메뉴 건너뛰기




Volumn 53, Issue 5, 2004, Pages 1331-1342

Respiration metabolism reduces oxidative and acid stress to improve long-term survival of Lactococcus lactis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; CELL PROTEIN; GREEN FLUORESCENT PROTEIN; HEME; OXYGEN;

EID: 4444364187     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2004.04217.x     Document Type: Article
Times cited : (88)

References (59)
  • 1
    • 0021100151 scopus 로고
    • Hemin-mediated DNA strand scission
    • Aft, R.L., and Mueller, G.C. (1983) Hemin-mediated DNA strand scission. J Biol Chem 258: 12069-12072.
    • (1983) J Biol Chem , vol.258 , pp. 12069-12072
    • Aft, R.L.1    Mueller, G.C.2
  • 2
    • 0021322523 scopus 로고
    • Hemin-mediated oxidative degradation of proteins
    • Aft, R.L., and Mueller, G.C. (1984) Hemin-mediated oxidative degradation of proteins. J Biol Chem 259: 301-305.
    • (1984) J Biol Chem , vol.259 , pp. 301-305
    • Aft, R.L.1    Mueller, G.C.2
  • 3
    • 0033895840 scopus 로고    scopus 로고
    • Effects of limited aeration and of the ArcAB system on intermediary pyruvate catabolism in Escherichia coli
    • Alexeeva, S., de Kort, B., Sawers, G., Hellingwerf, K.J., and de Mattos, M.J. (2000) Effects of limited aeration and of the ArcAB system on intermediary pyruvate catabolism in Escherichia coli. J Bacteriol 182: 4934-4940.
    • (2000) J Bacteriol , vol.182 , pp. 4934-4940
    • Alexeeva, S.1    De Kort, B.2    Sawers, G.3    Hellingwerf, K.J.4    De Mattos, M.J.5
  • 4
    • 0037216801 scopus 로고    scopus 로고
    • Requirement of ArcA for redox regulation in Escherichia coli under microaerobic but not anaerobic or aerobic conditions
    • Alexeeva, S., Hellingwerf, K.J., and Teixeira de Mattos, M.J. (2003) Requirement of ArcA for redox regulation in Escherichia coli under microaerobic but not anaerobic or aerobic conditions. J Bacteriol 185: 204-209.
    • (2003) J Bacteriol , vol.185 , pp. 204-209
    • Alexeeva, S.1    Hellingwerf, K.J.2    Teixeira De Mattos, M.J.3
  • 5
    • 0028263624 scopus 로고
    • Determination of the oxygen affinities of terminal oxidases in Azotobacter vinelandii using the deoxygenation of oxyleghemoglobin and oxymyoglobin: Cytochrome bd is a low-affinity oxidase
    • D'Mello, R., Hill, S., and Poole, R.K. (1994) Determination of the oxygen affinities of terminal oxidases in Azotobacter vinelandii using the deoxygenation of oxyleghemoglobin and oxymyoglobin: cytochrome bd is a low-affinity oxidase. Microbiology 140: 1395-1402.
    • (1994) Microbiology , vol.140 , pp. 1395-1402
    • D'Mello, R.1    Hill, S.2    Poole, R.K.3
  • 6
    • 0029981912 scopus 로고    scopus 로고
    • The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: Implications for regulation of activity in vivo by oxygen inhibition
    • D'Mello, R., Hill, S., and Poole, R.K. (1996) The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: implications for regulation of activity in vivo by oxygen inhibition. Microbiology 142: 755-763.
    • (1996) Microbiology , vol.142 , pp. 755-763
    • D'Mello, R.1    Hill, S.2    Poole, R.K.3
  • 7
    • 0032213238 scopus 로고    scopus 로고
    • Bacterial senescence: Stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon
    • Dukan, S., and Nystrom, T. (1998) Bacterial senescence: stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon. Genes Dev 12: 3431-3441.
