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Volumn 195, Issue 7, 2013, Pages 1446-1455

YfdW and YfdU are required for oxalate-induced acid tolerance in Escherichia coli K-12

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLYASE; COENZYME A TRANSFERASE; OXALIC ACID; PROTEIN YFDU; PROTEIN YFDW; UNCLASSIFIED DRUG;

EID: 84875485795     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01936-12     Document Type: Article
Times cited : (22)

References (77)
  • 1
    • 0028324804 scopus 로고
    • Acid and base resistance in Escherichia coli and Shigella flexneri: role of rpoS and growth pH
    • Small P, Blankenhorn D, Welty D, Zinser E, Slonczewski JL. 1994. Acid and base resistance in Escherichia coli and Shigella flexneri: role of rpoS and growth pH. J. Bacteriol. 176:1729 -1737.
    • (1994) J. Bacteriol. , vol.176 , pp. 1729-1737
    • Small, P.1    Blankenhorn, D.2    Welty, D.3    Zinser, E.4    Slonczewski, J.L.5
  • 2
    • 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
  • 4
    • 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
  • 6
    • 4444226939 scopus 로고    scopus 로고
    • Escherichia coli glutamate- and argininedependent acid resistance systems increase internal pH and reverse transmembrane potential
    • Richard H, Foster JW. 2004. Escherichia coli glutamate- and argininedependent 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
  • 7
    • 0036714331 scopus 로고    scopus 로고
    • Signal transduction and regulatory mechanisms involved in control of the sigma(S) (RpoS) subunit of RNA polymerase
    • Hengge-Aronis R. 2002. Signal transduction and regulatory mechanisms involved in control of the sigma(S) (RpoS) subunit of RNA polymerase. Microbiol. Mol. Biol. Rev. 66:373-395.
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 373-395
    • Hengge-Aronis, R.1
  • 8
    • 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
  • 9
    • 77954313305 scopus 로고    scopus 로고
    • Acid stress response in Escherichia coli: mechanism of regulation of gadA transcription by RcsB and GadE
    • Castanie-Cornet MP, Cam K, Bastiat B, Cros A, Bordes P, Gutierrez C. 2010. Acid stress response in Escherichia coli: mechanism of regulation of gadA transcription by RcsB and GadE. Nucleic Acids Res. 38:3546 -3554.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 3546-3554
    • Castanie-cornet, M.P.1    Cam, K.2    Bastiat, B.3    Cros, A.4    Bordes, P.5    Gutierrez, C.6
  • 10
    • 0035086021 scopus 로고    scopus 로고
    • Escherichia coli acid resistance: cAMP receptor protein and a 20 bp cis-acting sequence control pH and stationary phase expression of the gadA and gadBC glutamate decarboxylase genes
    • Castanie-Cornet MP, Foster JW. 2001. Escherichia coli acid resistance: cAMP receptor protein and a 20 bp cis-acting sequence control pH and stationary phase expression of the gadA and gadBC glutamate decarboxylase genes. Microbiology 147:709 -715.
    • (2001) Microbiology , vol.147 , pp. 709-715
    • Castanie-cornet, M.P.1    Foster, J.W.2
  • 11
    • 6044275962 scopus 로고    scopus 로고
    • Characterization of EvgAS-YdeOGadE branched regulatory circuit governing glutamate-dependent acid resistance in Escherichia coli
    • Ma Z, Masuda N, Foster JW. 2004. Characterization of EvgAS-YdeOGadE branched regulatory circuit governing glutamate-dependent acid resistance in Escherichia coli. J. Bacteriol. 186:7378 -7389.
    • (2004) J. Bacteriol. , vol.186 , pp. 7378-7389
    • Ma, Z.1    Masuda, N.2    Foster, J.W.3
  • 12
    • 0036843687 scopus 로고    scopus 로고
    • Escherichia coli gene expression responsive to levels of the response regulator EvgA
    • Masuda N, Church GM. 2002. Escherichia coli gene expression responsive to levels of the response regulator EvgA. J. Bacteriol. 184:6225- 6234.
