메뉴 건너뛰기




Volumn 185, Issue 15, 2003, Pages 4499-4507

IS981-mediated adaptive evolution recovers lactate production by ldhB transcription activation in a lactate dehydrogenase-deficient strain of Lactococcus lactis

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; ACETOIN; ALCOHOL; LACTATE DEHYDROGENASE; LACTIC ACID;

EID: 0038105063     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.15.4499-4507.2003     Document Type: Article
Times cited : (64)

References (53)
  • 1
    • 0035663793 scopus 로고    scopus 로고
    • Lactate dehydrogenase has no control on lactate production but has a strong negative control on formate production in Lactococcus lactis
    • Andersen, H. W., M. B. Pedersen, K. Hammer, and P. R. Jensen. 2001. Lactate dehydrogenase has no control on lactate production but has a strong negative control on formate production in Lactococcus lactis. Eur. J. Biochem. 268:6379-6389.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6379-6389
    • Andersen, H.W.1    Pedersen, M.B.2    Hammer, K.3    Jensen, P.R.4
  • 2
    • 0028363150 scopus 로고
    • Cloning, characterization and insertional inactivation of the Lactobacillus helveticus D(-) lactate dehydrogenase gene
    • Bhowmik, T., and J. L. Steele. 1994. Cloning, characterization and insertional inactivation of the Lactobacillus helveticus D(-) lactate dehydrogenase gene. Appl. Microbiol. Biotechnol. 41:432-439.
    • (1994) Appl. Microbiol. Biotechnol. , vol.41 , pp. 432-439
    • Bhowmik, T.1    Steele, J.L.2
  • 3
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C., and J. Doly. 1979. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7:1513-1523.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 5
    • 0030970438 scopus 로고    scopus 로고
    • Isolation and properties of Lactococcus lactis subsp, lactis biovar diacetylactis CNRZ 483 mutants producing diacetyl and acetoin from glucose
    • Boumerdassi, H., C. Monnet, M. Desmazeaud, and G. Corrieu. 1997. Isolation and properties of Lactococcus lactis subsp, lactis biovar diacetylactis CNRZ 483 mutants producing diacetyl and acetoin from glucose. Appl. Environ. Microbiol. 63:2293-2299.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2293-2299
    • Boumerdassi, H.1    Monnet, C.2    Desmazeaud, M.3    Corrieu, G.4
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:52-58.
    • (1976) Anal. Biochem. , vol.72 , pp. 52-58
    • Bradford, M.M.1
  • 7
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban, M. J., and S. N. Cohen. 1980. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138:179-207.
    • (1980) J. Mol. Biol. , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 8
    • 0021209585 scopus 로고
    • Two plasmid-determined restriction and modification systems in Streptococcus lactis
    • Chopin, A., M. C. Chopin, A. Moillo-Batt, and P. Langella. 1984. Two plasmid-determined restriction and modification systems in Streptococcus lactis. Plasmid 11:260-263.
    • (1984) Plasmid , vol.11 , pp. 260-263
    • Chopin, A.1    Chopin, M.C.2    Moillo-Batt, A.3    Langella, P.4
  • 11
    • 0017407960 scopus 로고
    • Fructose 1,6-diphosphate-activated L-lactate dehydrogenase from Streptococcus lactis: Kinetic properties and factors affecting activation
    • Crow, V. L., and G. G. Pritchard. 1977. Fructose 1,6-diphosphate-activated L-lactate dehydrogenase from Streptococcus lactis: kinetic properties and factors affecting activation. J. Bacteriol. 131:82-91.
    • (1977) J. Bacteriol. , vol.131 , pp. 82-91
    • Crow, V.L.1    Pritchard, G.G.2
  • 13
    • 0024786318 scopus 로고
    • Cloning and expression of the Lactococcus lactis ssp. cremoris SK11 gene encoding an extracellular serine protease
    • de Vos, W. M., P. Vos, H. de Haard, and I. Boerrigter. 1989. Cloning and expression of the Lactococcus lactis ssp. cremoris SK11 gene encoding an extracellular serine protease. Gene 85:169-176.
