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Volumn 13, Issue 1, 2011, Pages 48-61

Two respiratory enzyme systems in Campylobacter jejuni NCTC 11168 contribute to growth on l-lactate

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; IRON SULFUR PROTEIN; LACTATE DEHYDROGENASE; LACTIC ACID;

EID: 78650800583     PISSN: 14622912     EISSN: 14622920     Source Type: Journal    
DOI: 10.1111/j.1462-2920.2010.02307.x     Document Type: Article
Times cited : (77)

References (39)
  • 1
    • 41949098532 scopus 로고    scopus 로고
    • Dual role of LldR in regulation of the lldPRD operon, involved in l-lactate metabolism in Escherichia coli
    • Aguilera, L., Campos, E., Giménez, R., Badía, J., Aguilar, J., and Baldoma, L. (2008) Dual role of LldR in regulation of the lldPRD operon, involved in l-lactate metabolism in Escherichia coli. J Bacteriol 190: 2997-3005.
    • (2008) J Bacteriol , vol.190 , pp. 2997-3005
    • Aguilera, L.1    Campos, E.2    Giménez, R.3    Badía, J.4    Aguilar, J.5    Baldoma, L.6
  • 2
    • 65249133908 scopus 로고    scopus 로고
    • A widely conserved gene cluster required for lactate utilisation in Bacillus subtilis and its involvement in biofilm formation
    • Chai, Y., Kolter, R., and Losick, R. (2009) A widely conserved gene cluster required for lactate utilisation in Bacillus subtilis and its involvement in biofilm formation. J Bacteriol 191: 2423-2430.
    • (2009) J Bacteriol , vol.191 , pp. 2423-2430
    • Chai, Y.1    Kolter, R.2    Losick, R.3
  • 3
    • 63449136189 scopus 로고    scopus 로고
    • The d-2-Hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis
    • Chambellon, E., Rijnen, L., Lorquet, F., Gitton, C., van Hylckama Vlieg, J.E.T., Wouters, J.A., and Yvon, M. (2009) The d-2-Hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis. J Bacteriol 191: 873-881.
    • (2009) J Bacteriol , vol.191 , pp. 873-881
    • Chambellon, E.1    Rijnen, L.2    Lorquet, F.3    Gitton, C.4    van Hylckama Vlieg, J.E.T.5    Wouters, J.A.6    Yvon, M.7
  • 4
    • 0027358810 scopus 로고
    • Three overlapping lct genes involved in l-lactate utilization by Escherichia coli
    • Dong, J.M., Taylor, J.S., Latour, D.J., Iuchi, S., and Lin, E.C.C. (1993) Three overlapping lct genes involved in l-lactate utilization by Escherichia coli. J Bacteriol 175: 6671-6678.
    • (1993) J Bacteriol , vol.175 , pp. 6671-6678
    • Dong, J.M.1    Taylor, J.S.2    Latour, D.J.3    Iuchi, S.4    Lin, E.C.C.5
  • 5
    • 0034662927 scopus 로고    scopus 로고
    • The crystal structure of d-lactate dehydrogenase, a peripheral membrane respiratory enzyme
    • Dym, O., Pratt, E.A., Ho, C., and Eisenberg, D. (2000) The crystal structure of d-lactate dehydrogenase, a peripheral membrane respiratory enzyme. Proc Natl Acad Sci USA 97: 9413-9418.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9413-9418
    • Dym, O.1    Pratt, E.A.2    Ho, C.3    Eisenberg, D.4
  • 6
    • 0027367411 scopus 로고
    • Oxidation of d-lactate and l-lactate by Neisseria meningitidis: Purification and cloning of meningococcal d-lactate dehydrogenase
    • Erwin, A.L., and Gotschlich, E.C. (1993) Oxidation of d-lactate and l-lactate by Neisseria meningitidis: Purification and cloning of meningococcal d-lactate dehydrogenase. J Bacteriol 175: 6382-6391.
    • (1993) J Bacteriol , vol.175 , pp. 6382-6391
    • Erwin, A.L.1    Gotschlich, E.C.2
  • 7
    • 0015854555 scopus 로고
    • Membrane d-lactate dehydrogenase from Escherichia coli. Purification and properties
    • Futai, M. (1973) Membrane d-lactate dehydrogenase from Escherichia coli. Purification and properties. Biochemistry 12: 2468-2474.