    • (2002) J. Bacteriol. , vol.184 , pp. 6225-6234
    • Masuda, N.1    Church, G.M.2
  • 13
    • 0038349356 scopus 로고    scopus 로고
    • Regulatory network of acid resistance genes in Escherichia coli
    • Masuda N, Church GM. 2003. Regulatory network of acid resistance genes in Escherichia coli. Mol. Microbiol. 48:699 -712.
    • (2003) Mol. Microbiol. , vol.48 , pp. 699-712
    • Masuda, N.1    Church, G.M.2
  • 14
    • 0036889029 scopus 로고    scopus 로고
    • Gene expression profiling of the pH response in Escherichia coli
    • Tucker DL, Tucker N, Conway T. 2002. Gene expression profiling of the pH response in Escherichia coli. J. Bacteriol. 184:6551- 6558.
    • (2002) J. Bacteriol. , vol.184 , pp. 6551-6558
    • Tucker, D.L.1    Tucker, N.2    Conway, T.3
  • 15
    • 0033573089 scopus 로고    scopus 로고
    • The Escherichia coli trmE (mnmE) gene, involved in tRNA modification, codes for an evolutionarily conserved GTPase with unusual biochemical properties
    • Cabedo H, Macian F, Villarroya M, Escudero JC, Martinez-Vicente M, Knecht E, Armengod ME. 1999. The Escherichia coli trmE (mnmE) gene, involved in tRNA modification, codes for an evolutionarily conserved GTPase with unusual biochemical properties. EMBO J. 18:7063-7076.
    • (1999) EMBO J. , vol.18 , pp. 7063-7076
    • Cabedo, H.1    Macian, F.2    Villarroya, M.3    Escudero, J.C.4    Martinez-vicente, M.5    Knecht, E.6    Armengod, M.E.7
  • 16
    • 54249135920 scopus 로고    scopus 로고
    • GadX/GadW-dependent regulation of the Escherichia coli acid fitness island: transcriptional control at the gadY-gadW divergent promoters and identification of four novel 42 bp GadX/GadW-specific binding sites
    • Tramonti A, De Canio M, De Biase D. 2008. GadX/GadW-dependent regulation of the Escherichia coli acid fitness island: transcriptional control at the gadY-gadW divergent promoters and identification of four novel 42 bp GadX/GadW-specific binding sites. Mol. Microbiol. 70:965-982.
    • (2008) Mol. Microbiol. , vol.70 , pp. 965-982
    • Tramonti, A.1    De Canio, M.2    De Biase, D.3
  • 17
    • 20444417420 scopus 로고    scopus 로고
    • Antagonistic role of H-NS and GadX in the regulation of the glutamate decarboxylase-dependent acid resistance system in Escherichia coli
    • Giangrossi M, Zattoni S, Tramonti A, De Biase D, Falconi M. 2005. Antagonistic role of H-NS and GadX in the regulation of the glutamate decarboxylase-dependent acid resistance system in Escherichia coli. J. Biol. Chem. 280:21498 -21505.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21498-21505
    • Giangrossi, M.1    Zattoni, S.2    Tramonti, A.3    De Biase, D.4    Falconi, M.5
  • 18
    • 33751555223 scopus 로고    scopus 로고
    • Mechanisms of transcription activation exerted by GadX and GadW at the gadA and gadBC gene promoters of the glutamate-based acid resistance system in Escherichia coli
    • Tramonti A, De Canio M, Delany I, Scarlato V, De Biase D. 2006. Mechanisms of transcription activation exerted by GadX and GadW at the gadA and gadBC gene promoters of the glutamate-based acid resistance system in Escherichia coli. J. Bacteriol. 188:8118-8127.