    • (1989) Gene , vol.85 , pp. 169-176
    • De Vos, W.M.1    Vos, P.2    De Haard, H.3    Boerrigter, I.4
  • 14
    • 0030746339 scopus 로고    scopus 로고
    • Characterization of Lactococcus lactis UV-sensitive mutants obtained by ISS1 transposition
    • Duwat, P., A. Cochu, S. D. Ehrlich, and A. Gruss. 1997. Characterization of Lactococcus lactis UV-sensitive mutants obtained by ISS1 transposition. J. Bacteriol. 179:4473-4479.
    • (1997) J. Bacteriol. , vol.179 , pp. 4473-4479
    • Duwat, P.1    Cochu, A.2    Ehrlich, S.D.3    Gruss, A.4
  • 15
    • 0028010007 scopus 로고
    • Lactobacillus plantarum ldhL gene: Overexpression and deletion
    • Ferain, T., D. Garmyn, N. Bernard, P. Hols, and J. Delcour. 1994. Lactobacillus plantarum ldhL gene: overexpression and deletion. J. Bacteriol. 176:596-601.
    • (1994) J. Bacteriol. , vol.176 , pp. 596-601
    • Ferain, T.1    Garmyn, D.2    Bernard, N.3    Hols, P.4    Delcour, J.5
  • 16
    • 0002734187 scopus 로고
    • Bacterial insertion sequences
    • D. E. Berg and M. M. Howe (ed.). American Society for Microbiology, Washington, D.C.
    • Galas, D. J., and M. Chandler. 1989. Bacterial insertion sequences, p. 109-162. In D. E. Berg and M. M. Howe (ed.), Mobile DNA. American Society for Microbiology, Washington, D.C.
    • (1989) Mobile DNA , pp. 109-162
    • Galas, D.J.1    Chandler, M.2
  • 17
    • 0034877264 scopus 로고    scopus 로고
    • Glucose metabolism and regulation of glycolysis in Lactococcus lactis strains with decreased lactate dehydrogenase activity
    • Garrigues, C., N. Goupil-Feuillerat, M. Cocaign-Bousquet, P. Renault, N. D. Lindley, and P. Loubiere. 2001. Glucose metabolism and regulation of glycolysis in Lactococcus lactis strains with decreased lactate dehydrogenase activity. Metab. Eng. 3:211-217.
    • (2001) Metab. Eng. , vol.3 , pp. 211-217
    • Garrigues, C.1    Goupil-Feuillerat, N.2    Cocaign-Bousquet, M.3    Renault, P.4    Lindley, N.D.5    Loubiere, P.6
  • 19
    • 0018022577 scopus 로고
    • Lactate dehydrogenases of Streptococcus thermophilus
    • Garvie, E. I. 1978. Lactate dehydrogenases of Streptococcus thermophilus. J. Dairy Res. 45:515-518.
    • (1978) J. Dairy Res. , vol.45 , pp. 515-518
    • Garvie, E.I.1
  • 20
    • 0040455226 scopus 로고    scopus 로고
    • Metabolic engineering of the Lactococcus lactis diacetyl pathway
    • Gasson, M., K. Benson, S. Swindell, and H. Griffin. 1996. Metabolic engineering of the Lactococcus lactis diacetyl pathway. Lait 76:33-40.
    • (1996) Lait , vol.76 , pp. 33-40
    • Gasson, M.1    Benson, K.2    Swindell, S.3    Griffin, H.4
  • 21
    • 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
  • 22
    • 0020347802 scopus 로고
    • L-Lactate dehydrogenase, FDP-activated, from Streptococcus cremoris
    • Hillier, A. J., and G. R. Jago. 1982. L-Lactate dehydrogenase, FDP-activated, from Streptococcus cremoris. Methods Enzymol. 89:362-367.