    • (1973) Biochemistry , vol.12 , pp. 2468-2474
    • Futai, M.1
  • 8
    • 0017709139 scopus 로고
    • Inducible membrane-bound l-lactate dehydrogenase from Escherichia coli: purification and properties
    • Futai, M., and Kimura, H. (1977) Inducible membrane-bound l-lactate dehydrogenase from Escherichia coli: purification and properties. J Biol Chem 252: 5820-5827.
    • (1977) J Biol Chem , vol.252 , pp. 5820-5827
    • Futai, M.1    Kimura, H.2
  • 9
    • 0018818947 scopus 로고
    • Bacterial lactate dehydrogenases
    • Garvie, E. (1980) Bacterial lactate dehydrogenases. Microbiol Rev 44: 106-139.
    • (1980) Microbiol Rev , vol.44 , pp. 106-139
    • Garvie, E.1
  • 10
    • 77957862665 scopus 로고    scopus 로고
    • The Campylobacter genetic toolbox: development of tractable and generally applicable genetic techniques for Campylobacter jejuni
    • Gaskin, D.J.H., van Vliet, A.H.M., and Pearson, B.M. (2007) The Campylobacter genetic toolbox: development of tractable and generally applicable genetic techniques for Campylobacter jejuni. Zoon Publ Health 54 (suppl. 1): 101.
    • (2007) Zoon Publ Health , vol.54 , Issue.1 SUPPL. , pp. 101
    • Gaskin, D.J.H.1    van Vliet, A.H.M.2    Pearson, B.M.3
  • 11
    • 77953943092 scopus 로고    scopus 로고
    • Reduction of fumarate, mesaconate and crotonate by Mfr, a novel oxygen-regulated periplasmic reductase in Campylobacter jejuni
    • Guccione, E., Hitchock, A., Hall, S.J., Mulholland, F., Shearer, N., van Vliet, A.H.M., and Kelly, D.J. (2010) Reduction of fumarate, mesaconate and crotonate by Mfr, a novel oxygen-regulated periplasmic reductase in Campylobacter jejuni. Environ Microbiol 12: 576-591.
    • (2010) Environ Microbiol , vol.12 , pp. 576-591
    • Guccione, E.1    Hitchock, A.2    Hall, S.J.3    Mulholland, F.4    Shearer, N.5    van Vliet, A.H.M.6    Kelly, D.J.7
  • 12
    • 45149111730 scopus 로고    scopus 로고
    • Amino acid-dependent growth of Campylobacter jejuni: key roles for aspartase (AspA) under microaerobic and oxygen-limited conditions and identification of AspB (Cj0762), essential for growth on glutamate
    • Guccione, E.J., Leon-Kempis, M.R., Pearson, B.M., Hitchin, E., Mulholland, F., van Diemen, P.M., et al. (2008) Amino acid-dependent growth of Campylobacter jejuni: key roles for aspartase (AspA) under microaerobic and oxygen-limited conditions and identification of AspB (Cj0762), essential for growth on glutamate. Mol Microbiol 69: 77-93.
    • (2008) Mol Microbiol , vol.69 , pp. 77-93
    • Guccione, E.J.1    Leon-Kempis, M.R.2    Pearson, B.M.3    Hitchin, E.4    Mulholland, F.5    van Diemen, P.M.6
  • 14
    • 0027203858 scopus 로고
    • TnMax -a versatile mini-transposon for the analysis of cloned genes and shuttle mutagenesis
    • Haas, R., Kahrs, A.F., Facius, D., Allmeier, H., Schmitt, R., and Meyer, T.F. (1993) TnMax -a versatile mini-transposon for the analysis of cloned genes and shuttle mutagenesis. Gene 130: 23-31.
    • (1993) Gene , vol.130 , pp. 23-31
    • Haas, R.1    Kahrs, A.F.2    Facius, D.3    Allmeier, H.4    Schmitt, R.5    Meyer, T.F.6
  • 15
    • 31144479663 scopus 로고    scopus 로고
    • Growth of Campylobacter in media supplemented with organic acids
    • Hinton, A. (2006) Growth of Campylobacter in media supplemented with organic acids. J Food Prot 69: 34-38.