    • (2006) J. Bacteriol. , vol.188 , pp. 8118-8127
    • Tramonti, A.1    De Canio, M.2    Delany, I.3    Scarlato, V.4    De Biase, D.5
  • 19
    • 0036237890 scopus 로고    scopus 로고
    • Functional characterization and regulation of gadX, a gene encoding an AraC/XylS-like transcriptional activator of the Escherichia coli glutamic acid decarboxylase system
    • Tramonti A, Visca P, De Canio M, Falconi M, De Biase D. 2002. Functional characterization and regulation of gadX, a gene encoding an AraC/XylS-like transcriptional activator of the Escherichia coli glutamic acid decarboxylase system. J. Bacteriol. 184:2603-2613.
    • (2002) J. Bacteriol. , vol.184 , pp. 2603-2613
    • Tramonti, A.1    Visca, P.2    De Canio, M.3    Falconi, M.4    De Biase, D.5
  • 20
    • 34547858215 scopus 로고    scopus 로고
    • The Escherichia coli AraC-family regulators GadX and GadW activate gadE, the central activator of glutamate- dependent acid resistance
    • Sayed AK, Odom C, Foster JW. 2007. The Escherichia coli AraC-family regulators GadX and GadW activate gadE, the central activator of glutamate- dependent acid resistance. Microbiology 153:2584 -2592.
    • (2007) Microbiology , vol.153 , pp. 2584-2592
    • Sayed, A.K.1    Odom, C.2    Foster, J.W.3
  • 21
    • 0021720525 scopus 로고
    • The effect of food preservatives on pH homeostasis in Escherichia coli
    • Salmond CV, Kroll RG, Booth IR. 1984. The effect of food preservatives on pH homeostasis in Escherichia coli. J. Gen. Microbiol. 130:2845-2850.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 2845-2850
    • Salmond, C.V.1    Kroll, R.G.2    Booth, I.R.3
  • 22
    • 16544391413 scopus 로고    scopus 로고
    • Weak organic acids: a panoply of effects on bacteria
    • Hirshfield IN, Terzulli S, O'Byrne C. 2003. Weak organic acids: a panoply of effects on bacteria. Sci. Prog. 86:245-269.
    • (2003) Sci. Prog. , vol.86 , pp. 245-269
    • Hirshfield, I.N.1    Terzulli, S.2    O'Byrne, C.3
  • 23
    • 0031882597 scopus 로고    scopus 로고
    • Perturbation of anion balance during inhibition of growth of Escherichia coli by weak acids
    • Roe AJ, McLaggan D, Davidson I, O'Byrne C, Booth IR. 1998. Perturbation of anion balance during inhibition of growth of Escherichia coli by weak acids. J. Bacteriol. 180:767-772.
    • (1998) J. Bacteriol. , vol.180 , pp. 767-772
    • Roe, A.J.1    McLaggan, D.2    Davidson, I.3    O'Byrne, C.4    Booth, I.R.5
  • 24
    • 0032452737 scopus 로고    scopus 로고
    • The effects of fermentation acids on bacterial growth
    • Russell JB, Diez-Gonzalez F. 1998. The effects of fermentation acids on bacterial growth. Adv. Microb. Physiol. 39:205-234.
    • (1998) Adv. Microb. Physiol. , vol.39 , pp. 205-234
    • Russell, J.B.1    Diez-gonzalez, F.2
  • 25
    • 58649111284 scopus 로고    scopus 로고
    • External concentration of organic acid anions and pH: key independent variables for studying how organic acids inhibit growth of bacteria in mildly acidic foods
    • doi:10.1111/j.1750-3841.2008.00994.x
    • Carpenter CE, Broadbent JR. 2009. External concentration of organic acid anions and pH: key independent variables for studying how organic acids inhibit growth of bacteria in mildly acidic foods. J. Food Sci. 74:R12- R15. doi:10.1111/j.1750-3841.2008.00994.x.
    • (2009) J. Food Sci. , vol.74
    • Carpenter, C.E.1    Broadbent, J.R.2
  • 26
    • 0024330203 scopus 로고
    • Resistance of acid-habituated Escherichia coli to organic acids and its medical and applied significance
    • Goodson M, Rowbury RJ. 1989. Resistance of acid-habituated Escherichia coli to organic acids and its medical and applied significance. Lett. Appl. Microbiol. 8:211-214.
