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Volumn 182, Issue 8, 2000, Pages 2230-2237

Genetic and biochemical characterization of the pathway in Pantoea citrea leading to pink disease of pineapple

Author keywords

[No Author keywords available]

Indexed keywords

GLUCONIC ACID;

EID: 0034111025     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.8.2230-2237.2000     Document Type: Article
Times cited : (39)

References (44)
  • 1
    • 0029063381 scopus 로고
    • Mini-Tn10 transposon derivatives for insertion mutagenesis and gene delivery into the chromosome of gram-negative bacteria
    • Alexeyev, M. F., and I. N. Shokolenko. 1995. Mini-Tn10 transposon derivatives for insertion mutagenesis and gene delivery into the chromosome of gram-negative bacteria. Gene 160:59-62.
    • (1995) Gene , vol.160 , pp. 59-62
    • Alexeyev, M.F.1    Shokolenko, I.N.2
  • 2
    • 0013098708 scopus 로고
    • 2-Keto-D-gluconate reductase from acetic acid bacteria
    • Ameyama, M., and O. Adachi. 1982. 2-Keto-D-gluconate reductase from acetic acid bacteria. Methods Enzymol. 89:203-209.
    • (1982) Methods Enzymol. , vol.89 , pp. 203-209
    • Ameyama, M.1    Adachi, O.2
  • 3
    • 0022372833 scopus 로고
    • Production of 2-keto-L-gulonate, an intermediate in L-ascorbate synthesis, by a genetically modified Erwinia herbicola
    • Anderson, S., C. B. Marks, R. Lazarus, J. Miller, K. Stafford, J. Seymour, D. Light, W. Rastetler, and D. Estell. 1985. Production of 2-keto-L-gulonate, an intermediate in L-ascorbate synthesis, by a genetically modified Erwinia herbicola. Science 230:144-149.
    • (1985) Science , vol.230 , pp. 144-149
    • Anderson, S.1    Marks, C.B.2    Lazarus, R.3    Miller, J.4    Stafford, K.5    Seymour, J.6    Light, D.7    Rastetler, W.8    Estell, D.9
  • 4
    • 0020971311 scopus 로고
    • A rapid alkaline extraction method for the isolation of plasmid DNA
    • Birnboim, H. C. 1983. A rapid alkaline extraction method for the isolation of plasmid DNA. Methods Enzymol. 100:243-255.
    • (1983) Methods Enzymol. , vol.100 , pp. 243-255
    • Birnboim, H.C.1
  • 5
    • 0024557388 scopus 로고
    • Taxonomic diversity of the D-glucose oxidation pathway in the enterobacteriaceae
    • Bouvet, O. M., P. Lenormand, and P. A. Grimont. 1989. Taxonomic diversity of the D-glucose oxidation pathway in the enterobacteriaceae. Int. J. Syst. b Bacteriol. 39:61-67.
    • (1989) Int. J. Syst. B Bacteriol. , vol.39 , pp. 61-67
    • Bouvet, O.M.1    Lenormand, P.2    Grimont, P.A.3
  • 7
    • 0031035647 scopus 로고    scopus 로고
    • Identification and characterization of a Pantoea citrea gene encoding glucose dehydrogenase that is essential for causing pink disease of pineapple
    • Cha, J.-S., C. J. Pujol, and C. I. Kado. 1997. Identification and characterization of a Pantoea citrea gene encoding glucose dehydrogenase that is essential for causing pink disease of pineapple. Appl. Environ. Microbiol. 63: 71-76.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 71-76
    • Cha, J.-S.1    Pujol, C.J.2    Kado, C.I.3
  • 9
    • 0023874871 scopus 로고
    • Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: Evidence for the presence of a second enzyme
    • Cleton-Jansen, A.-M., N. Goosen, T. J. Wenzel, and P. van de Putte. 1988. Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: evidence for the presence of a second enzyme. J. Bacteriol. 170:2121-2125.
    • (1988) J. Bacteriol. , vol.170 , pp. 2121-2125
    • Cleton-Jansen, A.-M.1    Goosen, N.2    Wenzel, T.J.3    Van De Putte, P.4
  • 11
    • 0028930524 scopus 로고
    • The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain
    • Crooke, H., and J. Cole. 1995. The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain. Mol. Microbiol. 15:1139-1150.
    • (1995) Mol. Microbiol. , vol.15 , pp. 1139-1150
    • Crooke, H.1    Cole, J.2
  • 12
    • 0018568175 scopus 로고
