 66349115722 scopus 로고    scopus 로고
    • The ins and outs of Na+ bioenergetics in Acetobacterium woodii
    • S. Schmidt, E. Biegel, and V. Muller The ins and outs of Na+ bioenergetics in Acetobacterium woodii Biochim. Biophys. Acta 1787 2009 691 696
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 691-696
    • Schmidt, S.1    Biegel, E.2    Muller, V.3
  • 44
    • 0034737857 scopus 로고    scopus 로고
    • 0 ATPases: Structure, arrangement, and role of the ε subunit in energy coupling within the complex
    • DOI 10.1016/S0005-2728(00)00078-5, PII S0005272800000785
    • 0 ATPases. Structure, arrangement and role of the ε subunit in energy coupling within the complex Biochim Biophys Acta 1458 2000 263 269 (Pubitemid 30320709)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1458 , Issue.2-3 , pp. 263-269
    • Capaldi, R.A.1    Schulenberg, B.2
  • 45
    • 0003518480 scopus 로고
    • John Wiley and Sons, Inc. New York
    • I.H. Segel Enzyme Kinetics 1975 John Wiley and Sons, Inc. New York
    • (1975) Enzyme Kinetics
    • Segel, I.H.1
  • 46
    • 48249108462 scopus 로고    scopus 로고
    • Unique rotary ATP synthase and its biological diversity
    • C. Von Ballmoos, G.M. Cook, and P. Dimroth Unique rotary ATP synthase and its biological diversity Ann. Rev. Biophys. 37 2008 43 64
    • (2008) Ann. Rev. Biophys. , vol.37 , pp. 43-64
    • Von Ballmoos, C.1    Cook, G.M.2    Dimroth, P.3
  • 47
    • 0018371450 scopus 로고
    • Inhibitors of the ATP synthase system
    • P.E. Limnett, and R.B. Beechey Inhibitors of the ATP synthase system Methods Enzymol. 55 1979 472 518
    • (1979) Methods Enzymol. , vol.55 , pp. 472-518
    • Limnett, P.E.1    Beechey, R.B.2
  • 49
    • 0027279864 scopus 로고
    • 0-ATPase of Propionigenium modestum from the reaction with dicyclohexylcarbodiimide
    • o-ATPase of Propionigenium modestum from the reaction with dicyclohexylcarbodiimide J. Biol. Chem. 268 1993 14557 14560 (Pubitemid 23206582)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.20 , pp. 14557-14560
    • Kluge, C.1    Dimroth, P.2
  • 51
    • 0028921917 scopus 로고
    • o-ATPase from Acetobacterium woodii - Probing the site(s) involved in ion-transport
    • o-ATPase from Acetobacterium woodii - probing the site(s) involved in ion-transport Biochim. Biophys. Acta 1229 1995 96 102
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 96-102
    • Spruth, M.1    Reidlinger, J.2    Muller, V.3
  • 52
    • 33644866074 scopus 로고    scopus 로고
    • The role of the ε subunit in the Escherichia coli ATP synthase: The C-terminal domain is required for efficient energy coupling
    • DOI 10.1074/jbc.M509986200
    • D.J. Cipriano, and S.D. Dunn The role of the ε subunit in the Escherichia coli ATP synthase. The C-terminal domain is required for efficient energy coupling J. Biol. Chem. 281 2006 501 507 (Pubitemid 43671213)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.1 , pp. 501-507
    • Cipriano, D.J.1    Dunn, S.D.2
  • 56
    • 16644375462 scopus 로고    scopus 로고
    • o motor of the sodium ATPase
    • DOI 10.1529/biophysj.104.042093
    • J. Xing, H. Wang, C. von Ballmoos, P. Dimroth, and G. Oster Torque generation by the Fo motor of the sodium ATPase Biophys. J. 87 2004 2148 2163 (Pubitemid 41071318)
    • (2004) Biophysical Journal , vol.87 , Issue.4 , pp. 2148-2163
    • Xing, J.1    Wang, H.2    Von Ballmoos, C.3    Dimroth, P.4    Oster, G.5


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