    • (1989) Lett. Appl. Microbiol. , vol.8 , pp. 211-214
    • Goodson, M.1    Rowbury, R.J.2
  • 27
    • 0029886938 scopus 로고    scopus 로고
    • The survival benefit of short-chain organic acids and the inducible arginine and lysine decarboxylase genes for Escherichia coli
    • Guilfoyle DE, Hirshfield IN. 1996. The survival benefit of short-chain organic acids and the inducible arginine and lysine decarboxylase genes for Escherichia coli. Lett. Appl. Microbiol. 22:393-396.
    • (1996) Lett. Appl. Microbiol. , vol.22 , pp. 393-396
    • Guilfoyle, D.E.1    Hirshfield, I.N.2
  • 28
    • 0031717130 scopus 로고    scopus 로고
    • Induction of acid resistance of Salmonella typhimurium by exposure to short-chain fatty acids
    • Kwon YM, Ricke SC. 1998. Induction of acid resistance of Salmonella typhimurium by exposure to short-chain fatty acids. Appl. Environ. Microbiol. 64:3458 -3463.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3458-3463
    • Kwon, Y.M.1    Ricke, S.C.2
  • 29
    • 0029959309 scopus 로고    scopus 로고
    • The acid tolerance response of Salmonella typhimurium provides protection against organic acids
    • Baik HS, Bearson S, Dunbar S, Foster JW. 1996. The acid tolerance response of Salmonella typhimurium provides protection against organic acids. Microbiology 142(Part 11):3195-3200.
    • (1996) Microbiology , vol.142 , Issue.PART 11 , pp. 3195-3200
    • Baik, H.S.1    Bearson, S.2    Dunbar, S.3    Foster, J.W.4
  • 30
    • 0026710387 scopus 로고
    • Regulation of katF and katE in Escherichia coli K-12 by weak acids
    • Schellhorn HE, Stones VL. 1992. Regulation of katF and katE in Escherichia coli K-12 by weak acids. J. Bacteriol. 174:4769-4776.
    • (1992) J. Bacteriol. , vol.174 , pp. 4769-4776
    • Schellhorn, H.E.1    Stones, V.L.2
  • 31
    • 0035088098 scopus 로고    scopus 로고
    • Global analysis of Escherichia coli gene expression during the acetate-induced acid tolerance response
    • Arnold CN, McElhanon J, Lee A, Leonhart R, Siegele DA. 2001. Global analysis of Escherichia coli gene expression during the acetate-induced acid tolerance response. J. Bacteriol. 183:2178 -2186.
    • (2001) J. Bacteriol. , vol.183 , pp. 2178-2186
    • Arnold, C.N.1    McElhanon, J.2    Lee, A.3    Leonhart, R.4    Siegele, D.A.5
  • 37
    • 0000889768 scopus 로고
    • Oxidation of glyoxylic acid to oxalic acid by glycolic acid oxidase
    • Richardson K, Tolbert NE. 1961. Oxidation of glyoxylic acid to oxalic acid by glycolic acid oxidase. J. Biol. Chem. 236:1280 -1284.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1280-1284
    • Richardson, K.1    Tolbert, N.E.2
  • 38
    • 0011186629 scopus 로고
    • Photosynthetic production of oxalic acid in Oxalis corniculata
    • Seal SN, Sen SP. 1970. Photosynthetic production of oxalic acid in Oxalis corniculata. Plant Cell Physiol. 11:119 -128.
    • (1970) Plant Cell Physiol. , vol.11 , pp. 119-128
    • Seal, S.N.1    Sen, S.P.2
  • 39
    • 0008806776 scopus 로고    scopus 로고
    • Glyoxylate synthesis, and its modulation and influence on oxalate synthesis
    • Holmes RP, Assimos DG. 1998. Glyoxylate synthesis, and its modulation and influence on oxalate synthesis. J. Urol. 160:1617-1624.
