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Volumn 7, Issue 12, 2012, Pages

Respiration and the F1Fo-ATPase Enhance Survival under Acidic Conditions in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; GLUTAMATE 1 SEMIALDEHYDE; GLUTAMIC ACID; GLUTAMIC ACID TRANSFER RNA; PHOSPHATE; PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCLASSIFIED DRUG;

EID: 84871677534     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0052577     Document Type: Article
Times cited : (40)

References (39)
  • 1
    • 9444285788 scopus 로고    scopus 로고
    • Escherichia coli acid resistance: tales of an amateur acidophile
    • Foster JW, (2004) Escherichia coli acid resistance: tales of an amateur acidophile. Nat Rev Microbiol 2: 898-907.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 898-907
    • Foster, J.W.1
  • 4
    • 4444226939 scopus 로고    scopus 로고
    • Escherichia coli glutamate- and arginine-dependent acid resistance systems increase internal pH and reverse transmembrane potential
    • Richard H, Foster JW, (2004) Escherichia coli glutamate- and arginine-dependent acid resistance systems increase internal pH and reverse transmembrane potential. J Bacteriol 186: 6032-6041.
    • (2004) J Bacteriol , vol.186 , pp. 6032-6041
    • Richard, H.1    Foster, J.W.2
  • 5
    • 0038782170 scopus 로고    scopus 로고
    • YjdE (AdiC) is the arginine:agmatine antiporter essential for arginine-dependent acid resistance in Escherichia coli
    • Gong S, Richard H, Foster JW, (2003) YjdE (AdiC) is the arginine:agmatine antiporter essential for arginine-dependent acid resistance in Escherichia coli. J Bacteriol 185: 4402-4409.
    • (2003) J Bacteriol , vol.185 , pp. 4402-4409
    • Gong, S.1    Richard, H.2    Foster, J.W.3
  • 6
    • 0242659209 scopus 로고    scopus 로고
    • Arginine-agmatine antiporter in extreme acid resistance in Escherichia coli
    • Iyer R, Williams C, Miller C, (2003) Arginine-agmatine antiporter in extreme acid resistance in Escherichia coli. J Bacteriol 185: 6556-6561.
    • (2003) J Bacteriol , vol.185 , pp. 6556-6561
    • Iyer, R.1    Williams, C.2    Miller, C.3
  • 7
    • 0026772547 scopus 로고
    • Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH
    • Meng SY, Bennett GN, (1992) Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH. J Bacteriol 174: 2659-2669.
    • (1992) J Bacteriol , vol.174 , pp. 2659-2669
    • Meng, S.Y.1    Bennett, G.N.2
  • 8
    • 0026772549 scopus 로고
    • Regulation of the Escherichia coli cad operon: location of a site required for acid induction
    • Meng SY, Bennett GN, (1992) Regulation of the Escherichia coli cad operon: location of a site required for acid induction. J Bacteriol 174: 2670-2678.
    • (1992) J Bacteriol , vol.174 , pp. 2670-2678
    • Meng, S.Y.1    Bennett, G.N.2
  • 9
  • 10
    • 84862789502 scopus 로고    scopus 로고
    • Adenosine deamination increases the survival under acidic conditions in Escherichia coli
    • Sun Y, Fukamachi T, Saito H, Kobayashi H, (2012) Adenosine deamination increases the survival under acidic conditions in Escherichia coli. J Appl Microbiol 112: 775-781.
    • (2012) J Appl Microbiol , vol.112 , pp. 775-781
    • Sun, Y.1    Fukamachi, T.2    Saito, H.3    Kobayashi, H.4
  • 11
    • 79958076326 scopus 로고    scopus 로고
    • ATP requirement for acidic resistance in Escherichia coli
    • Sun Y, Fukamachi T, Saito H, Kobayashi H, (2011) ATP requirement for acidic resistance in Escherichia coli. J Bacteriol 193: 3072-3077.