    • (1998) Genes Dev , vol.12 , pp. 3431-3441
    • Dukan, S.1    Nystrom, T.2
  • 8
    • 0028821695 scopus 로고
    • The recA gene of Lactococcus lactis: Characterization and involvement in oxidative and thermal stress
    • Duwat, P., Ehrlich, S.D., and Gruss, A. (1995) The recA gene of Lactococcus lactis: characterization and involvement in oxidative and thermal stress. Mol Microbiol 17: 1121-1131.
    • (1995) Mol Microbiol , vol.17 , pp. 1121-1131
    • Duwat, P.1    Ehrlich, S.D.2    Gruss, A.3
  • 9
    • 0034941874 scopus 로고    scopus 로고
    • Respiration capacity of the fermenting bacterium Lactococcus lactis and its positive effects on growth and survival
    • Duwat, P., Sourice, S., Cesselin, B., Lamberet, G., Vido, K., Gaudu, P., et al. (2001) Respiration capacity of the fermenting bacterium Lactococcus lactis and its positive effects on growth and survival. J Bacteriol 183: 4509-4516.
    • (2001) J Bacteriol , vol.183 , pp. 4509-4516
    • Duwat, P.1    Sourice, S.2    Cesselin, B.3    Lamberet, G.4    Vido, K.5    Gaudu, P.6
  • 10
    • 0035089129 scopus 로고    scopus 로고
    • Interruption of the cydB locus in Brucella abortus attenuates intracellular survival and virulence in the mouse model of infection
    • Endley, S., McMurray, D., and Ficht, T.A. (2001) Interruption of the cydB locus in Brucella abortus attenuates intracellular survival and virulence in the mouse model of infection. J Bacteriol 183: 2454-2462.
    • (2001) J Bacteriol , vol.183 , pp. 2454-2462
    • Endley, S.1    McMurray, D.2    Ficht, T.A.3
  • 11
    • 0036041922 scopus 로고    scopus 로고
    • Dynamic response of catabolic pathways to autoacidification in Lactococcus lactis: Transcript profiling and stability in relation to metabolic and energetic constraints
    • Even, S., Lindley, N.D., Loubiere, P., and Cocaign-Bousquet, M. (2002) Dynamic response of catabolic pathways to autoacidification in Lactococcus lactis: transcript profiling and stability in relation to metabolic and energetic constraints. Mol Microbiol 45: 1143-1152.
    • (2002) Mol Microbiol , vol.45 , pp. 1143-1152
    • Even, S.1    Lindley, N.D.2    Loubiere, P.3    Cocaign-Bousquet, M.4
  • 12
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner, P.R., and Fridovich, I. (1991) Superoxide sensitivity of the Escherichia coli aconitase. J Biol Chem 266: 19328-19333.
    • (1991) J Biol Chem , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 13
    • 0020600404 scopus 로고
    • Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing
    • Gasson, M.J. (1983) Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing. J Bacteriol 154: 1-9.
    • (1983) J Bacteriol , vol.154 , pp. 1-9
    • Gasson, M.J.1
  • 15
    • 0141595858 scopus 로고    scopus 로고
    • CcpA regulation of aerobic and respiration growth in Lactococcus lactis
    • Gaudu, P., Lamberet, G., Poncet, S., and Gruss, A. (2003) CcpA regulation of aerobic and respiration growth in Lactococcus lactis. Mol Microbiol 50: 183-192.
    • (2003) Mol Microbiol , vol.50 , pp. 183-192
    • Gaudu, P.1    Lamberet, G.2    Poncet, S.3    Gruss, A.4
  • 17
    • 0029917388 scopus 로고    scopus 로고
    • The temperature-sensitive growth and survival phenotypes of Escherichia coli cydDC and cydAB strains are due to deficiencies in cytochrome bd and are corrected by exogenous catalase and reducing agents
    • Goldman, B.S., Gabbert, K.K., and Kranz, R.G. (1996) The temperature-sensitive growth and survival phenotypes of Escherichia coli cydDC and cydAB strains are due to deficiencies in cytochrome bd and are corrected by exogenous catalase and reducing agents. J Bacteriol 178: 6348-6351.