    • (1982) Methods Enzymol. , vol.89 , pp. 362-367
    • Hillier, A.J.1    Jago, G.R.2
  • 24
  • 25
    • 0032879297 scopus 로고    scopus 로고
    • Acetate utilization in Lactococcus lactis deficient in lactate dehydrogenase: A rescue pathway for maintaining redox balance
    • Hols, P., A. Ramos, J. Hugenholtz, J. Delcour, W. M. de Vos, H. Santos, and M. Kleerebezem. 1999. Acetate utilization in Lactococcus lactis deficient in lactate dehydrogenase: a rescue pathway for maintaining redox balance. J. Bacteriol. 181:5521-5526.
    • (1999) J. Bacteriol. , vol.181 , pp. 5521-5526
    • Hols, P.1    Ramos, A.2    Hugenholtz, J.3    Delcour, J.4    De Vos, W.M.5    Santos, H.6    Kleerebezem, M.7
  • 27
    • 0031965086 scopus 로고    scopus 로고
    • The sequence of spacers between the consensus sequences modulates the strength of prokaryotic promoters
    • Jensen, P. R., and K. Hammer. 1998. The sequence of spacers between the consensus sequences modulates the strength of prokaryotic promoters. Appl. Environ. Microbiol. 64:82-87.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 82-87
    • Jensen, P.R.1    Hammer, K.2
  • 30
    • 0027162304 scopus 로고
    • Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis: Requirement of expression of the nisA and nisI genes for development of immunity
    • Kuipers, O. P., M. M. Beerthuyzen, R. J. Siezen, and W. M. De Vos. 1993. Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis: requirement of expression of the nisA and nisI genes for development of immunity. Eur. J. Biochem. 216:281-291.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 281-291
    • Kuipers, O.P.1    Beerthuyzen, M.M.2    Siezen, R.J.3    De Vos, W.M.4
  • 32
    • 0036158160 scopus 로고    scopus 로고
    • Regulation and adaptive evolution of lactose operon expression in Lactobacillus delbrueckii
    • Lapierre, L., B. Mollet, and J. E. Germond. 2002. Regulation and adaptive evolution of lactose operon expression in Lactobacillus delbrueckii. J. Bacteriol. 184:928-935.
    • (2002) J. Bacteriol. , vol.184 , pp. 928-935
    • Lapierre, L.1    Mollet, B.2    Germond, J.E.3
  • 33
    • 0027193138 scopus 로고
    • Identification of a novel operon in Lactococcus lactis encoding three enzymes for lactic acid synthesis: Phosphofructokinase, pyruvate kinase, and lactate dehydrogenase
    • Llanos, R. M., C. J. Harris, A. J. Hillier, and B. E. Davidson. 1993. Identification of a novel operon in Lactococcus lactis encoding three enzymes for lactic acid synthesis: phosphofructokinase, pyruvate kinase, and lactate dehydrogenase. J. Bacteriol. 175:2541-2551.
    • (1993) J. Bacteriol. , vol.175 , pp. 2541-2551
    • Llanos, R.M.1    Harris, C.J.2    Hillier, A.J.3    Davidson, B.E.4
  • 34
    • 0026712388 scopus 로고
    • Cloning, nucleotide sequence, expression, and chromosomal location of ldh, the gene encoding L-(+)-lactate dehydrogenase, from Lactococcus lactis
    • Llanos, R. M., A. J. Hillier, and B. E. Davidson. 1992. Cloning, nucleotide sequence, expression, and chromosomal location of ldh, the gene encoding L-(+)-lactate dehydrogenase, from Lactococcus lactis. J. Bacteriol. 174:6956-6964.