    • Isolation of a methanol dehydrogenase with a functional coupling to cytochrome c
    • Duine, J. A., J. Frank, and L. G. De Ruiter. 1979. Isolation of a methanol dehydrogenase with a functional coupling to cytochrome c. J. Gen. Microbiol. 115:523-526.
    • (1979) J. Gen. Microbiol. , vol.115 , pp. 523-526
    • Duine, J.A.1    Frank, J.2    De Ruiter, L.G.3
  • 13
    • 38149145427 scopus 로고
    • Cytochrome c springs a surprise
    • Ferguson, S. J. 1987. Cytochrome c springs a surprise. Trends Biochem. Sci. 12:124-125.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 124-125
    • Ferguson, S.J.1
  • 14
    • 0006885378 scopus 로고
    • Periplasmic electron transport reactions
    • Anthony C. (ed.). Academic Press, London, England
    • Ferguson, S. J. 1988. Periplasmic electron transport reactions, p. 151-182. In Anthony C. (ed.), Bacterial energy transduction. Academic Press, London, England.
    • (1988) Bacterial Energy Transduction , pp. 151-182
    • Ferguson, S.J.1
  • 15
    • 0028965483 scopus 로고
    • Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12
    • Fong, S. T., J. Camakaris, and B. T. Lee. 1995. Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12. Mol. Microbiol. 15:1127-1137.
    • (1995) Mol. Microbiol. , vol.15 , pp. 1127-1137
    • Fong, S.T.1    Camakaris, J.2    Lee, B.T.3
  • 16
    • 0023762137 scopus 로고
    • Conversion of glucose to 2-keto-L-gulonate, an intermediate in L-ascorbate synthesis, by a recombinant strain of Erwinia citreus
    • Grindley, J. F., M. A. Payton, H. van de Pol, and K. G. Hardy. 1988. Conversion of glucose to 2-keto-L-gulonate, an intermediate in L-ascorbate synthesis, by a recombinant strain of Erwinia citreus. Appl. Environ. Microbiol. 54:1770-1775.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 1770-1775
    • Grindley, J.F.1    Payton, M.A.2    Van De Pol, H.3    Hardy, K.G.4
  • 17
    • 0342633274 scopus 로고
    • Glucose dehydrogenase: Pseudomonas sp. and Bacterium anitratum
    • Hauge, J. G. 1966. Glucose dehydrogenase: Pseudomonas sp. and Bacterium anitratum. Methods Enzymol. 9:92-98.
    • (1966) Methods Enzymol. , vol.9 , pp. 92-98
    • Hauge, J.G.1
  • 18
    • 0342937272 scopus 로고
    • Epidemiology of pink disease of pineapple fruit
    • Hine, R. B. 1975. Epidemiology of pink disease of pineapple fruit. Phytopathology 66:323-327.
    • (1975) Phytopathology , vol.66 , pp. 323-327
    • Hine, R.B.1
  • 19
    • 0343503447 scopus 로고
    • Determination of intermediates in bioconversion of 2,5-diketo-D-gluconic acid by genus Corynebacterium by thin-layer Chromatography
    • Joveva, S., R. Nozinie, and V. Delie. 1991. Determination of intermediates in bioconversion of 2,5-diketo-D-gluconic acid by genus Corynebacterium by thin-layer Chromatography. Prehrambeno-tehnol. Biotehnol. Rev. 29:87-90.
    • (1991) Prehrambeno-tehnol. Biotehnol. Rev. , vol.29 , pp. 87-90
    • Joveva, S.1    Nozinie, R.2    Delie, V.3
  • 20
    • 0026562718 scopus 로고
    • Pantoea punctata sp. nov., Pantoea citrea sp. nov., and Pantoea terrea sp. nov. isolated from fruit and soil samples
    • Kageyama, B., M. Nakae, S. Vagi, and T. Sonoyama. 1992. Pantoea punctata sp. nov., Pantoea citrea sp. nov., and Pantoea terrea sp. nov. isolated from fruit and soil samples. Int. J. Syst. Bacteriol. 42:203-210.
    • (1992) Int. J. Syst. Bacteriol. , vol.42 , pp. 203-210
    • Kageyama, B.1    Nakae, M.2    Vagi, S.3    Sonoyama, T.4
  • 21
    • 0032499712 scopus 로고    scopus 로고
    • Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-Å resolution
    • Khurana, S., D. B. Powers, S. Anderson, and M. Blaber. 1998. Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-Å resolution. Proc. Natl. Acad. Sci. USA 95:6768-6773.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6768-6773
    • Khurana, S.1    Powers, D.B.2    Anderson, S.3    Blaber, M.4
  • 22