    • (1996) J Bacteriol , vol.178 , pp. 6348-6351
    • Goldman, B.S.1    Gabbert, K.K.2    Kranz, R.G.3
  • 18
    • 0029018721 scopus 로고
    • Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli
    • Gonzalez-Flecha, B., and Demple, B. (1995) Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli. J Biol Chem 270: 13681-13687.
    • (1995) J Biol Chem , vol.270 , pp. 13681-13687
    • Gonzalez-Flecha, B.1    Demple, B.2
  • 19
    • 0035862437 scopus 로고    scopus 로고
    • Use of green fluorescent protein to monitor Lactobacillus sakei in fermented meat products
    • Gory, L., Montel, M.C., and Zagorec, M. (2001) Use of green fluorescent protein to monitor Lactobacillus sakei in fermented meat products. FEMS Microbiol Lett 194: 127-133.
    • (2001) FEMS Microbiol Lett , vol.194 , pp. 127-133
    • Gory, L.1    Montel, M.C.2    Zagorec, M.3
  • 20
    • 0020505048 scopus 로고
    • Isolation and characterization of an Escherichia coli mutant lacking cytochrome d terminal oxidase
    • Green, G.N., and Gennis, R.B. (1983) Isolation and characterization of an Escherichia coli mutant lacking cytochrome d terminal oxidase. J Bacteriol 154: 1269-1275.
    • (1983) J Bacteriol , vol.154 , pp. 1269-1275
    • Green, G.N.1    Gennis, R.B.2
  • 21
    • 0035007851 scopus 로고    scopus 로고
    • Assessment of GFP fluorescence in cells of Streptococcus gordonii under conditions of low pH and low oxygen concentration
    • Hansen, M.C., Palmer, R.J., Jr, Udsen, C., White, D.C., and Molin, S. (2001) Assessment of GFP fluorescence in cells of Streptococcus gordonii under conditions of low pH and low oxygen concentration. Microbiology 147: 1383-1391.
    • (2001) Microbiology , vol.147 , pp. 1383-1391
    • Hansen, M.C.1    Palmer Jr., R.J.2    Udsen, C.3    White, D.C.4    Molin, S.5
  • 22
    • 0030797051 scopus 로고    scopus 로고
    • Formation, prevention, and repair of DNA damage by iron/hydrogen peroxide
    • Henle, E.S., and Linn, S. (1997) Formation, prevention, and repair of DNA damage by iron/hydrogen peroxide. J Biol Chem 272: 19095-19098.
    • (1997) J Biol Chem , vol.272 , pp. 19095-19098
    • Henle, E.S.1    Linn, S.2
  • 24
    • 0035159222 scopus 로고    scopus 로고
    • Extracellular superoxide production by Enterococcus faecalis requires demethylmenaquinone and is attenuated by functional terminal quinol oxidases
    • Huycke, M.M., Moore, D., Joyce, W., Wise, P., Shepard, L., Kotake, Y., and Gilmore, M.S. (2001) Extracellular superoxide production by Enterococcus faecalis requires demethylmenaquinone and is attenuated by functional terminal quinol oxidases. Mol Microbiol 42: 729-740.
    • (2001) Mol Microbiol , vol.42 , pp. 729-740
    • Huycke, M.M.1    Moore, D.2    Joyce, W.3    Wise, P.4    Shepard, L.5    Kotake, Y.6    Gilmore, M.S.7
  • 25
    • 0025800392 scopus 로고
    • Assay of metabolic superoxide production in Escherichia coli
    • Imlay, J.A., and Fridovich, I. (1991) Assay of metabolic superoxide production in Escherichia coli. J Biol Chem 266: 6957-6965.
    • (1991) J Biol Chem , vol.266 , pp. 6957-6965
    • Imlay, J.A.1    Fridovich, I.2
  • 26
    • 0023905646 scopus 로고
    • Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
    • Imlay, J.A., Chin, S.M., and Linn, S. (1988) Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 240: 640-642.
