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Volumn 25, Issue 11, 2006, Pages 2643-2651

Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB

Author keywords

Autoinhibition; Bacterial acid resistance; Chloride binding; Glutamate decarboxylase; Pyridoxal 50 phosphate

Indexed keywords

ACETIC ACID; ACID; CARBOXYLYASE; CHLORIDE; GLUTAMATE DECARBOXYLASE; HALIDE; PROTON; PYRIDOXAL 5 PHOSPHATE;

EID: 33745752814     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7601107     Document Type: Article
Times cited : (88)

References (43)
  • 3
    • 0031959714 scopus 로고    scopus 로고
    • Ecological control of the gastrointestinal tract. The role of probiotic flora
    • Bengmark S (1998) Ecological control of the gastrointestinal tract. The role of probiotic flora. Gut 42: 2-7
    • (1998) Gut , vol.42 , pp. 2-7
    • Bengmark, S.1
  • 4
    • 0037162435 scopus 로고    scopus 로고
    • Spectroscopic and kinetic analyses reveal the pyridoxal 5′-phosphate binding mode and the catalytic features of Treponema denticola cystalysin
    • Bertoldi M, Cellini B, Clausen T, Voltattorni CB (2002) Spectroscopic and kinetic analyses reveal the pyridoxal 5′-phosphate binding mode and the catalytic features of Treponema denticola cystalysin. Biochemistry 41: 9153-9164
    • (2002) Biochemistry , vol.41 , pp. 9153-9164
    • Bertoldi, M.1    Cellini, B.2    Clausen, T.3    Voltattorni, C.B.4
  • 6
    • 0041465717 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase
    • Capitani G, De Biase D, Aurizi C, Gut H, Bossa F, Grutter MG (2003) Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase. EMBO J 22: 4027-4037
    • (2003) EMBO J , vol.22 , pp. 4027-4037
    • Capitani, G.1    De Biase, D.2    Aurizi, C.3    Gut, H.4    Bossa, F.5    Grutter, M.G.6
  • 8
    • 0035035812 scopus 로고    scopus 로고
    • A glutamate decarboxylase system protects Listeria monocytogenes in gastric fluid
    • Cotter PD, Gahan CG, Hill C (2001) A glutamate decarboxylase system protects Listeria monocytogenes in gastric fluid. Mol Microbiol 40: 465-475
    • (2001) Mol Microbiol , vol.40 , pp. 465-475
    • Cotter, P.D.1    Gahan, C.G.2    Hill, C.3
  • 9
    • 0033037702 scopus 로고    scopus 로고
    • The response to stationary-phase stress conditions in Escherichia coli: Role and regulation of the glutamic acid decarboxylase system
    • De Biase D, Tramonti A, Bossa F, Visca P (1999) The response to stationary-phase stress conditions in Escherichia coli: role and regulation of the glutamic acid decarboxylase system. Mol Microbiol 32: 1198-1211
    • (1999) Mol Microbiol , vol.32 , pp. 1198-1211
    • De Biase, D.1    Tramonti, A.2    Bossa, F.3    Visca, P.4
  • 10
    • 0030470440 scopus 로고    scopus 로고
    • Isolation, overexpression, and biochemical characterization of the two isoforms of glutamic acid decarboxylase from Escherichia coli
    • De Biase D, Tramonti A, John RA, Bossa F (1996) Isolation, overexpression, and biochemical characterization of the two isoforms of glutamic acid decarboxylase from Escherichia coli. Protein Expr Purif 8: 430-438
    • (1996) Protein Expr Purif , vol.8 , pp. 430-438
    • De Biase, D.1    Tramonti, A.2    John, R.A.3    Bossa, F.4
  • 12
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 a reveals the molecular basis of anion selectivity
    • Dutzler R, Campbell EB, Cadene M, Chait BT, MacKinnon R (2002) X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature 415: 287-294
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 13
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler R, Campbell EB, MacKinnon R (2003) Gating the selectivity filter in ClC chloride channels. Science 300: 108-112
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 14