    • 0343372630 scopus 로고
    • A survey of the pineapple problems
    • Lyon, H. L. 1915. A survey of the pineapple problems. Hawaii. Plant. Rec. 13:125-139.
    • (1915) Hawaii. Plant. Rec. , vol.13 , pp. 125-139
    • Lyon, H.L.1
  • 23
    • 0028979629 scopus 로고
    • Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
    • Missiakas, D., F. Schwager, and S. Raina. 1995. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14:3415-3424.
    • (1995) EMBO J. , vol.14 , pp. 3415-3424
    • Missiakas, D.1    Schwager, F.2    Raina, S.3
  • 24
    • 0343503446 scopus 로고
    • Diseases of the pineapple
    • Oxenham, B. L. 1957. Diseases of the pineapple. Queensl. Agric. J. 83:13-26.
    • (1957) Queensl. Agric. J. , vol.83 , pp. 13-26
    • Oxenham, B.L.1
  • 25
    • 0004219125 scopus 로고
    • Springer-Verlag Berlin, Germany
    • Pettigrew, G. W., and G. R. Moore. 1987. Cytochromes c, p. 160-179. Springer-Verlag Berlin, Germany.
    • (1987) Cytochromes C , pp. 160-179
    • Pettigrew, G.W.1    Moore, G.R.2
  • 26
    • 0032946590 scopus 로고    scopus 로고
    • gdhB, a gene encoding a second quinoprotein glucose dehydrogenase in Pantoea citrea, is required for the pink disease of pineapple
    • Pujol, C. J., and C. I. Kado. 1999. gdhB, a gene encoding a second quinoprotein glucose dehydrogenase in Pantoea citrea, is required for the pink disease of pineapple. Microbiology 145:1217-1226.
    • (1999) Microbiology , vol.145 , pp. 1217-1226
    • Pujol, C.J.1    Kado, C.I.2
  • 27
    • 0041386886 scopus 로고
    • Unusual tropical fruit diseases with extended latent periods
    • Rohrbach, K. G. 1989. Unusual tropical fruit diseases with extended latent periods. Plant Dis. 73:607-609.
    • (1989) Plant Dis. , vol.73 , pp. 607-609
    • Rohrbach, K.G.1
  • 28
    • 0342503079 scopus 로고
    • The interaction of four bacteria causing pink disease of pineapple with several pineapple cultivars
    • Rohrbach, K. G., and J. B. Pfeiffer. 1976. The interaction of four bacteria causing pink disease of pineapple with several pineapple cultivars. Phytopathology 66:396-399.
    • (1976) Phytopathology , vol.66 , pp. 396-399
    • Rohrbach, K.G.1    Pfeiffer, J.B.2
  • 31
    • 0033033305 scopus 로고    scopus 로고
    • Heme transfer to the heme chaperone CcmE during cytochrome c maturation requires the CcmC protein, which may function independently of the ABC-transporter CcmAB
    • Schulz, H., R. A. Fabianek, E. C. Pellicioli, H. Hennecke, and L. Thöny-Meyer. 1999. Heme transfer to the heme chaperone CcmE during cytochrome c maturation requires the CcmC protein, which may function independently of the ABC-transporter CcmAB. Proc. Natl. Acad. Sci. USA 96: 6462-6467.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6462-6467
    • Schulz, H.1    Fabianek, R.A.2    Pellicioli, E.C.3    Hennecke, H.4    Thöny-Meyer, L.5
  • 32
    • 0032555539 scopus 로고    scopus 로고
    • Prototype of a heme chaperone essential for cytochrome c maturation
    • Schulz, H., H. Hennecke, and L. Thäny-Meyer. 1998. Prototype of a heme chaperone essential for cytochrome c maturation. Science 281:1197-1200.
    • (1998) Science , vol.281 , pp. 1197-1200
    • Schulz, H.1    Hennecke, H.2    Thäny-Meyer, L.3
  • 33
    • 0017845775 scopus 로고
    • Distribution of gluconate dehydrogenase and ketogluconate reductases in aerobic bacteria
    • Shinagawa, E., T. Chiyonobu, K. Matsushita, O. Adachi, and M. Ameyama. 1978. Distribution of gluconate dehydrogenase and ketogluconate reductases in aerobic bacteria. Agric. Biol. Chem. 42:1055-1057.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 1055-1057
    • Shinagawa, E.1    Chiyonobu, T.2    Matsushita, K.3    Adachi, O.4    Ameyama, M.5
  • 34
    • 0013050778 scopus 로고
    • D-Gluconate dehydrogenase, 2-keto-D-gluconate yielding, from Gluconobacter dioxyacetonicus: Purification and characterization
