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Volumn 193, Issue 8, 2011, Pages 2046-2052

The regulatory C-terminal domain of subunit ε of FoF1 ATP synthase is dispensable for growth and survival of Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 79955457931     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01422-10     Document Type: Note
Times cited : (17)

References (54)
  • 1
    • 77957093882 scopus 로고    scopus 로고
    • The Kdp-ATPase of Escherichia coli
    • A. G. Lee (ed.), JAI press Inc., Greenwich, CT
    • Altendorf, K., and W. Epstein. 1996. The Kdp-ATPase of Escherichia coli, p. 403-420. In A. G. Lee (ed.), Biomembranes. JAI press Inc., Greenwich, CT.
    • (1996) Biomembranes , pp. 403-420
    • Altendorf, K.1    Epstein, W.2
  • 2
    • 0015451273 scopus 로고
    • Pedigrees of some mutant strains of Escherichia coli K-12
    • Bachmann, B. J. 1972. Pedigrees of some mutant strains of Escherichia coli K-12. Bacteriol. Rev. 36:525-557.
    • (1972) Bacteriol. Rev. , vol.36 , pp. 525-557
    • Bachmann, B.J.1
  • 3
    • 0022349278 scopus 로고
    • Regulation of cytoplasmic pH in bacteria
    • Booth, I. R. 1985. Regulation of cytoplasmic pH in bacteria. Microbiol. Rev. 49:359-378.
    • (1985) Microbiol. Rev. , vol.49 , pp. 359-378
    • Booth, I.R.1
  • 4
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase-a splendid molecular machine
    • Boyer, P. D. 1997. The ATP synthase-a splendid molecular machine. Annu. Rev. Biochem. 66:717-749.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 5
    • 0036496185 scopus 로고    scopus 로고
    • Mechanism of the F1F0-type ATP synthase, a biological rotary motor
    • Capaldi, R. A., and R. Aggeler. 2002. Mechanism of the F1F0-type ATP synthase, a biological rotary motor. Trends Biochem. Sci. 27:154-160.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 154-160
    • Capaldi, R.A.1    Aggeler, R.2
  • 6
    • 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
    • Cipriano, D. J., and S. D. Dunn. 2006. 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. 281:501-507.
    • (2006) J. Biol. Chem. , vol.281 , pp. 501-507
    • Cipriano, D.J.1    Dunn, S.D.2
  • 7
    • 0028241256 scopus 로고
    • Energy-spilling reactions of Streptococcus bovis and resistance of its membrane to proton conductance
    • Cook, G. M., and J. B. Russell. 1994. Energy-spilling reactions of Streptococcus bovis and resistance of its membrane to proton conductance. Appl. Environ. Microbiol. 60:1942-1948.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1942-1948
    • Cook, G.M.1    Russell, J.B.2
  • 8
    • 56449116785 scopus 로고    scopus 로고
    • Intrinsic uncoupling in the ATP synthase of Escherichia coli
    • D'Alessandro, M., P. Turina, and B. A. Melandri. 2008. Intrinsic uncoupling in the ATP synthase of Escherichia coli. Biochim. Biophys. Acta 1777:1518-1527.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1518-1527
    • D'Alessandro, M.1    Turina, P.2    Melandri, B.A.3
  • 9
    • 0025323480 scopus 로고
    • Activation of Escherichia coli F1-ATPase by lauryldimethylamine oxide and ethylene glycol: relationship of ATPase activity to the interaction of the ε and β subunits
    • Dunn, S. D., R. G. Tozer, and V. D. Zadorozny. 1990. Activation of Escherichia coli F1-ATPase by lauryldimethylamine oxide and ethylene glycol: relationship of ATPase activity to the interaction of the ε and β subunits. Biochemistry 29:4335-4340.
    • (1990) Biochemistry , vol.29 , pp. 4335-4340
    • Dunn, S.D.1    Tozer, R.G.2    Zadorozny, V.D.3
  • 16
    • 0030610598 scopus 로고    scopus 로고
    • 1-ATPase is activated without dissociation of an endogenous inhibitor ε subunit
    • 1-ATPase is activated without dissociation of an endogenous inhibitor, ε subunit. J. Biol. Chem. 272:24906-24912.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24906-24912
    • Kato, Y.1
  • 17
    • 28844477927 scopus 로고    scopus 로고
    • 1-ATPase binds ATP
    • 1-ATPase binds ATP. FEBS Lett. 579:6875-6878.
