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Volumn 8, Issue 8, 2008, Pages 1631-1644

Protein expression profile of Gluconacetobacter diazotrophicus PAL5, a sugarcane endophytic plant growth-promoting bacterium

Author keywords

Bacterial metabolism; Gluconacetobacter diazotrophicus; Sugarcane; Sustainable agriculture

Indexed keywords

AMINO ACID DERIVATIVE; BACTERIAL PROTEIN; CARBOHYDRATE; CARBOHYDRATE DERIVATIVE; LIPID; NUCLEOTIDE DERIVATIVE; PROTEIN PAL5; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 42549135435     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200700912     Document Type: Article
Times cited : (15)

References (91)
  • 1
    • 0028126007 scopus 로고
    • Nitrogenase and biological nitrogen fixation
    • Kim, J., Rees, D. C., Nitrogenase and biological nitrogen fixation. Biochemistry 1994, 33, 389-397.
    • (1994) Biochemistry , vol.33 , pp. 389-397
    • Kim, J.1    Rees, D.C.2
  • 2
    • 0042348365 scopus 로고    scopus 로고
    • Gluconacetobacter diazotrophicus (syn. Acetobacter diazotrophicus), a promising diazotrophic endophyte in tropics
    • Muthukumarasamy, R., Revathi, G., Seshadri, S., Lakshminarasimhan, C., Gluconacetobacter diazotrophicus (syn. Acetobacter diazotrophicus), a promising diazotrophic endophyte in tropics. Curr. Sci. 2002, 83, 137-145.
    • (2002) Curr. Sci , vol.83 , pp. 137-145
    • Muthukumarasamy, R.1    Revathi, G.2    Seshadri, S.3    Lakshminarasimhan, C.4
  • 3
    • 42549125418 scopus 로고
    • Biological Nitrogen Fixation: Research Challenges - A Review of Research Grants Funded by the U.S. Agency for International Development
    • Hardy, R. W. F., Biological Nitrogen Fixation: Research Challenges - A Review of Research Grants Funded by the U.S. Agency for International Development. National Academy Press 1994, 1.
    • (1994) National Academy Press , vol.1
    • Hardy, R.W.F.1
  • 4
    • 0141590419 scopus 로고    scopus 로고
    • Changing concepts in the systematics of bacterial nitrogen-fixing legume symbionts
    • Sawada, H., Kuykendall, L. D., Young, J. M., Changing concepts in the systematics of bacterial nitrogen-fixing legume symbionts. J. Gen. Appl. Microbiol. 2003, 49, 155-179.
    • (2003) J. Gen. Appl. Microbiol , vol.49 , pp. 155-179
    • Sawada, H.1    Kuykendall, L.D.2    Young, J.M.3
  • 5
    • 0001975986 scopus 로고
    • Phylogenetic classification of nitrogen-fixing organisms
    • Stacy, G, Burris, R. H, Evans, H. J, Eds, Chapman e Hall, New York NY
    • Young, J. P. W., Phylogenetic classification of nitrogen-fixing organisms. In: Stacy, G., Burris, R. H., Evans, H. J. (Eds.). Biological Nitrogen Fixation. Chapman e Hall, New York NY 1992, pp. 43-86.
    • (1992) Biological Nitrogen Fixation , pp. 43-86
    • Young, J.P.W.1
  • 6
    • 0032039641 scopus 로고    scopus 로고
    • Nitrogen cycle enzymology
    • Ferguson, S. J., Nitrogen cycle enzymology. Curr. Opin. Chem. Biol. 1998, 2, 182-193.
    • (1998) Curr. Opin. Chem. Biol , vol.2 , pp. 182-193
    • Ferguson, S.J.1
  • 7
    • 0002060133 scopus 로고
    • History and new perspectives of diazotrophs in association with non-leguminous plants
    • Döbereiner, J., History and new perspectives of diazotrophs in association with non-leguminous plants. Symbiosis 1992, 13, 1-13.
    • (1992) Symbiosis , vol.13 , pp. 1-13
    • Döbereiner, J.1
  • 8
    • 0003216001 scopus 로고    scopus 로고
    • Endophytic microorganisms: A review on insect control and recent advances on tropical plants
    • Azevedo, J. L., Maccheroni Junior, W., Pereira, J. O., Araújo, W. L., Endophytic microorganisms: a review on insect control and recent advances on tropical plants. Electronic J. Biotechnol. 2000, 3, 40-65.