    • Shinagawa, E., K. Matsushita, O. Adachi, and M. Ameyama. 1984. D-Gluconate dehydrogenase, 2-keto-D-gluconate yielding, from Gluconobacter dioxyacetonicus: purification and characterization. Agric. Biol. Chem. 48:1517-1522.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 1517-1522
    • Shinagawa, E.1    Matsushita, K.2    Adachi, O.3    Ameyama, M.4
  • 35
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vitro engineering: Transposon mutagenesis in gram-negative bacteria
    • Simon, R., U. Priefer, and A. Puhler. 1983. A broad host range mobilization system for in vitro engineering: transposon mutagenesis in gram-negative bacteria. Bio/Technology 1:742-791.
    • (1983) Bio/Technology , vol.1 , pp. 742-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 36
    • 0000171516 scopus 로고
    • Purification and properties of two 2,5-diketo-D-gluconate reductases from a mutant strain derived from Corynebacterium species
    • Sonoyama, T., and B. Kobayashi. 1987. Purification and properties of two 2,5-diketo-D-gluconate reductases from a mutant strain derived from Corynebacterium species. J. Ferment. Technol. 65:311-317.
    • (1987) J. Ferment. Technol. , vol.65 , pp. 311-317
    • Sonoyama, T.1    Kobayashi, B.2
  • 37
    • 85004245320 scopus 로고
    • Facultatively anaerobic bacteria showing high productivities of 2,5-diketo-D-gluconate from D-glucose
    • Sonoyama, T., S. Yagi, and B. Kageyama. 1988. Facultatively anaerobic bacteria showing high productivities of 2,5-diketo-D-gluconate from D-glucose. Agric. Biol. Chem. 52:667-674.
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 667-674
    • Sonoyama, T.1    Yagi, S.2    Kageyama, B.3
  • 39
    • 1842383697 scopus 로고
    • Single-stranded plasmid DNA in Bacillus subtilis and Staphylococcus aureus
    • te Riele, H., B. Michel, and S. D. Ehrlich. 1986. Single-stranded plasmid DNA in Bacillus subtilis and Staphylococcus aureus. Proc. Natl. Acad. Sci. USA 83:2541-2545.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2541-2545
    • Te Riele, H.1    Michel, B.2    Ehrlich, S.D.3
  • 40
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • Thöny-Meyer, L. 1997. Biogenesis of respiratory cytochromes in bacteria. Microbiol. Mol. Rev. 61:337-376.
    • (1997) Microbiol. Mol. Rev. , vol.61 , pp. 337-376
    • Thöny-Meyer, L.1
  • 42
    • 0029987670 scopus 로고    scopus 로고
    • A chromosomal locus required for copper resistance, competitive fitness, and cytochrome c biogenesis in Pseudomonas fluorescent
    • Yang, C., H. Azad, and D. Cooksey. 1996. A chromosomal locus required for copper resistance, competitive fitness, and cytochrome c biogenesis in Pseudomonas fluorescent. Proc. Natl. Acad. Sci. USA 93:7315-7320.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7315-7320
    • Yang, C.1    Azad, H.2    Cooksey, D.3
  • 43
    • 0030668086 scopus 로고    scopus 로고
    • Cloning and expression of a gene cluster encoding three subunits of membrane-bound gluconate dehydrogenase from Erwinia cypripedii ATCC 29267 in Escherichia coli
    • Yum, D. Y., Y. P. Lee, and J. G. Pan. 1997. Cloning and expression of a gene cluster encoding three subunits of membrane-bound gluconate dehydrogenase from Erwinia cypripedii ATCC 29267 in Escherichia coli. J. Bacteriol. 179:6566-6572.
    • (1997) J. Bacteriol. , vol.179 , pp. 6566-6572
    • Yum, D.Y.1    Lee, Y.P.2    Pan, J.G.3
  • 44
    • 0031791394 scopus 로고    scopus 로고
    • The yiaE gene, located at 80.1 minutes on the Escherichia coli chromosome, encodes a 2-ketoaldonate reductase
    • Yum, D.-Y., B.-Y. Lee, D.-H. Hahm, and J.-G. Pan. 1998. The yiaE gene, located at 80.1 minutes on the Escherichia coli chromosome, encodes a 2-ketoaldonate reductase. J. Bacteriol. 180:5984-5988.
    • (1998) J. Bacteriol. , vol.180 , pp. 5984-5988
    • Yum, D.-Y.1    Lee, B.-Y.2    Hahm, D.-H.3    Pan, J.-G.4


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