    • (1992) J. Bacteriol. , vol.174 , pp. 6956-6964
    • Llanos, R.M.1    Hillier, A.J.2    Davidson, B.E.3
  • 35
    • 0032824868 scopus 로고    scopus 로고
    • Pyruvate flux distribution in NADH-oxidase-overproducing Lactococcus lactis strain as a function of culture conditions
    • Lopez de Felipe, F., and J. Hugenholtz. 1999. Pyruvate flux distribution in NADH-oxidase-overproducing Lactococcus lactis strain as a function of culture conditions. FEMS Microbiol. Lett. 179:461-466.
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 461-466
    • Lopez de Felipe, F.1    Hugenholtz, J.2
  • 36
    • 0031877248 scopus 로고    scopus 로고
    • Cofactor engineering: A novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase
    • Lopez de Felipe, F., M. Kleerebezem, W. M. de Vos, and J. Hugenholtz. 1998. Cofactor engineering: a novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase. J. Bacteriol. 180:3804-3808.
    • (1998) J. Bacteriol. , vol.180 , pp. 3804-3808
    • Lopez de Felipe, F.1    Kleerebezem, M.2    De Vos, W.M.3    Hugenholtz, J.4
  • 37
    • 0029919467 scopus 로고    scopus 로고
    • Transcriptional activation of the citrate permease P gene of Lactococcus lactis biovar diacetylactis by an insertion sequence-like element present in plasmid pCIT264
    • Lopez de Felipe, F., C. Magni, D. de Mendoza, and P. Lopez. 1996. Transcriptional activation of the citrate permease P gene of Lactococcus lactis biovar diacetylactis by an insertion sequence-like element present in plasmid pCIT264. Mol. Gen. Genet. 250:428-436.
    • (1996) Mol. Gen. Genet. , vol.250 , pp. 428-436
    • Lopez de Felipe, F.1    Magni, C.2    De Mendoza, D.3    Lopez, P.4
  • 38
    • 0031735564 scopus 로고    scopus 로고
    • Transcriptional activation of the glycolytic las operon and catabolite repression of the gal operon in Lactococcus lactis are mediated by the catabolite control protein CcpA
    • Luesink, E. J., R. E. van Herpen, B. P. Grossiord, O. P. Kuipers, and W. M. de Vos. 1998. Transcriptional activation of the glycolytic las operon and catabolite repression of the gal operon in Lactococcus lactis are mediated by the catabolite control protein CcpA. Mol. Microbiol. 30:789-798.
    • (1998) Mol. Microbiol. , vol.30 , pp. 789-798
    • Luesink, E.J.1    Van Herpen, R.E.2    Grossiord, B.P.3    Kuipers, O.P.4    De Vos, W.M.5
  • 39
    • 0028065674 scopus 로고
    • Adaptive evolution of highly mutable loci in pathogenic bacteria
    • Moxon, E. R., P. B. Rainey, M. A. Nowak, and R. E. Lenski. 1994. Adaptive evolution of highly mutable loci in pathogenic bacteria. Curr. Biol. 4:24-33.
    • (1994) Curr. Biol. , vol.4 , pp. 24-33
    • Moxon, E.R.1    Rainey, P.B.2    Nowak, M.A.3    Lenski, R.E.4
  • 43
    • 0028853944 scopus 로고
    • Metabolic engineering of Lactococcus lactis: Influence of the overproduction of α-acetolactate synthase in strains deficient in lactate dehydrogenase as a function of culture conditions
    • Platteeuw, C., J. Hugenholtz, M. Starrenburg, I. van Alen-Boerrigter, and W. M. de Vos. 1995. Metabolic engineering of Lactococcus lactis: influence of the overproduction of α-acetolactate synthase in strains deficient in lactate dehydrogenase as a function of culture conditions. Appl. Environ. Microbiol. 61:3967-3971.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3967-3971
    • Platteeuw, C.1    Hugenholtz, J.2    Starrenburg, M.3    Van Alen-Boerrigter, I.4    De Vos, W.M.5
  • 44
    • 0023042749 scopus 로고
    • Functional promoters created by the insertion of transposable element IS1
    • Prentki, P., B. Teter, M. Chandler, and D. J. Galas. 1986. Functional promoters created by the insertion of transposable element IS1. J. Mol. Biol. 191:383-393.