    • (2000) Electronic J. Biotechnol , vol.3 , pp. 40-65
    • Azevedo, J.L.1    Maccheroni Junior, W.2    Pereira, J.O.3    Araújo, W.L.4
  • 9
    • 0034096733 scopus 로고    scopus 로고
    • Nitrogen fixation in endophytic and associative symbiosis
    • James, E. K., Nitrogen fixation in endophytic and associative symbiosis. Field Crops Res. 2000, 65, 197-209.
    • (2000) Field Crops Res , vol.65 , pp. 197-209
    • James, E.K.1
  • 10
    • 0031966083 scopus 로고    scopus 로고
    • Life in grasses: Diazotrophic endophytes
    • Reinhold-Hurek, B., Hurek, T., Life in grasses: diazotrophic endophytes. Trends Microbiol. 1998, 6, 139-144.
    • (1998) Trends Microbiol , vol.6 , pp. 139-144
    • Reinhold-Hurek, B.1    Hurek, T.2
  • 11
    • 0000859563 scopus 로고
    • Quantification of biological nitrogen fixation associated with sugar cane using a 15N-aided nitrogen balance
    • Lima, E., Boddey, R. M., Döbereiner, J., Quantification of biological nitrogen fixation associated with sugar cane using a 15N-aided nitrogen balance. Soil Biol. Biochem. 1987, 19, 165-170.
    • (1987) Soil Biol. Biochem , vol.19 , pp. 165-170
    • Lima, E.1    Boddey, R.M.2    Döbereiner, J.3
  • 12
    • 0028833960 scopus 로고
    • Biological nitrogen fixation in sugar cane: A key to energetically viable biofuel production
    • Boddey, R. M., Biological nitrogen fixation in sugar cane: a key to energetically viable biofuel production. Crit. Rev. Plant Sci. 1995, 14, 263-279.
    • (1995) Crit. Rev. Plant Sci , vol.14 , pp. 263-279
    • Boddey, R.M.1
  • 13
    • 0030857580 scopus 로고    scopus 로고
    • The contribution of biological nitrogen fixation for sustainable agricultural systems in tropics
    • Boddey, R. M., Sá, J. C. M., Alves, B. J., Urquiaga, S., The contribution of biological nitrogen fixation for sustainable agricultural systems in tropics. Soil Biol. Biochem. 1997, 29, 787-799.
    • (1997) Soil Biol. Biochem , vol.29 , pp. 787-799
    • Boddey, R.M.1    Sá, J.C.M.2    Alves, B.J.3    Urquiaga, S.4
  • 14
    • 0028119681 scopus 로고
    • Improved methodology for isolation of Acetobacter diazotrophicus and confirmation of its endophytic habitat
    • Reis, V. M., Olivares, F. L., Döbereiner, J., Improved methodology for isolation of Acetobacter diazotrophicus and confirmation of its endophytic habitat. World J. Microbiol. Biotechnol. 1994, 10, 401-405.
    • (1994) World J. Microbiol. Biotechnol , vol.10 , pp. 401-405
    • Reis, V.M.1    Olivares, F.L.2    Döbereiner, J.3
  • 15
    • 0002563277 scopus 로고
    • A new acid-tolerant nitrogen-fixing bacterium associated with sugarcane
    • Cavalcante, V. A., Döbereiner, J., A new acid-tolerant nitrogen-fixing bacterium associated with sugarcane. Plant Soil 1988, 108, 23-31.
    • (1988) Plant Soil , vol.108 , pp. 23-31
    • Cavalcante, V.A.1    Döbereiner, J.2
  • 16
    • 0042348365 scopus 로고    scopus 로고
    • Gluconacetobacter diazotrophicus (syn. Acetobacter diazotrophicus), a promising diazotrophic endophyte in tropics
    • Muthukumarasamy, R., Revathi, G., Seshadri, S., Lakshminarasimhan, C., Gluconacetobacter diazotrophicus (syn. Acetobacter diazotrophicus), a promising diazotrophic endophyte in tropics. Curr. Sci. 2002, 83, 137-145.
    • (2002) Curr. Sci , vol.83 , pp. 137-145
    • Muthukumarasamy, R.1    Revathi, G.2    Seshadri, S.3    Lakshminarasimhan, C.4
  • 17
    • 0026279709 scopus 로고
    • Biological nitrogen fixation associated with sugarcane
    • Boddey, R. M., Urquiaga, S., Reis, V., Döbereiner, J., Biological nitrogen fixation associated with sugarcane. Plant Soil 1991, 137, 111-117.