    • (2011) J Bacteriol , vol.193 , pp. 3072-3077
    • Sun, Y.1    Fukamachi, T.2    Saito, H.3    Kobayashi, H.4
  • 12
    • 0021682543 scopus 로고
    • Proton motive force is not obligatory for growth of Escherichia coli
    • Kinoshita N, Unemoto T, Kobayashi H, (1984) Proton motive force is not obligatory for growth of Escherichia coli. J Bacteriol 160: 1074-1077.
    • (1984) J Bacteriol , vol.160 , pp. 1074-1077
    • Kinoshita, N.1    Unemoto, T.2    Kobayashi, H.3
  • 13
    • 0021990909 scopus 로고
    • A proton-translocating ATPase regulates pH of the bacterial cytoplasm
    • Kobayashi H, (1985) A proton-translocating ATPase regulates pH of the bacterial cytoplasm. J Biol Chem 260: 72-76.
    • (1985) J Biol Chem , vol.260 , pp. 72-76
    • Kobayashi, H.1
  • 14
    • 0027251266 scopus 로고
    • The Escherichia coli K-12 "wild types" W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels
    • Jensen KF, (1993) The Escherichia coli K-12 "wild types" W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels. J Bacteriol 175: 3401-3407.
    • (1993) J Bacteriol , vol.175 , pp. 3401-3407
    • Jensen, K.F.1
  • 15
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL, (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 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 DJ, Brusilow WSA, Simoni RD, (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
  • 17
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: partial purification and some properties
    • Vogel HJ, Bonner DM, (1956) Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem 218: 97-106.
    • (1956) J Biol Chem , vol.218 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 18
    • 0028857775 scopus 로고
    • Acid adaptation of Escherichia coli O157:H7 increases survival in acidic foods
    • Leyer GJ, Wang LL, Johnson EA, (1995) Acid adaptation of Escherichia coli O157:H7 increases survival in acidic foods. Appl Environ Microbiol 61: 3752-3755.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3752-3755
    • Leyer, G.J.1    Wang, L.L.2    Johnson, E.A.3
  • 19
    • 0037330622 scopus 로고    scopus 로고
    • Global metabolite analysis: the influence of extraction methodology on metabolome profiles of Escherichia coli
    • Maharjan RP, Ferenci T, (2003) Global metabolite analysis: the influence of extraction methodology on metabolome profiles of Escherichia coli. Anal Biochem 313: 145-154.
    • (2003) Anal Biochem , vol.313 , pp. 145-154
    • Maharjan, R.P.1    Ferenci, T.2
  • 20
    • 0027909395 scopus 로고
    • In situ fermentation monitoring with recombinant firefly luciferase
    • Lasko DR, Wang DI, (1993) In situ fermentation monitoring with recombinant firefly luciferase. Biotechnol Bioeng 42: 30-36.
    • (1993) Biotechnol Bioeng , vol.42 , pp. 30-36
    • Lasko, D.R.1    Wang, D.I.2
  • 21
    • 0021783513 scopus 로고
    • The proton motive force in bacteria: a critical assessment of methods
    • Kashket ER, (1985) The proton motive force in bacteria: a critical assessment of methods. Annu Rev Microbiol 39: 219-242.
    • (1985) Annu Rev Microbiol , vol.39 , pp. 219-242
    • Kashket, E.R.1
  • 22
    • 0025837235 scopus 로고
    • One-step purification of Escherichia coli H+-ATPase (FOF1) and its reconstitution into liposomes with neurotransmitter transporters
    • Moriyama Y, Iwamoto A, Hanada H, Maeda M, Futai M, (1991) One-step purification of Escherichia coli H+-ATPase (FOF1) and its reconstitution into liposomes with neurotransmitter transporters. J Biol Chem 266: 22141-22146.