    • (1988) Science , vol.240 , pp. 640-642
    • Imlay, J.A.1    Chin, S.M.2    Linn, S.3
  • 27
    • 0025144171 scopus 로고
    • Requirement for terminal cytochromes in generation of the aerobic signal for the arc regulatory system in Escherichia coli: Study utilizing deletions and lac fusions of cyo and cyd
    • luchi, S., Chepuri, V., Fu, H.A., Gennis, R.B., and Lin, E.C. (1990) Requirement for terminal cytochromes in generation of the aerobic signal for the arc regulatory system in Escherichia coli: study utilizing deletions and lac fusions of cyo and cyd. J Bacteriol 172: 6020-6025.
    • (1990) J Bacteriol , vol.172 , pp. 6020-6025
    • Luchi, S.1    Chepuri, V.2    Fu, H.A.3    Gennis, R.B.4    Lin, E.C.5
  • 28
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • Keyer, K., and Imlay, J.A. (1996) Superoxide accelerates DNA damage by elevating free-iron levels. Proc Natl Acad Sci USA 93: 13635-13640.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 29
    • 0027383520 scopus 로고
    • The stationary phase of the bacterial life cycle
    • Kolter, R., Siegele, D.A., and Tormo, A. (1993) The stationary phase of the bacterial life cycle. Annu Rev Microbiol 47: 855-874.
    • (1993) Annu Rev Microbiol , vol.47 , pp. 855-874
    • Kolter, R.1    Siegele, D.A.2    Tormo, A.3
  • 30
    • 0037130175 scopus 로고    scopus 로고
    • Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration
    • Lin, S.J., Kaeberlein, M., Andalis, A.A., Sturtz, L.A., Defossez, P.A., Culotta, V.C., et al. (2002) Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration. Nature 418: 344-348.
    • (2002) Nature , vol.418 , pp. 344-348
    • Lin, S.J.1    Kaeberlein, M.2    Andalis, A.A.3    Sturtz, L.A.4    Defossez, P.A.5    Culotta, V.C.6
  • 31
    • 0033826231 scopus 로고    scopus 로고
    • Roles of respiratory oxidases in protecting Escherichia coli K12 from oxidative stress
    • Lindqvist, A., Membrillo-Hernandez, J., Poole, R.K., and Cook, G.M. (2000) Roles of respiratory oxidases in protecting Escherichia coli K12 from oxidative stress. Antonie Van Leeuwenhoek 78: 23-31.
    • (2000) Antonie Van Leeuwenhoek , vol.78 , pp. 23-31
    • Lindqvist, A.1    Membrillo-Hernandez, J.2    Poole, R.K.3    Cook, G.M.4
  • 32
    • 0029868750 scopus 로고    scopus 로고
    • The role of iron-sulfur clusters in in vivo hydroxyl radical production
    • Liochev, S.L. (1996) The role of iron-sulfur clusters in in vivo hydroxyl radical production. Free Radic Res 25: 369-384.
    • (1996) Free Radic Res , vol.25 , pp. 369-384
    • Liochev, S.L.1
  • 33
    • 0030027865 scopus 로고    scopus 로고
    • Efficient insertional mutagenesis in lactococci and other gram-positive bacteria
    • Maguin, E., Prevost, H., Ehrlich, S.D., and Gruss, A. (1996) Efficient insertional mutagenesis in lactococci and other gram-positive bacteria. J Bacteriol 178: 931-935.
    • (1996) J Bacteriol , vol.178 , pp. 931-935
    • Maguin, E.1    Prevost, H.2    Ehrlich, S.D.3    Gruss, A.4
  • 34
    • 0036727268 scopus 로고    scopus 로고
    • In situ determination of the intracellular pH of Lactococcus lactis and Lactobacillus plantarum during pressure treatment
    • Molina-Gutierrez, A., Stippl, V., Delgado, A., Ganzle, M.G., and Vogel, R.F. (2002) In situ determination of the intracellular pH of Lactococcus lactis and Lactobacillus plantarum during pressure treatment. Appl Environ Microbiol 68: 4399-4406.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 4399-4406
    • Molina-Gutierrez, A.1    Stippl, V.2    Delgado, A.3    Ganzle, M.G.4    Vogel, R.F.5
  • 35
    • 0036546931 scopus 로고    scopus 로고
    • Repressed respiration of oral streptococci grown in biofilms
    • Nguyen, P.T., Abranches, J., Phan, T.N., and Marquis, R.E. (2002) Repressed respiration of oral streptococci grown in biofilms. Curr Microbiol 44: 262-266.