    • (2006) J Food Prot , vol.69 , pp. 34-38
    • Hinton, A.1
  • 16
    • 0020029133 scopus 로고
    • Respiratory physiology and energy conservation efficiency of Campylobacter jejuni
    • Hoffman, P.S., and Goodman, T.G. (1982) Respiratory physiology and energy conservation efficiency of Campylobacter jejuni. J Bacteriol 150: 319-326.
    • (1982) J Bacteriol , vol.150 , pp. 319-326
    • Hoffman, P.S.1    Goodman, T.G.2
  • 17
    • 55249102409 scopus 로고    scopus 로고
    • Metabolic diversity in Campylobacter jejuni enhances specific tissue colonization
    • Hofreuter, D., Novic, V., and Galan, J.E. (2008) Metabolic diversity in Campylobacter jejuni enhances specific tissue colonization. Cell Host Microbe 4: 425-433.
    • (2008) Cell Host Microbe , vol.4 , pp. 425-433
    • Hofreuter, D.1    Novic, V.2    Galan, J.E.3
  • 18
    • 0002665065 scopus 로고    scopus 로고
    • Campylobacter
    • 3rd, edn., Nachamkin, I., Szymanski, C.M., and Blaser, M.J. (eds). Washington, DC, USA: ASM Press
    • Jacobs-Reitsma, W., Lyhs, U., and Wagenaar, J. (2008) Campylobacter in the food supply. In Campylobacter. 3rd edn. Nachamkin, I., Szymanski, C.M., and Blaser, M.J. (eds). Washington, DC, USA: ASM Press, pp. 627-644.
    • (2008) Campylobacter in the food supply , pp. 627-644
    • Jacobs-Reitsma, W.1    Lyhs, U.2    Wagenaar, J.3
  • 19
    • 33748771961 scopus 로고    scopus 로고
    • Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of l-leucine to isocaproate by Clostridium difficile
    • Kim, J., Darley, D., Selmer, T., and Buckel, W. (2006) Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of l-leucine to isocaproate by Clostridium difficile. Appl Environ Microbiol 72: 6062-6069.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 6062-6069
    • Kim, J.1    Darley, D.2    Selmer, T.3    Buckel, W.4
  • 20
    • 0030969593 scopus 로고    scopus 로고
    • Changes with growth rate in membrane lipid composition and amino acid utilisation by continuous cultures of Campylobacter jejuni
    • Leach, S., Harvey, P., and Wait, R. (1997) Changes with growth rate in membrane lipid composition and amino acid utilisation by continuous cultures of Campylobacter jejuni. J Appl Microbiol 82: 631-640.
    • (1997) J Appl Microbiol , vol.82 , pp. 631-640
    • Leach, S.1    Harvey, P.2    Wait, R.3
  • 21
    • 34247371381 scopus 로고    scopus 로고
    • Understanding the effects of diet on bacterial metabolism in the large intestine
    • Louis, P., Scott, K.P., Duncan, S.H., and Flint, H.J. (2007) Understanding the effects of diet on bacterial metabolism in the large intestine. J Appl Microbiol 102: 1197-1208.
    • (2007) J Appl Microbiol , vol.102 , pp. 1197-1208
    • Louis, P.1    Scott, K.P.2    Duncan, S.H.3    Flint, H.J.4
  • 22
    • 57649129414 scopus 로고    scopus 로고
    • Oxygen- and NssR-dependent globin expression and enhanced iron acquisition in the response of Campylobacter to nitrosative stress
    • Monk, C.E., Pearson, B.M., Mulholland, F., Smith, H.K., and Poole, R.K. (2008) Oxygen- and NssR-dependent globin expression and enhanced iron acquisition in the response of Campylobacter to nitrosative stress. J Biol Chem 283: 28413-28425.
    • (2008) J Biol Chem , vol.283 , pp. 28413-28425
    • Monk, C.E.1    Pearson, B.M.2    Mulholland, F.3    Smith, H.K.4    Poole, R.K.5
  • 23
    • 13444259982 scopus 로고    scopus 로고
    • A sulphite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni
    • Myers, J.D., and Kelly, D.J. (2005) A sulphite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni. Microbiology 151: 233-242.