    • (1991) J Biol Chem , vol.266 , pp. 22141-22146
    • Moriyama, Y.1    Iwamoto, A.2    Hanada, H.3    Maeda, M.4    Futai, M.5
  • 23
    • 67650270097 scopus 로고    scopus 로고
    • The b subunits in the peripheral stalk of F1FO ATP synthase preferentially adopt an offset relationship
    • Claggett SB, O'Neil Plancher M, Dunn SD, Cain BD, (2009) The b subunits in the peripheral stalk of F1FO ATP synthase preferentially adopt an offset relationship. J Biol Chem 284: 16531-16540.
    • (2009) J Biol Chem , vol.284 , pp. 16531-16540
    • Claggett, S.B.1    O'Neil Plancher, M.2    Dunn, S.D.3    Cain, B.D.4
  • 24
    • 0015304036 scopus 로고
    • Membrane-bound adenosine triphosphatase of Escherichia coli. I. Partial purification and properties
    • Kobayashi H, Anraku Y, (1972) Membrane-bound adenosine triphosphatase of Escherichia coli. I. Partial purification and properties. J Biochem 71: 387-399.
    • (1972) J Biochem , vol.71 , pp. 387-399
    • Kobayashi, H.1    Anraku, Y.2
  • 25
    • 0023687516 scopus 로고
    • Novel streptococcal mutants defective in the regulation of H+-ATPase biosynthesis and in FO complex
    • Suzuki T, Unemoto T, Kobayashi H, (1988) Novel streptococcal mutants defective in the regulation of H+-ATPase biosynthesis and in FO complex. J Biol Chem 263: 11840-11843.
    • (1988) J Biol Chem , vol.263 , pp. 11840-11843
    • Suzuki, T.1    Unemoto, T.2    Kobayashi, H.3
  • 26
    • 0021144978 scopus 로고
    • The respiratory chains of Escherichia coli
    • Ingledew WJ, Poole RK, (1984) The respiratory chains of Escherichia coli. Microbiol Reviews 48(3): 222-271.
    • (1984) Microbiol Reviews , vol.48 , Issue.3 , pp. 222-271
    • Ingledew, W.J.1    Poole, R.K.2
  • 27
    • 0024977998 scopus 로고
    • Proton translocation by the F1FO-ATPase of Escherichia coli. Mutagenic analysis of the a subunit
    • Cain BD, Simoni RD, (1989) Proton translocation by the F1FO-ATPase of Escherichia coli. Mutagenic analysis of the a subunit. J Biol Chem 264: 3292-3300.
    • (1989) J Biol Chem , vol.264 , pp. 3292-3300
    • Cain, B.D.1    Simoni, R.D.2
  • 28
    • 33748752793 scopus 로고    scopus 로고
    • Lipid raft components cholesterol and sphingomyelin increase H+/OH- permeability of phosphatidylcholine membranes
    • Gensure RH, Zeidel ML, Hill WG, (2006) Lipid raft components cholesterol and sphingomyelin increase H+/OH- permeability of phosphatidylcholine membranes. Biochem J 398: 485-495.
    • (2006) Biochem J , vol.398 , pp. 485-495
    • Gensure, R.H.1    Zeidel, M.L.2    Hill, W.G.3
  • 29
    • 0034054685 scopus 로고    scopus 로고
    • Expression of outer membrane proteins in Escherichia coli growing at acid pH
    • Sato M, Machida K, Arikado E, Saito H, Kakegawa T, et al. (2000) Expression of outer membrane proteins in Escherichia coli growing at acid pH. Appl Environ Microbiol 66: 943-947.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 943-947
    • Sato, M.1    Machida, K.2    Arikado, E.3    Saito, H.4    Kakegawa, T.5
  • 30
    • 37749019788 scopus 로고    scopus 로고
    • Extracellular acidic environments induce phosphorylation of ZAP-70 in Jurkat T cells
    • Hirata S, Fukamachi T, Sakano H, Tarora A, Saito H, et al. (2008) Extracellular acidic environments induce phosphorylation of ZAP-70 in Jurkat T cells. Immunol Lett 115: 105-109.