    • (1991) Plant Soil , vol.137 , pp. 111-117
    • Boddey, R.M.1    Urquiaga, S.2    Reis, V.3    Döbereiner, J.4
  • 19
    • 0031939581 scopus 로고    scopus 로고
    • Production of indole-3-acetic acid and gibberellins A1 y A3 by Acetobacter diazotrophicus and Herbaspirillum seropedicae in chemically-defined culture media
    • Bastian, F., Cohen, A., Piccoli, P., Luna, V., Baraldi, R., Production of indole-3-acetic acid and gibberellins A1 y A3 by Acetobacter diazotrophicus and Herbaspirillum seropedicae in chemically-defined culture media. Plant Growth Reg. 1998, 24, 7-11.
    • (1998) Plant Growth Reg , vol.24 , pp. 7-11
    • Bastian, F.1    Cohen, A.2    Piccoli, P.3    Luna, V.4    Baraldi, R.5
  • 20
    • 0000297851 scopus 로고    scopus 로고
    • Acetobacter diazotrophicus, and indolacetic acid producing bacterium isolated from sugarcane cultivars of Mexico
    • Fuentes-Ramirez, L. E., Jimenez-Salgado, T., Abarca-Ocampo, I. R., Caballero-Mellado, J., Acetobacter diazotrophicus, and indolacetic acid producing bacterium isolated from sugarcane cultivars of Mexico. Plant Soil 2003, 154, 145-150.
    • (2003) Plant Soil , vol.154 , pp. 145-150
    • Fuentes-Ramirez, L.E.1    Jimenez-Salgado, T.2    Abarca-Ocampo, I.R.3    Caballero-Mellado, J.4
  • 21
    • 0036337590 scopus 로고    scopus 로고
    • Gluconacetobacter diazotrophicus, a sugar cane endosymbiont, produces a bacteriocin against Xanthomonas albilineans, a sugar cane pathogen
    • Pinon, D., Casas, M., Blanch, M., Fontaniella, B. et al., Gluconacetobacter diazotrophicus, a sugar cane endosymbiont, produces a bacteriocin against Xanthomonas albilineans, a sugar cane pathogen. Res. Microbiol. 2002, 153, 345-351.
    • (2002) Res. Microbiol , vol.153 , pp. 345-351
    • Pinon, D.1    Casas, M.2    Blanch, M.3    Fontaniella, B.4
  • 22
    • 0009957151 scopus 로고    scopus 로고
    • Antagonistic potential of N2-fixing Acetobacter diazotrophicus against Colletotrichum falcatum Went., a causal of red-rot of sugarcane
    • Muthukumarasamy, R., Rebathi, G., Vadivelu, M., Antagonistic potential of N2-fixing Acetobacter diazotrophicus against Colletotrichum falcatum Went., a causal of red-rot of sugarcane. Curr. Sci. 2000, 78, 1063-1065.
    • (2000) Curr. Sci , vol.78 , pp. 1063-1065
    • Muthukumarasamy, R.1    Rebathi, G.2    Vadivelu, M.3
  • 23
    • 3242808951 scopus 로고    scopus 로고
    • A type II protein secretory pathway required for levansucrase secretion by Gluconacetobacter diazotrophicus
    • Arrieta, J. G., Sotolongo, M., Menendez, C., Alfonso, D. et al., A type II protein secretory pathway required for levansucrase secretion by Gluconacetobacter diazotrophicus. J Bacteriol. 2004, 186, 5031-5039.
    • (2004) J Bacteriol , vol.186 , pp. 5031-5039
    • Arrieta, J.G.1    Sotolongo, M.2    Menendez, C.3    Alfonso, D.4
  • 24
    • 0033888323 scopus 로고    scopus 로고
    • Structural levansucrase gene (lsdA) constitutes a functional locus conserved in the species Gluconacetobacter diazotrophicus
    • Hernandez, L., Sotolongo, M., Rosabal, Y., Menendez, C. et al., Structural levansucrase gene (lsdA) constitutes a functional locus conserved in the species Gluconacetobacter diazotrophicus. Arch. Microbiol. 2000, 174, 120-124.