    • (1986) J. Mol. Biol. , vol.191 , pp. 383-393
    • Prentki, P.1    Teter, B.2    Chandler, M.3    Galas, D.J.4
  • 45
    • 0035895278 scopus 로고    scopus 로고
    • Genetic architecture of thermal adaptation in Escherichia coli
    • Riehle, M. M., A. F. Bennett, and A. D. Long. 2001. Genetic architecture of thermal adaptation in Escherichia coli. Proc. Natl. Acad. Sci. USA 98:525-530.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 525-530
    • Riehle, M.M.1    Bennett, A.F.2    Long, A.D.3
  • 47
    • 0030844235 scopus 로고    scopus 로고
    • Molecular genetic characterization of the L-lactate dehydrogenase gene (ldhL) of Lactobacillus helveticus and biochemical characterization of the enzyme
    • Savijoki, K., and A. Palva. 1997. Molecular genetic characterization of the L-lactate dehydrogenase gene (ldhL) of Lactobacillus helveticus and biochemical characterization of the enzyme. Appl. Environ. Microbiol. 63:2850-2856.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2850-2856
    • Savijoki, K.1    Palva, A.2
  • 48
    • 0033786720 scopus 로고    scopus 로고
    • Long-term experimental evolution in Escherichia coli. IX. Characterization of insertion sequence-mediated mutations and rearrangements
    • Schneider, D., E. Duperchy, E. Coursange, R. E. Lenski, and M. Blot. 2000. Long-term experimental evolution in Escherichia coli. IX. Characterization of insertion sequence-mediated mutations and rearrangements. Genetics 156:477-488.
    • (2000) Genetics , vol.156 , pp. 477-488
    • Schneider, D.1    Duperchy, E.2    Coursange, E.3    Lenski, R.E.4    Blot, M.5
  • 49
    • 0025790130 scopus 로고
    • Citrate fermentation by Lactococcus and Leuconostoc spp.
    • Starrenburg, M. J. C., and J. Hugenholtz. 1991. Citrate fermentation by Lactococcus and Leuconostoc spp. Appl. Environ. Microbiol. 57:3535-3540.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 3535-3540
    • Starrenburg, M.J.C.1    Hugenholtz, J.2
  • 51
    • 0025779127 scopus 로고
    • D-Lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family: Cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum
    • Taguchi, H., and T. Ohta. 1991. D-Lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family: cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum. J. Biol. Chem. 266:12588-12594.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12588-12594
    • Taguchi, H.1    Ohta, T.2
  • 52
    • 0025052301 scopus 로고
    • Molecular cloning, transcriptional analysis, and nucleotide sequence of lacR, a gene encoding the repressor of the lactose phosphotransferase system of Lactococcus lactis
    • van Rooijen, R. J., and W. M. de Vos. 1990. Molecular cloning, transcriptional analysis, and nucleotide sequence of lacR, a gene encoding the repressor of the lactose phosphotransferase system of Lactococcus lactis. J. Biol. Chem. 265:18499-18503.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18499-18503
    • Van Rooijen, R.J.1    De Vos, W.M.2
  • 53
    • 0024538493 scopus 로고
    • A maturation protein is essential for the production of active forms of Lactococcus lactis SK11 serine proteinase located in or secreted from the cell envelope
    • Vos, P., M. van Asseldonk, F. van Jeveren, R. Siezen, G. Simons, and W. M. de Vos. 1989. A maturation protein is essential for the production of active forms of Lactococcus lactis SK11 serine proteinase located in or secreted from the cell envelope. J. Bacteriol. 171:2795-2802.
    • (1989) J. Bacteriol. , vol.171 , pp. 2795-2802
    • Vos, P.1    Van Asseldonk, M.2    Van Jeveren, F.3    Siezen, R.4    Simons, G.5    De Vos, W.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.