    • (2008) Immunol Lett , vol.115 , pp. 105-109
    • Hirata, S.1    Fukamachi, T.2    Sakano, H.3    Tarora, A.4    Saito, H.5
  • 31
    • 50449147866 scopus 로고
    • Transduction of linked genetic characters of the host by bacteriophage P1
    • Lennox ES, (1955) Transduction of linked genetic characters of the host by bacteriophage P1. Virology 1: 190-206.
    • (1955) Virology , vol.1 , pp. 190-206
    • Lennox, E.S.1
  • 33
    • 0017063727 scopus 로고
    • The electrochemical gradient of protons and its relationship to active transport in Escherichia coli membrane vesicles
    • Ramos S, Schuldiner S, Kaback HR, (1976) The electrochemical gradient of protons and its relationship to active transport in Escherichia coli membrane vesicles. Proc Natl Acad Sci USA 73: 1892-1896.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 1892-1896
    • Ramos, S.1    Schuldiner, S.2    Kaback, H.R.3
  • 34
    • 0032576724 scopus 로고    scopus 로고
    • Energy transduction in ATP synthase
    • Elston T, Wang H, Oster G, (1998) Energy transduction in ATP synthase. Nature 391: 510-513.
    • (1998) Nature , vol.391 , pp. 510-513
    • Elston, T.1    Wang, H.2    Oster, G.3
  • 35
    • 0037415728 scopus 로고    scopus 로고
    • H+/ATP ratio of proton transport-coupled ATP synthesis and hydrolysis catalysed by CFOF1-liposomes
    • Turina P, Samoray D, Gräber P, (2003) H+/ATP ratio of proton transport-coupled ATP synthesis and hydrolysis catalysed by CFOF1-liposomes. EMBO J 22: 418-426.
    • (2003) EMBO J , vol.22 , pp. 418-426
    • Turina, P.1    Samoray, D.2    Gräber, P.3
  • 36
    • 64049091511 scopus 로고    scopus 로고
    • Constant c10 ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking
    • Ballhausen B, Altendorf K, Deckers-Hebestreit G, (2009) Constant c10 ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking. J Bacteriol 191: 2400-2404.
    • (2009) J Bacteriol , vol.191 , pp. 2400-2404
    • Ballhausen, B.1    Altendorf, K.2    Deckers-Hebestreit, G.3
  • 37
    • 0024371112 scopus 로고
    • Identification of the enzymatic basis for δ-aminolevulinic acid auxotrophy in a hemA mutant of Escherichia coli
    • Avissar YJ, Beale SI, (1989) Identification of the enzymatic basis for δ-aminolevulinic acid auxotrophy in a hemA mutant of Escherichia coli. J Bacteriol 171: 2919-2924.
    • (1989) J Bacteriol , vol.171 , pp. 2919-2924
    • Avissar, Y.J.1    Beale, S.I.2
  • 38
    • 0029787019 scopus 로고    scopus 로고
    • Expression of catalytically active barley glutamyl tRNAGlu reductase in Escherichia coli as a fusion protein with glutathione S-transferase
    • Vothknecht UC, Kannangara CG, Wettstein DV, (1996) Expression of catalytically active barley glutamyl tRNAGlu reductase in Escherichia coli as a fusion protein with glutathione S-transferase. Proc Natl Acad Sci USA 93: 9287-9291.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9287-9291
    • Vothknecht, U.C.1    Kannangara, C.G.2    Wettstein, D.V.3
  • 39
    • 20044396589 scopus 로고    scopus 로고
    • Carbon dioxide increases acid resistance in Escherichia coli
    • Sun L, Fukamachi T, Saito H, Kobayashi H, (2005) Carbon dioxide increases acid resistance in Escherichia coli. Lett Appl Microbiol 40: 397-400.
    • (2005) Lett Appl Microbiol , vol.40 , pp. 397-400
    • Sun, L.1    Fukamachi, T.2    Saito, H.3    Kobayashi, H.4


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