    • 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
  • 15
    • 0015319397 scopus 로고
    • Gastric acid barrier to ingested microorganisms in man: Studies in vivo and in vitro
    • Giannella RA, Broitmann SA, Zamcheck N (1972) Gastric acid barrier to ingested microorganisms in man: studies in vivo and in vitro. Gut 13: 251-256
    • (1972) Gut , vol.13 , pp. 251-256
    • Giannella, R.A.1    Broitmann, S.A.2    Zamcheck, N.3
  • 16
    • 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
  • 17
    • 0031058883 scopus 로고    scopus 로고
    • Phase determination from multiwavelength anomalous diffraction measurements
    • Hendrickson WA, Ogata CM (1997) Phase determination from multiwavelength anomalous diffraction measurements. In Macromolecular Crystallography, Part A, Vol. 276, pp 494-523
    • (1997) Macromolecular Crystallography , vol.276 , Issue.PART A , pp. 494-523
    • Hendrickson, W.A.1    Ogata, C.M.2
  • 19
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of the molecules of haemoglobin on its oxygen dissociation curve
    • Hill AV (1910) The possible effects of the aggregation of the molecules of haemoglobin on its oxygen dissociation curve. J Physiol (London) 40: 4-7
    • (1910) J Physiol (London) , vol.40 , pp. 4-7
    • Hill, A.V.1
  • 21
    • 34247513828 scopus 로고
    • Zur Lehre von der Wirkung der Salze. II
    • Hofmeister F (1888) Zur Lehre von der Wirkung der Salze. II. Arch Exp Pathol Pharmakol 24: 247-260
    • (1888) Arch Exp Pathol Pharmakol , vol.24 , pp. 247-260
    • Hofmeister, F.1
  • 22
    • 0032478296 scopus 로고    scopus 로고
    • Analysis of the pH- and ligand-induced spectral transitions of tryptophanase: Activation of the coenzyme at the early steps of the catalytic cycle
    • Ikushiro H, Hayashi H, Kawata Y, Kagamiyama H (1998) Analysis of the pH- and ligand-induced spectral transitions of tryptophanase: activation of the coenzyme at the early steps of the catalytic cycle. Biochemistry 37: 3043-3052
    • (1998) Biochemistry , vol.37 , pp. 3043-3052
    • Ikushiro, H.1    Hayashi, H.2    Kawata, Y.3    Kagamiyama, H.4
  • 23
    • 0037126294 scopus 로고    scopus 로고
    • A biological role for prokaryotic ClC chloride channels
    • Iyer R, Iverson TM, Accardi A, Miller C (2002) A biological role for prokaryotic ClC chloride channels. Nature 419: 715-718
    • (2002) Nature , vol.419 , pp. 715-718
    • Iyer, R.1    Iverson, T.M.2    Accardi, A.3    Miller, C.4
  • 24
    • 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
  • 25
    • 0035029389 scopus 로고    scopus 로고
    • Sodium chloride enhances recovery and growth of acid-stressed E. coli O157:H7
    • Jordan KN, Davies KW (2001) Sodium chloride enhances recovery and growth of acid-stressed E. coli O157:H7. Lett Appl Microbiol 32: 312-315
    • (2001) Lett Appl Microbiol , vol.32 , pp. 312-315
    • Jordan, K.N.1    Davies, K.W.2
  • 26
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallog 26: 795-800
    • (1993) J Appl Crystallog , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 27
    • 0029073161 scopus 로고
    • Comparative analysis of extreme acid survival in Salmonella typhimurium, Shigella flexneri, and Escherichia coli
    • Lin J, Lee IS, Frey J, Slonczewski JL, Foster JW (1995) Comparative analysis of extreme acid survival in Salmonella typhimurium, Shigella flexneri, and Escherichia coli. J Bacteriol 177: 4097-4104
    • (1995) J Bacteriol , vol.177 , pp. 4097-4104
    • Lin, J.1    Lee, I.S.2    Frey, J.3    Slonczewski, J.L.4    Foster, J.W.5
  • 29
    • 0032617914 scopus 로고    scopus 로고
    • pH homeostasis in acidophiles
    • Matin A (1999) pH homeostasis in acidophiles. Novartis Found Symp 221: 152-163; discussion 163-156
    • (1999) Novartis Found Symp , vol.221 , pp. 152-163