    • (2005) Microbiology , vol.151 , pp. 233-242
    • Myers, J.D.1    Kelly, D.J.2
  • 24
    • 0035046989 scopus 로고    scopus 로고
    • The gene yghK linked to the glc operon of Escherichia coli encodes a permease for glycolate that is structurally and functionally similar to l-lactate permease
    • Nunez, M.F., Pellicer, M.T., Badía, J., Aguilar, J., and Baldoma, L. (2001) The gene yghK linked to the glc operon of Escherichia coli encodes a permease for glycolate that is structurally and functionally similar to l-lactate permease. Microbiology 147: 1069-1077.
    • (2001) Microbiology , vol.147 , pp. 1069-1077
    • Nunez, M.F.1    Pellicer, M.T.2    Badía, J.3    Aguilar, J.4    Baldoma, L.5
  • 25
    • 0036296183 scopus 로고    scopus 로고
    • Transport of l-lactate, d-lactate, and glycolate by the LldP and GlcA membrane carriers of Echerichia coli
    • Nunez, M.F., Kwon, O., Wilson, T.H., Aguilar, J., Baldoma, L., and Lin, E.C.C. (2002) Transport of l-lactate, d-lactate, and glycolate by the LldP and GlcA membrane carriers of Echerichia coli. Biochem Biophys Res Commun 290: 824-829.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 824-829
    • Nunez, M.F.1    Kwon, O.2    Wilson, T.H.3    Aguilar, J.4    Baldoma, L.5    Lin, E.C.C.6
  • 27
    • 0034628526 scopus 로고    scopus 로고
    • The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences
    • Parkhill, J., Wren, B.W., Mungall, K., Ketley, J.M., Churcher, C., Basham, D., et al. (2000) The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences. Nature 403: 665-668.
    • (2000) Nature , vol.403 , pp. 665-668
    • Parkhill, J.1    Wren, B.W.2    Mungall, K.3    Ketley, J.M.4    Churcher, C.5    Basham, D.6
  • 28
    • 0032521076 scopus 로고    scopus 로고
    • Construction of PCR-ligated long flanking homology cassettes for use in the functional analysis of six unknown open reading frames from the left and right arms of Saccharomyces cerevisiae chromosome XV
    • Pearson, B.M., Hernando, Y., and Schweizer, M. (1998) Construction of PCR-ligated long flanking homology cassettes for use in the functional analysis of six unknown open reading frames from the left and right arms of Saccharomyces cerevisiae chromosome XV. Yeast 14: 391-399.
    • (1998) Yeast , vol.14 , pp. 391-399
    • Pearson, B.M.1    Hernando, Y.2    Schweizer, M.3
  • 30
    • 62449305520 scopus 로고    scopus 로고
    • Genomic reconstruction of Shewanella oneidensis MR-1 metabolism reveals a previously uncharacterised machinery for lactate utilisation
    • Pinchuk, G.E., Rodionov, D.A., Yang, C., Li, X., Osterman, A.L., Dervyn, E., et al. (2009) Genomic reconstruction of Shewanella oneidensis MR-1 metabolism reveals a previously uncharacterised machinery for lactate utilisation. Proc Natl Acad Sci USA 106: 2874-2879.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 2874-2879
    • Pinchuk, G.E.1    Rodionov, D.A.2    Yang, C.3    Li, X.4    Osterman, A.L.5    Dervyn, E.6
  • 31
    • 0034462324 scopus 로고    scopus 로고
    • Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Escherichia coli
    • van der Rest, M.E., Frank, C., and Molenaar, D. (2000) Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Escherichia coli. J Bacteriol 182: 6892-6899.
    • (2000) J Bacteriol , vol.182 , pp. 6892-6899
    • van der Rest, M.E.1    Frank, C.2    Molenaar, D.3
  • 32
    • 0004136246 scopus 로고
    • Molecular Cloning: A Laboratory Manual
    • New York, USA: Cold Spring Harbor Laboratory Press.
    • Sambrook, J., Maniatis, T., and Fritsch, E.F. (1989) Molecular Cloning: A Laboratory Manual. New York, USA: Cold Spring Harbor Laboratory Press.