    • (2002) Curr Microbiol , vol.44 , pp. 262-266
    • Nguyen, P.T.1    Abranches, J.2    Phan, T.N.3    Marquis, R.E.4
  • 36
    • 0030035132 scopus 로고    scopus 로고
    • Bacterial defense against aging: Role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis
    • Nystrom, T., Larsson, C., and Gustafsson, L. (1996) Bacterial defense against aging: role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis. EMBO J 15: 3219-3228.
    • (1996) EMBO J , vol.15 , pp. 3219-3228
    • Nystrom, T.1    Larsson, C.2    Gustafsson, L.3
  • 37
    • 0345687929 scopus 로고    scopus 로고
    • Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the fenton reaction
    • Pericone, C.D., Park, S., Imlay, J.A., and Weiser, J.N. (2003) Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the fenton reaction. J Bacteriol 185: 6815-6825.
    • (2003) J Bacteriol , vol.185 , pp. 6815-6825
    • Pericone, C.D.1    Park, S.2    Imlay, J.A.3    Weiser, J.N.4
  • 38
    • 0033928977 scopus 로고    scopus 로고
    • Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation
    • Poole, R.K., and Cook, G.M. (2000) Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation. Adv Microb Physiol 43: 165-224.
    • (2000) Adv Microb Physiol , vol.43 , pp. 165-224
    • Poole, R.K.1    Cook, G.M.2
  • 39
    • 0017927714 scopus 로고
    • Cytochrome formation, oxygen-induced proton extrusion and respiratory activity in Streptococcus faecalis var. zymogenes grown in the presence of haematin
    • Pritchard, G.G., and Wimpenny, J.W. (1978) Cytochrome formation, oxygen-induced proton extrusion and respiratory activity in Streptococcus faecalis var. zymogenes grown in the presence of haematin. J General Microbiol 104: 15-22.
    • (1978) J General Microbiol , vol.104 , pp. 15-22
    • Pritchard, G.G.1    Wimpenny, J.W.2
  • 40
    • 0020532809 scopus 로고
    • Determination of plasmid copy number by fluorescence densitometry
    • Projan, S.J., Carleton, S., and Novick, R.P. (1983) Determination of plasmid copy number by fluorescence densitometry. Plasmid 9: 182-190.
    • (1983) Plasmid , vol.9 , pp. 182-190
    • Projan, S.J.1    Carleton, S.2    Novick, R.P.3
  • 41
    • 0017858515 scopus 로고
    • Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli
    • Rice, C.W., and Hempfling, W.P. (1978) Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli. J Bacteriol 134: 115-124.
    • (1978) J Bacteriol , vol.134 , pp. 115-124
    • Rice, C.W.1    Hempfling, W.P.2
  • 42
    • 0034153610 scopus 로고    scopus 로고
    • Bacterial respiration: A flexible process for a changing environment
    • Richardson, D.J. (2000) Bacterial respiration: a flexible process for a changing environment. Microbiology 146: 551-571.
    • (2000) Microbiology , vol.146 , pp. 551-571
    • Richardson, D.J.1
  • 43
    • 0029123490 scopus 로고
    • Stress response in Lactococcus lactis: Cloning, expression analysis, and mutation of the lactococcal superoxide dismutase gene
    • Sanders, J.W., Leenhouts, K.J., Haandrikman, A.J., Venema, G., and Kok, J. (1995) Stress response in Lactococcus lactis: cloning, expression analysis, and mutation of the lactococcal superoxide dismutase gene. J Bacteriol 177: 5254-5260.