    • Matin, A.1
  • 30
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr A 50: 157
    • (1994) Acta Crystallogr A , vol.50 , pp. 157
    • Navaza, J.1
  • 31
    • 0015233910 scopus 로고
    • A proposed structure for the 330-nm chromophore of glutamate decarboxylase and other pyridoxal 5′-phosphate dependent enzymes
    • O'Leary MH (1971) A proposed structure for the 330-nm chromophore of glutamate decarboxylase and other pyridoxal 5′-phosphate dependent enzymes. Biochim Biophys Acta 242: 484-492
    • (1971) Biochim Biophys Acta , vol.242 , pp. 484-492
    • O'Leary, M.H.1
  • 32
    • 0016161063 scopus 로고
    • pH jump studies of glutamate decarboxylase. Evidence for a pH-dependent conformation change
    • O'Leary MH, Brummund Jr W (1974) pH jump studies of glutamate decarboxylase. Evidence for a pH-dependent conformation change. J Biol Chem 249: 3737-3745
    • (1974) J Biol Chem , vol.249 , pp. 3737-3745
    • O'Leary, M.H.1    Brummund Jr., W.2
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter CW and Sweet RM (eds) New York: Academic Press
    • Otwinowski Z, Minor W (1996) Processing of X-ray diffraction data collected in oscillation mode. In: Carter CW and Sweet RM (eds) Meth Enzymol Macromolecular Crystallography. Vol. 276, pp 307-326. New York: Academic Press
    • (1996) Meth Enzymol Macromolecular Crystallography , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5
    • Picollo A, Pusch M (2005) Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature 436: 420-423
    • (2005) Nature , vol.436 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 35
    • 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
  • 36
  • 37
    • 22944479662 scopus 로고    scopus 로고
    • Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins
    • Scheel O, Zdebik AA, Lourdel S, Jentsch TJ (2005) Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins. Nature 436: 424-427
    • (2005) Nature , vol.436 , pp. 424-427
    • Scheel, O.1    Zdebik, A.A.2    Lourdel, S.3    Jentsch, T.J.4
  • 38
    • 72849170954 scopus 로고
    • Glutamic acid decarboxylase. 1. Isolation procedures and properties of the enzyme
    • Shukuya R, Schwert GW (1960a) Glutamic acid decarboxylase. 1. Isolation procedures and properties of the enzyme. J Biol Chem 235: 1649-1652
    • (1960) J Biol Chem , vol.235 , pp. 1649-1652
    • Shukuya, R.1    Schwert, G.W.2
  • 39
    • 72849177700 scopus 로고
    • Glutamic acid decarboxylase. 2. Spectrum of the enzyme
    • Shukuya R, Schwert GW (1960b) Glutamic acid decarboxylase. 2. Spectrum of the enzyme. J Biol Chem 235: 1653-1657
    • (1960) J Biol Chem , vol.235 , pp. 1653-1657
    • Shukuya, R.1    Schwert, G.W.2
  • 42
    • 0036411892 scopus 로고    scopus 로고
    • Contribution of Lys276 to the conformational flexibility of the active site of glutamate decarboxylase from Escherichia coli
    • Tramonti A, John RA, Bossa F, De Biase D (2002) Contribution of Lys276 to the conformational flexibility of the active site of glutamate decarboxylase from Escherichia coli. Eur J Biochem 269: 4913-4920
    • (2002) Eur J Biochem , vol.269 , pp. 4913-4920
    • Tramonti, A.1    John, R.A.2    Bossa, F.3    De Biase, D.4
  • 43
    • 17744379377 scopus 로고    scopus 로고
    • Conversion of 5-aminole-vulinate synthase into a more active enzyme by linking the two subunits: Spectroscopic and kinetic properties
    • Zhang J, Cheltsov AV, Ferreira GC (2005) Conversion of 5-aminole-vulinate synthase into a more active enzyme by linking the two subunits: spectroscopic and kinetic properties. Protein Sci 14: 1190-1200
    • (2005) Protein Sci , vol.14 , pp. 1190-1200
    • Zhang, J.1    Cheltsov, A.V.2    Ferreira, G.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.