    • (1998) J. Urol. , vol.160 , pp. 1617-1624
    • Holmes, R.P.1    Assimos, D.G.2
  • 40
    • 35448997400 scopus 로고    scopus 로고
    • Oxalate consumption by lactobacilli: evaluation of oxalyl-CoA decarboxylase and formyl-CoA transferase activity in Lactobacillus acidophilus
    • Turroni S, Vitali B, Bendazzoli C, Candela M, Gotti R, Federici F, Pirovano F, Brigidi P. 2007. Oxalate consumption by lactobacilli: evaluation of oxalyl-CoA decarboxylase and formyl-CoA transferase activity in Lactobacillus acidophilus. J. Appl. Microbiol. 103:1600 -1609.
    • (2007) J. Appl. Microbiol. , vol.103 , pp. 1600-1609
    • Turroni, S.1    Vitali, B.2    Bendazzoli, C.3    Candela, M.4    Gotti, R.5    Federici, F.6    Pirovano, F.7    Brigidi, P.8
  • 41
    • 0021992519 scopus 로고
    • Oxalobacter formigenes gen. nov., sp. nov.: oxalate-degrading anaerobes that inhabit the gastrointestinal tract
    • Allison MJ, Dawson KA, Mayberry WR, Foss JG. 1985. Oxalobacter formigenes gen. nov., sp. nov.: oxalate-degrading anaerobes that inhabit the gastrointestinal tract. Arch. Microbiol. 141:1-7.
    • (1985) Arch. Microbiol. , vol.141 , pp. 1-7
    • Allison, M.J.1    Dawson, K.A.2    Mayberry, W.R.3    Foss, J.G.4
  • 42
    • 0019204930 scopus 로고
    • Characteristics of anaerobic oxalate-degrading enrichment cultures from the rumen
    • Dawson KA, Allison MJ, Hartman PA. 1980. Characteristics of anaerobic oxalate-degrading enrichment cultures from the rumen. Appl. Environ. Microbiol. 40:840-846.
    • (1980) Appl. Environ. Microbiol. , vol.40 , pp. 840-846
    • Dawson, K.A.1    Allison, M.J.2    Hartman, P.A.3
  • 43
    • 77954283084 scopus 로고    scopus 로고
    • Oxalate-degrading bacteria of the human gut as probiotics in the management of kidney stone disease
    • Abratt VR, Reid SJ. 2010. Oxalate-degrading bacteria of the human gut as probiotics in the management of kidney stone disease. Adv. Appl. Microbiol. 72:63- 87.
    • (2010) Adv. Appl. Microbiol. , vol.72 , pp. 63-87
    • Abratt, V.R.1    Reid, S.J.2
  • 44
    • 41549156949 scopus 로고    scopus 로고
    • Differential substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase
    • Toyota CG, Berthold CL, Gruez A, Jonsson S, Lindqvist Y, Cambillau C, Richards NG. 2008. Differential substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase. J. Bacteriol. 190:2556 -2564.
    • (2008) J. Bacteriol. , vol.190 , pp. 2556-2564
    • Toyota, C.G.1    Berthold, C.L.2    Gruez, A.3    Jonsson, S.4    Lindqvist, Y.5    Cambillau, C.6    Richards, N.G.7
  • 45
    • 84875548743 scopus 로고    scopus 로고
    • Oxalate metabolizing enzymes of Oxalobacter formigenes and Escherichia coli
    • University of Florida, Gainesville, FL
    • Toyota CG. 2008. Oxalate metabolizing enzymes of Oxalobacter formigenes and Escherichia coli. Ph.D. dissertation, University of Florida, Gainesville, FL.
    • (2008) Ph.D. dissertation
    • Toyota, C.G.1
  • 46
    • 77953207313 scopus 로고    scopus 로고
    • New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli
    • Werther T, Zimmer A, Wille G, Golbik R, Weiss MS, Konig S. 2010. New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli. FEBS J. 277:2628 -2640.