    • (2005) FEBS Lett , vol.579 , pp. 6875-6878
    • Kato-Yamada, Y.1
  • 21
    • 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. Brusilow, and R. 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.2    Simoni, R.3
  • 24
    • 0001546971 scopus 로고
    • Firefly assay of adenine nucleotides from algae: comparison of extraction methods
    • Larsson, C. M., and T. Olsson. 1979. Firefly assay of adenine nucleotides from algae: comparison of extraction methods. Plant Cell Physiol. 20:145-155.
    • (1979) Plant Cell Physiol , vol.20 , pp. 145-155
    • Larsson, C.M.1    Olsson, T.2
  • 25
    • 0021772486 scopus 로고
    • 1 by the detergent lauryldimethylamine oxide
    • 1 by the detergent lauryldimethylamine oxide. Biochemistry 23:4140-4143.
    • (1984) Biochemistry , vol.23 , pp. 4140-4143
    • Lotscher, H.1    Capaldi, R.A.2
  • 26
    • 0016791330 scopus 로고
    • Comparison of methods for extraction of bacterial adenine nucleotides determined by firefly assay
    • Lundin, A., and A. Thore. 1975. Comparison of methods for extraction of bacterial adenine nucleotides determined by firefly assay. Appl. Microbiol. 30:713-721.
    • (1975) Appl. Microbiol. , vol.30 , pp. 713-721
    • Lundin, A.1    Thore, A.2
  • 28
    • 0025855423 scopus 로고
    • Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the ε subunit in Escherichia coli adenosinetriphosphatase
    • Mendel-Hartvig, J., and R. A. Capaldi. 1991. Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the ε subunit in Escherichia coli adenosinetriphosphatase. Biochemistry 30:1278-1284.
    • (1991) Biochemistry , vol.30 , pp. 1278-1284
    • Mendel-Hartvig, J.1    Capaldi, R.A.2
  • 29
    • 0030043465 scopus 로고    scopus 로고
    • Conditionally replicative and conjugative plasmids carrying lacZα for cloning, mutagenesis, and allele replacement in bacteria
    • Metcalf, W. W., et al. 1996. Conditionally replicative and conjugative plasmids carrying lacZα for cloning, mutagenesis, and allele replacement in bacteria. Plasmid 35:1-13.
    • (1996) Plasmid , vol.35 , pp. 1-13
    • Metcalf, W.W.1
  • 30
    • 0023892552 scopus 로고
    • A novel suicide vector and its use in construction of insertion mutations: osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR
    • Miller, V. L., and J. J. Mekalanos. 1988. A novel suicide vector and its use in construction of insertion mutations: osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR. J. Bacteriol. 170:2575-2583.
    • (1988) J. Bacteriol. , vol.170 , pp. 2575-2583
    • Miller, V.L.1    Mekalanos, J.J.2
  • 33
    • 0026662710 scopus 로고
    • An improved suicide vector for construction of chromosomal insertion mutations in bacteria
    • Penfold, R. J., and J. M. Pemberton. 1992. An improved suicide vector for construction of chromosomal insertion mutations in bacteria. Gene 118:145-146.
    • (1992) Gene , vol.118 , pp. 145-146
    • Penfold, R.J.1    Pemberton, J.M.2
  • 34
    • 0033623349 scopus 로고    scopus 로고
    • Structure of the γ-ε complex of ATP synthase
    • Rodgers, A. J., and M. C. Wilce. 2000. Structure of the γ-ε complex of ATP synthase. Nat. Struct. Biol. 7:1051-1054.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1051-1054
    • Rodgers, A.J.1    Wilce, M.C.2
  • 35
    • 0028926047 scopus 로고
    • Energetics of bacterial growth: balance of anabolic and catabolic reactions
    • Russell, J. B., and G. M. Cook. 1995. Energetics of bacterial growth: balance of anabolic and catabolic reactions. Microbiol. Rev. 59:48-62.
    • (1995) Microbiol. Rev. , vol.59 , pp. 48-62
    • Russell, J.B.1    Cook, G.M.2
  • 38
    • 77953298121 scopus 로고    scopus 로고
    • Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism
    • Shepherd, M., G. Sanguinetti, G. M. Cook, and R. K. Poole. 2010. Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism. J. Biol. Chem. 285:18464-18472.
    • (2010) J. Biol. Chem. , vol.285 , pp. 18464-18472
    • Shepherd, M.1    Sanguinetti, G.2    Cook, G.M.3    Poole, R.K.4
  • 39
    • 0027179864 scopus 로고
    • Location of conserved residue histidine-38 of the ε subunit of Escherichia coli ATP synthase
    • Skakoon, E. N., and S. D. Dunn. 1993. Location of conserved residue histidine-38 of the ε subunit of Escherichia coli ATP synthase. Arch. Biochem. Biophys. 302:272-278.