    • (1995) J Bacteriol , vol.177 , pp. 5254-5260
    • Sanders, J.W.1    Leenhouts, K.J.2    Haandrikman, A.J.3    Venema, G.4    Kok, J.5
  • 44
    • 0029858145 scopus 로고    scopus 로고
    • The stationary-phase-exit defect of cydC (surB) mutants is due to the lack of a functional terminal cytochrome oxidase
    • Siegele, D.A., Imlay, K.R., and Imlay, J.A. (1996) The stationary-phase-exit defect of cydC (surB) mutants is due to the lack of a functional terminal cytochrome oxidase. J Bacteriol 178: 6091-6096.
    • (1996) J Bacteriol , vol.178 , pp. 6091-6096
    • Siegele, D.A.1    Imlay, K.R.2    Imlay, J.A.3
  • 45
    • 0014912569 scopus 로고
    • Induction of cytochrome formation and stimulation of oxidative dissimilation by hemin in Streptococcus lactis and Leuconostoc mesenteroides
    • Sijpesteijn, A.K. (1970) Induction of cytochrome formation and stimulation of oxidative dissimilation by hemin in Streptococcus lactis and Leuconostoc mesenteroides. Antonie Van Leeuwenhoek 36: 335-348.
    • (1970) Antonie Van Leeuwenhoek , vol.36 , pp. 335-348
    • Sijpesteijn, A.K.1
  • 46
    • 0023992075 scopus 로고
    • Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis
    • Simon, D., and Chopin, A. (1988) Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis. Biochimie 70: 559-566.
    • (1988) Biochimie , vol.70 , pp. 559-566
    • Simon, D.1    Chopin, A.2
  • 47
    • 0036840950 scopus 로고    scopus 로고
    • Staphylococcus aureus aconitase inactivation unexpectedly inhibits post-exponential-phase growth and enhances stationary-phase survival
    • Somerville, G.A., Chaussee, M.S., Morgan, C.I., Fitzgerald, J.R., Dorward, D.W., Reitzer, L.J., and Musser, J.M. (2002) Staphylococcus aureus aconitase inactivation unexpectedly inhibits post-exponential-phase growth and enhances stationary-phase survival. Infect Immun 70: 6373-6382.
    • (2002) Infect Immun , vol.70 , pp. 6373-6382
    • Somerville, G.A.1    Chaussee, M.S.2    Morgan, C.I.3    Fitzgerald, J.R.4    Dorward, D.W.5    Reitzer, L.J.6    Musser, J.M.7
  • 49
    • 0032579371 scopus 로고    scopus 로고
    • Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress
    • Tamarit, J., Cabiscol, E., and Ros, J. (1998) Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. J Biol Chem 273: 3027-3032.
    • (1998) J Biol Chem , vol.273 , pp. 3027-3032
    • Tamarit, J.1    Cabiscol, E.2    Ros, J.3
  • 50
    • 0037109068 scopus 로고    scopus 로고
    • Adaptation to famine: A family of stationary-phase genes revealed by microarray analysis
    • Tani, T.H., Khodursky, A., Blumenthal, R.M., Brown, P.O., and Matthews, R.G. (2002) Adaptation to famine: a family of stationary-phase genes revealed by microarray analysis. Proc Natl Acad Sci USA 99: 13471-13476.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13471-13476
    • Tani, T.H.1    Khodursky, A.2    Blumenthal, R.M.3    Brown, P.O.4    Matthews, R.G.5
  • 51
    • 0025309069 scopus 로고
    • surA, an Escherichia coli gene essential for survival in stationary phase
    • Tormo, A., Almiron, M., and Kolter, R. (1990) surA, an Escherichia coli gene essential for survival in stationary phase. J Bacteriol 172: 4339-4347.
    • (1990) J Bacteriol , vol.172 , pp. 4339-4347
    • Tormo, A.1    Almiron, M.2    Kolter, R.3
  • 52
    • 0030067649 scopus 로고    scopus 로고
    • Effect of microaerophilic cell growth conditions on expression of the aerobic (cyoABCDE and cydAB) and anaerobic (narGHJI, frdABCD, and dmsABC) respiratory pathway genes in Escherichia coli
    • Tseng, C.P., Albrecht, J., and Gunsalus, R.P. (1996) Effect of microaerophilic cell growth conditions on expression of the aerobic (cyoABCDE and cydAB) and anaerobic (narGHJI, frdABCD, and dmsABC) respiratory pathway genes in Escherichia coli. J Bacteriol 178: 1094-1098.