    • (2010) FEBS J. , vol.277 , pp. 2628-2640
    • Werther, T.1    Zimmer, A.2    Wille, G.3    Golbik, R.4    Weiss, M.S.5    Konig, S.6
  • 47
    • 0345862001 scopus 로고    scopus 로고
    • Oxalobacter formigenes and its role in oxalate metabolism in the human gut
    • Stewart CS, Duncan SH, Cave DR. 2004. Oxalobacter formigenes and its role in oxalate metabolism in the human gut. FEMS Microbiol. Lett. 230: 1-7.
    • (2004) FEMS Microbiol. Lett. , vol.230 , pp. 1-7
    • Stewart, C.S.1    Duncan, S.H.2    Cave, D.R.3
  • 48
    • 0024961965 scopus 로고
    • Oxalate:formate exchange. The basis for energy coupling in Oxalobacter
    • Anantharam V, Allison MJ, Maloney PC. 1989. Oxalate:formate exchange. The basis for energy coupling in Oxalobacter. J. Biol. Chem. 264: 7244-7250.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7244-7250
    • Anantharam, V.1    Allison, M.J.2    Maloney, P.C.3
  • 49
    • 4143147626 scopus 로고    scopus 로고
    • Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes
    • Jonsson S, Ricagno S, Lindqvist Y, Richards NG. 2004. Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes. J. Biol. Chem. 279:36003-36012.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36003-36012
    • Jonsson, S.1    Ricagno, S.2    Lindqvist, Y.3    Richards, N.G.4
  • 50
    • 0025294601 scopus 로고
    • Purification and characterization of formylcoenzyme A transferase from Oxalobacter formigenes
    • Baetz AL, Allison MJ. 1990. Purification and characterization of formylcoenzyme A transferase from Oxalobacter formigenes. J. Bacteriol. 172: 3537-3540.
    • (1990) J. Bacteriol. , vol.172 , pp. 3537-3540
    • Baetz, A.L.1    Allison, M.J.2
  • 51
    • 29244469942 scopus 로고    scopus 로고
    • Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl- CoA decarboxylase by adenosine diphosphate
    • Berthold CL, Moussatche P, Richards NG, Lindqvist Y. 2005. Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl- CoA decarboxylase by adenosine diphosphate. J. Biol. Chem. 280:41645- 41654.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41645-41654
    • Berthold, C.L.1    Moussatche, P.2    Richards, N.G.3    Lindqvist, Y.4
  • 52
    • 0024672742 scopus 로고
    • Purification and characterization of oxalylcoenzyme A decarboxylase from Oxalobacter formigenes
    • Baetz AL, Allison MJ. 1989. Purification and characterization of oxalylcoenzyme A decarboxylase from Oxalobacter formigenes. J. Bacteriol. 171: 2605-2608.
    • (1989) J. Bacteriol. , vol.171 , pp. 2605-2608
    • Baetz, A.L.1    Allison, M.J.2
  • 54
    • 33748651219 scopus 로고    scopus 로고
    • Analysis of substrate-binding elements in OxlT, the oxalate:formate antiporter of Oxalobacter formigenes
    • Wang X, Sarker RI, Maloney PC. 2006. Analysis of substrate-binding elements in OxlT, the oxalate:formate antiporter of Oxalobacter formigenes. Biochemistry 45:10344 -10350.
    • (2006) Biochemistry , vol.45 , pp. 10344-10350
    • Wang, X.1    Sarker, R.I.2    Maloney, P.C.3
  • 55
    • 0035145680 scopus 로고    scopus 로고
    • Overexpression of the response regulator evgA of the two-component signal transduction system modulates multi- drug resistance conferred by multidrug resistance transporters
    • Nishino K, Yamaguchi A. 2001. Overexpression of the response regulator evgA of the two-component signal transduction system modulates multi- drug resistance conferred by multidrug resistance transporters. J. Bacteriol. 183:1455-1458.