    • (1993) Arch. Biochem. Biophys. , vol.302 , pp. 272-278
    • Skakoon, E.N.1    Dunn, S.D.2
  • 40
    • 0037066772 scopus 로고    scopus 로고
    • 0 of ATP synthase is a rotary proton channel: obligatory coupling of proton translocation with rotation of c-subunit ring
    • 0 of ATP synthase is a rotary proton channel: obligatory coupling of proton translocation with rotation of c-subunit ring. J. Biol. Chem. 277:13281-13285.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13281-13285
    • Suzuki, T.1    Ueno, H.2    Mitome, N.3    Suzuki, J.4    Yoshida, M.5
  • 42
    • 0345306622 scopus 로고    scopus 로고
    • 1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of ε subunit in response to proton motive force and ADP/ATP balance
    • 1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of ε subunit in response to proton motive force and ADP/ATP balance. J. Biol. Chem. 278:46840-46846.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46840-46846
    • Suzuki, T.1
  • 44
    • 0023571657 scopus 로고
    • High-copy-number and low-copy-number plasmid vectors for lacZα-complementation and chloramphenicol- or kanamycin-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- or kanamycin-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
  • 45
    • 0006010204 scopus 로고
    • A correction in the nucleotide sequence of the Tn903 kanamycin resistance determinant in pUC4K
    • Taylor, L. A., and R. E. Rose. 1988. A correction in the nucleotide sequence of the Tn903 kanamycin resistance determinant in pUC4K. Nucleic Acids Res. 16:358.
    • (1988) Nucleic Acids Res , vol.16 , pp. 358
    • Taylor, L.A.1    Rose, R.E.2
  • 46
    • 0030611634 scopus 로고    scopus 로고
    • Crystal structure of the ε subunit of the proton-translocating ATP synthase from Escherichia coli
    • Uhlin, U., G. B. Cox, and J. M. Guss. 1997. Crystal structure of the ε subunit of the proton-translocating ATP synthase from Escherichia coli. Structure 5:1219-1230.
    • (1997) Structure , vol.5 , pp. 1219-1230
    • Uhlin, U.1    Cox, G.B.2    Guss, J.M.3
  • 47
    • 0028970620 scopus 로고
    • Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy
    • Wilkens, S., F. W. Dahlquist, L. P. McIntosh, L. W. Donaldson, and R. A. Capaldi. 1995. Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Nat. Struct. Biol. 2:961-967.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 961-967
    • Wilkens, S.1    Dahlquist, F.W.2    McIntosh, L.P.3    Donaldson, L.W.4    Capaldi, R.A.5
  • 48
    • 0032500380 scopus 로고    scopus 로고
    • 1-ATPase from Escherichia coli and interactions of this subunit with β subunits in the complex
    • 1-ATPase from Escherichia coli and interactions of this subunit with β subunits in the complex. J. Biol. Chem. 273:26645-26651.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26645-26651
    • Wilkens, S.1    Capaldi, R.A.2
  • 49
    • 0032541944 scopus 로고    scopus 로고
    • Subunit ε of the Escherichia coli ATP synthase: novel insights into structure and function by analysis of thirteen mutant forms
    • Xiong, H., D. Zhang, and S. B. Vik. 1998. Subunit ε of the Escherichia coli ATP synthase: novel insights into structure and function by analysis of thirteen mutant forms. Biochemistry 37:16423-16429.
    • (1998) Biochemistry , vol.37 , pp. 16423-16429
    • Xiong, H.1    Zhang, D.2    Vik, S.B.3
  • 51
    • 0017579462 scopus 로고
    • Reconstitution of thermostable ATPase capable of energy coupling from its purified subunits
    • Yoshida, M. 1977. Reconstitution of thermostable ATPase capable of energy coupling from its purified subunits. Proc. Natl. Acad. Sci. U. S. A. 74:936-940.
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , pp. 936-940
    • Yoshida, M.1
  • 53
    • 0021100485 scopus 로고
    • 1-ATPase from the thermophilic bacterium, PS3, with dicyclohexylcarbodiimide
    • 1-ATPase from the thermophilic bacterium, PS3, with dicyclohexylcarbodiimide. J. Biol. Chem. 258:14407-14412.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14407-14412
    • Yoshida, M.1    Allison, W.S.2
  • 54
    • 0018796271 scopus 로고
    • Proton electrochemical gradient in Escherichia coli cells and its relation to active transport of lactose
    • Zilberstein, D., S. Schuldiner, and E. Padan. 1979. Proton electrochemical gradient in Escherichia coli cells and its relation to active transport of lactose. Biochemistry 18:669-673.
    • (1979) Biochemistry , vol.18 , pp. 669-673
    • Zilberstein, D.1    Schuldiner, S.2    Padan, E.3


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