    • (1989)
    • Sambrook, J.1    Maniatis, T.2    Fritsch, E.F.3
  • 33
    • 0036066808 scopus 로고    scopus 로고
    • Growth of Campylobacter jejuni supported by respiration of fumarate, nitrate, nitrite, trimethylamine-N-oxide, or dimethyl sulfoxide requires oxygen
    • Sellars, M.J., Hall, S.J., and Kelly, D.J. (2002) Growth of Campylobacter jejuni supported by respiration of fumarate, nitrate, nitrite, trimethylamine-N-oxide, or dimethyl sulfoxide requires oxygen. J Bacteriol 184: 4187-4196.
    • (2002) J Bacteriol , vol.184 , pp. 4187-4196
    • Sellars, M.J.1    Hall, S.J.2    Kelly, D.J.3
  • 34
    • 70350406435 scopus 로고    scopus 로고
    • A role for tungsten in the biology of Campylobacter jejuni: tungstate stimulates formate dehydrogenase activity and is transported via an ultra-high affinity ABC system distinct from the molybdate transporter
    • Smart, J.P., Cliff, M.J., and Kelly, D.J. (2009) A role for tungsten in the biology of Campylobacter jejuni: tungstate stimulates formate dehydrogenase activity and is transported via an ultra-high affinity ABC system distinct from the molybdate transporter. Mol Microbiol 74: 742-757.
    • (2009) Mol Microbiol , vol.74 , pp. 742-757
    • Smart, J.P.1    Cliff, M.J.2    Kelly, D.J.3
  • 35
    • 0000944720 scopus 로고
    • Bergey's Manual of Systematic Bacteriology
    • In, Krieg, N.R. and, Holt, J.G. (eds). Baltimore, MD, USA: Williams & Wilkins
    • Smibert, R.M. (1984) Genus Campylobacter Sebald and Veron 1963. In Bergey's Manual of Systematic Bacteriology, Vol. 1. Krieg, N.R. and Holt, J.G. (eds). Baltimore, MD, USA: Williams & Wilkins, pp. 111-117.
    • (1984) Genus Campylobacter Sebald and Veron 1963 , vol.1 , pp. 111-117
    • Smibert, R.M.1
  • 36
    • 0036126078 scopus 로고    scopus 로고
    • Analysis of gluconeogenic and anaplerotic enzymes in Campylobacter jejuni: an essential role for phosphoenolpyruvate carboxykinase
    • Velayudhan, J., and Kelly, D.J. (2002) Analysis of gluconeogenic and anaplerotic enzymes in Campylobacter jejuni: an essential role for phosphoenolpyruvate carboxykinase. Microbiology 148: 685-694.
    • (2002) Microbiology , vol.148 , pp. 685-694
    • Velayudhan, J.1    Kelly, D.J.2
  • 37
    • 39149113138 scopus 로고    scopus 로고
    • Pyruvate relieves the necessity of high induction levels of catalase and enables Campylobacter jejuni to grow under fully aerobic conditions
    • Verhoeff-Bakkenes, L., Arends, A.P., Snoep, J.L., Zwietering, M.H., and de Jonge, R. (2008) Pyruvate relieves the necessity of high induction levels of catalase and enables Campylobacter jejuni to grow under fully aerobic conditions. Lett Appl Microbiol 46: 377-382.
    • (2008) Lett Appl Microbiol , vol.46 , pp. 377-382
    • Verhoeff-Bakkenes, L.1    Arends, A.P.2    Snoep, J.L.3    Zwietering, M.H.4    de Jonge, R.5
  • 38
    • 0031690670 scopus 로고    scopus 로고
    • Iron-responsive gene regulation in a Campylobacter jejuni fur mutant
    • van Vliet, A.H.M., Wooldridge, K.G., and Ketley, J.M. (1998) Iron-responsive gene regulation in a Campylobacter jejuni fur mutant. J Bacteriol 180: 5291-5298.
    • (1998) J Bacteriol , vol.180 , pp. 5291-5298
    • van Vliet, A.H.M.1    Wooldridge, K.G.2    Ketley, J.M.3
  • 39
    • 40549083689 scopus 로고    scopus 로고
    • Role of Campylobacter jejuni respiratory oxidases and reductases in host colonization
    • Weingarten, R.A., Grimes, J.L., and Olson, J.W. (2008) Role of Campylobacter jejuni respiratory oxidases and reductases in host colonization. Appl Environ Microbiol 74: 1367-1375.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 1367-1375
    • Weingarten, R.A.1    Grimes, J.L.2    Olson, J.W.3


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