    • (2001) J. Bacteriol. , vol.183 , pp. 1455-1458
    • Nishino, K.1    Yamaguchi, A.2
  • 56
    • 77955954783 scopus 로고    scopus 로고
    • Oxalate-degrading activity in Bifidobacterium animalis subsp. lactis: impact of acidic conditions on the transcriptional levels of the oxalyl coenzyme A (CoA) decarboxylase and formyl-CoA transferase genes Appl
    • Turroni S, Bendazzoli C, Dipalo SC, Candela M, Vitali B, Gotti R, Brigidi P. 2010. Oxalate-degrading activity in Bifidobacterium animalis subsp. lactis: impact of acidic conditions on the transcriptional levels of the oxalyl coenzyme A (CoA) decarboxylase and formyl-CoA transferase genes. Appl. Environ. Microbiol. 76:5609 -5620.
    • (2010) Environ. Microbiol. , vol.76 , pp. 5609-5620
    • Turroni, S.1    Bendazzoli, C.2    Dipalo, S.C.3    Candela, M.4    Vitali, B.5    Gotti, R.6    Brigidi, P.7
  • 58
    • 0029917173 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression in Escherichia coli of OxlT, the oxalate:formate exchange protein of Oxalobacter formigenes
    • Abe K, Ruan ZS, Maloney PC. 1996. Cloning, sequencing, and expression in Escherichia coli of OxlT, the oxalate:formate exchange protein of Oxalobacter formigenes. J. Biol. Chem. 271:6789-6793.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6789-6793
    • Abe, K.1    Ruan, Z.S.2    Maloney, P.C.3
  • 59
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research
    • Kitagawa M, Ara T, Arifuzzaman M, Ioka-Nakamichi T, Inamoto E, Toyonaga H, Mori H. 2005. Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res. 12:291-299.
    • (2005) DNA Res. , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Ioka-Nakamichi, T.4    Inamoto, E.5    Toyonaga, H.6    Mori, H.7
  • 61
    • 0015385368 scopus 로고
    • Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA
    • U.S.A.
    • Cohen SN, Chang AC, Hsu L. 1972. Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA. Proc. Natl. Acad. Sci. U. S. A. 69:2110 -2114.
    • (1972) Proc. Natl. Acad. Sci. , vol.69 , pp. 2110-2114
    • Cohen, S.N.1    Chang, A.C.2    Hsu, L.3
  • 62
    • 0014945433 scopus 로고
    • Calcium-dependent bacteriophage DNA infection
    • Mandel M, Higa A. 1970. Calcium-dependent bacteriophage DNA infection. J. Mol. Biol. 53:159 -162.
    • (1970) J. Mol. Biol. , vol.53 , pp. 159-162
    • Mandel, M.1    Higa, A.2
  • 63
    • 0030994059 scopus 로고    scopus 로고
    • Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli
    • Hoenke S, Schmid M, Dimroth P. 1997. Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli. Eur. J. Biochem. 246:530 -538.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 530-538
    • Hoenke, S.1    Schmid, M.2    Dimroth, P.3
  • 64
    • 38949188903 scopus 로고    scopus 로고
    • In vitro methane emission and acetate:propionate ratio are decreased when artificial stimulation of the rumen wall is combined with increasing grain diets in sheep
    • Christophersen CT, Wright AD, Vercoe PE. 2008. In vitro methane emission and acetate:propionate ratio are decreased when artificial stimulation of the rumen wall is combined with increasing grain diets in sheep. J. Anim. Sci. 86:384 -389.
    • (2008) J. Anim. Sci. , vol.86 , pp. 384-389
    • Christophersen, C.T.1    Wright, A.D.2    Vercoe, P.E.3
  • 65
    • 0032240058 scopus 로고    scopus 로고
    • The importance of pH in the regulation of ruminal acetate to propionate ratio and methane production in vitro
    • Russell JB. 1998. The importance of pH in the regulation of ruminal acetate to propionate ratio and methane production in vitro. J. Dairy Sci. 81:3222-3230.
    • (1998) J. Dairy Sci. , vol.81 , pp. 3222-3230
    • Russell, J.B.1
  • 66
    • 0014152720 scopus 로고
    • In vitro degradation of oxalate and of cellulose by rumen ingesta from sheep fed Halogeton glomeratus
    • James LF, Street JC, Butcher JE. 1967. In vitro degradation of oxalate and of cellulose by rumen ingesta from sheep fed Halogeton glomeratus. J. Anim. Sci. 26:1438 -1444.