    • (1996) J Bacteriol , vol.178 , pp. 1094-1098
    • Tseng, C.P.1    Albrecht, J.2    Gunsalus, R.P.3
  • 53
    • 0037214441 scopus 로고    scopus 로고
    • Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion
    • Varghese, S., Tang, Y., and Imlay, J.A. (2003) Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion. J Bacteriol 185: 221-230.
    • (2003) J Bacteriol , vol.185 , pp. 221-230
    • Varghese, S.1    Tang, Y.2    Imlay, J.A.3
  • 54
    • 0026646181 scopus 로고
    • Arc-dependent thermal regulation and extragenic suppression of the Escherichia coli cytochrome d operon
    • Wall, D., Delaney, J.M., Fayet, O., Lipinska, B., Yamamoto, T., and Georgopoulos, C. (1992) arc-dependent thermal regulation and extragenic suppression of the Escherichia coli cytochrome d operon. J Bacteriol 174: 6554-6562.
    • (1992) J Bacteriol , vol.174 , pp. 6554-6562
    • Wall, D.1    Delaney, J.M.2    Fayet, O.3    Lipinska, B.4    Yamamoto, T.5    Georgopoulos, C.6
  • 55
    • 0032989878 scopus 로고    scopus 로고
    • Impact of either elevated or decreased levels of cytochrome bd expression on Shigella flexneri virulence
    • Way, S.S., Sallustio, S., Magliozzo, R.S., and Goldberg, M.B. (1999) Impact of either elevated or decreased levels of cytochrome bd expression on Shigella flexneri virulence. J Bacteriol 181: 1229-1237.
    • (1999) J Bacteriol , vol.181 , pp. 1229-1237
    • Way, S.S.1    Sallustio, S.2    Magliozzo, R.S.3    Goldberg, M.B.4
  • 56
    • 0018111833 scopus 로고
    • Biochemical characteristics of Streptococcus species
    • Whittenbury, R. (1978) Biochemical characteristics of Streptococcus species. Soc Appl Bacteriol Symp Ser 7: 51-69.
    • (1978) Soc Appl Bacteriol Symp Ser , vol.7 , pp. 51-69
    • Whittenbury, R.1
  • 57
    • 0034123702 scopus 로고    scopus 로고
    • Enterococcus faecalis V583 contains a cytochrome bd-type respiratory oxidase
    • Winstedt, L., Frankenberg, L., Hederstedt, L., and von Wachenfeldt, C. (2000) Enterococcus faecalis V583 contains a cytochrome bd-type respiratory oxidase. J Bacteriol 182: 3863-3866.
    • (2000) J Bacteriol , vol.182 , pp. 3863-3866
    • Winstedt, L.1    Frankenberg, L.2    Hederstedt, L.3    Von Wachenfeldt, C.4
  • 58
    • 0028306066 scopus 로고
    • Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides
    • Sies, H. (ed). London: Academic Press
    • Wolff, S.P. (1994) Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides. In Methods in Enzymology: Oxygen Radicals in Biological Systems Part C, Vol. 233. Sies, H. (ed). London: Academic Press, pp. 182-189.
    • (1994) Methods in Enzymology: Oxygen Radicals in Biological Systems Part C , vol.233 , pp. 182-189
    • Wolff, S.P.1
  • 59
    • 0028181351 scopus 로고
    • A variant of the staphylococcal chloramphenicol resistance plasmid pC194 with enhanced ability to transform Lactococcus lactis subsp. lactis
    • von Wright, A., and Saarela, M. (1994) A variant of the staphylococcal chloramphenicol resistance plasmid pC194 with enhanced ability to transform Lactococcus lactis subsp. lactis. Plasmid 31: 106-110.
    • (1994) Plasmid , vol.31 , pp. 106-110
    • Von Wright, A.1    Saarela, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.