    • (1967) J. Anim. Sci. , vol.26 , pp. 1438-1444
    • James, L.F.1    Street, J.C.2    Butcher, J.E.3
  • 67
    • 79960003556 scopus 로고    scopus 로고
    • BioMetals: a historical and personal perspective
    • Silver S. 2011. BioMetals: a historical and personal perspective. Biometals 24:379 -390.
    • (2011) Biometals , vol.24 , pp. 379-390
    • Silver, S.1
  • 68
    • 79951615060 scopus 로고    scopus 로고
    • Regulation of acid resistance by connectors of two-component signal transduction systems in Escherichia coli
    • Eguchi Y, Ishii E, Hata K, Utsumi R. 2011. Regulation of acid resistance by connectors of two-component signal transduction systems in Escherichia coli. J. Bacteriol. 193:1222-1228.
    • (2011) J. Bacteriol. , vol.193 , pp. 1222-1228
    • Eguchi, Y.1    Ishii, E.2    Hata, K.3    Utsumi, R.4
  • 69
    • 0029671310 scopus 로고    scopus 로고
    • + as an extracellular signal: environmental regulation of Salmonella virulence
    • + as an extracellular signal: environmental regulation of Salmonella virulence. Cell 84: 165-174.
    • (1996) Cell , vol.84 , pp. 165-174
    • Garcia Vescovi, E.1    Soncini, F.C.2    Groisman, E.A.3
  • 70
    • 77956330310 scopus 로고    scopus 로고
    • Hydrogenase-3 contributes to anaerobic acid resistance of Escherichia coli
    • doi:10.1371/journal.pone.0010132.
    • Noguchi K, Riggins DP, Eldahan KC, Kitko RD, Slonczewski JL. 2010. Hydrogenase-3 contributes to anaerobic acid resistance of Escherichia coli. PLoS One 5:e10132. doi:10.1371/journal.pone.0010132.
    • (2010) PLoS One , vol.5
    • Noguchi, K.1    Riggins, D.P.2    Eldahan, K.C.3    Kitko, R.D.4    Slonczewski, J.L.5
  • 71
    • 0028938217 scopus 로고
    • Acid tolerance of enterohemorrhagic Escherichia coli
    • Benjamin MM, Datta AR. 1995. Acid tolerance of enterohemorrhagic Escherichia coli. Appl. Environ. Microbiol. 61:1669 -1672.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1669-1672
    • Benjamin, M.M.1    Datta, A.R.2
  • 73
    • 84886949970 scopus 로고    scopus 로고
    • Relationship between obesity and the volume of a mouthful in the human
    • Horio T. 2000. Relationship between obesity and the volume of a mouthful in the human. Bull. Koshien Univ. 28:57- 60.
    • (2000) Bull. Koshien Univ. , vol.28 , pp. 57-60
    • Horio, T.1
  • 75
    • 84898631568 scopus 로고    scopus 로고
    • Update on multistate outbreak of E. coli O157:H7 infections from fresh spinach
    • Centers for Disease Control and Prevention, Atlanta, GA
    • Centers for Disease Control and Prevention. 2006. Update on multistate outbreak of E. coli O157:H7 infections from fresh spinach. Centers for Disease Control and Prevention, Atlanta, GA.
    • (2006) Centers for Disease Control and Prevention
  • 76
    • 0019741898 scopus 로고
    • Identification of a sexfactor- affinity site in E. coli as gamma delta. Cold Spring Harb
    • PART 1
    • Guyer MS, Reed RR, Steitz JA, Low KB. 1981. Identification of a sexfactor- affinity site in E. coli as gamma delta. Cold Spring Harb. Symp. Quant. Biol. 45(Part 1):135-140.
    • (1981) Symp. Quant. Biol. , vol.45 , pp. 135-140
    • Guyer, M.S.1    Reed, R.R.2    Steitz, J.A.3    Low, K.B.4
  • 77
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • U.S.A.
    • Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.