    • (2000) Arch. Microbiol , vol.174 , pp. 120-124
    • Hernandez, L.1    Sotolongo, M.2    Rosabal, Y.3    Menendez, C.4
  • 25
    • 0032698768 scopus 로고    scopus 로고
    • The respiratory system and diazotrophic activity of Acetobacter diazotrophicus PAL5
    • Flores-Encarnacion, M., Contreras-Zentella, M., Soto-Urzua, L., Aguilar, G. R. et al., The respiratory system and diazotrophic activity of Acetobacter diazotrophicus PAL5. J. Bacteriol. 1999, 181, 6987-6995.
    • (1999) J. Bacteriol , vol.181 , pp. 6987-6995
    • Flores-Encarnacion, M.1    Contreras-Zentella, M.2    Soto-Urzua, L.3    Aguilar, G.R.4
  • 26
    • 33845209354 scopus 로고    scopus 로고
    • Solubilization of zinc compounds by the diazotrophic, plant growth promoting bacterium Gluconacetobacter diazotrophicus
    • Saravanan, V. S., Madhaiyan, M., Thangaraju, M., Solubilization of zinc compounds by the diazotrophic, plant growth promoting bacterium Gluconacetobacter diazotrophicus. Chemosphere 2007, 66, 1794-1798.
    • (2007) Chemosphere , vol.66 , pp. 1794-1798
    • Saravanan, V.S.1    Madhaiyan, M.2    Thangaraju, M.3
  • 28
    • 0035119414 scopus 로고    scopus 로고
    • Comparison of benefit to sugarcane plant growth and 15N2 incorporation following inoculation of sterile plants with Acetobacter diazotrophicus wild-type and Nif-mutants strains
    • Sevilla, M., Burris, R. H., Gunapala, N., Kennedy, C., Comparison of benefit to sugarcane plant growth and 15N2 incorporation following inoculation of sterile plants with Acetobacter diazotrophicus wild-type and Nif-mutants strains. Mol. Plant Microbe Interact. 2001, 14, 358-366.
    • (2001) Mol. Plant Microbe Interact , vol.14 , pp. 358-366
    • Sevilla, M.1    Burris, R.H.2    Gunapala, N.3    Kennedy, C.4
  • 29
    • 0038497512 scopus 로고    scopus 로고
    • Endophytic nitrogen fixation in sugarcane: Present knowledge and future applications
    • Boddey, R. M., Urquiaga, S., Alves, J. R. B., Reis, V., Endophytic nitrogen fixation in sugarcane: present knowledge and future applications. Plant Soil 2003, 252, 139-149.
    • (2003) Plant Soil , vol.252 , pp. 139-149
    • Boddey, R.M.1    Urquiaga, S.2    Alves, J.R.B.3    Reis, V.4
  • 30
    • 0000954824 scopus 로고
    • Biological nitrogen fixation associated with sugar cane and rice: Contributions and prospects for improvement
    • Boddey, R. M., de Oliveira, O. C., Urquiaga, S., Reis, V. M. et al., Biological nitrogen fixation associated with sugar cane and rice: contributions and prospects for improvement. Plant Soil 1995, 90, 195-209.
    • (1995) Plant Soil , vol.90 , pp. 195-209
    • Boddey, R.M.1    de Oliveira, O.C.2    Urquiaga, S.3    Reis, V.M.4
  • 31
    • 24344510274 scopus 로고    scopus 로고
    • special emphasis on the Brazilian experience
    • History on the biological nitrogen fixation research in graminaceous plants
    • Baldani, J. I., Baldani, V. L., History on the biological nitrogen fixation research in graminaceous plants: special emphasis on the Brazilian experience. An Acad Bras Cienc 2005, 77, 549-579.
    • (2005) An Acad Bras Cienc , vol.77 , pp. 549-579
    • Baldani, J.I.1    Baldani, V.L.2
  • 32
    • 0001884783 scopus 로고
    • Meio simples para isolamento e cultivo de Xanthomonas campestris pv. citri Tipo B.
    • Rodrigues Neto, J., Malavolta Jr., V. A., Victor, O., Meio simples para isolamento e cultivo de Xanthomonas campestris pv. citri Tipo B. Summa Phytopathol. 1986, 12, 16.
    • (1986) Summa Phytopathol , vol.12 , pp. 16
    • Rodrigues Neto, J.1    Malavolta Jr., V.A.2    Victor, O.3
  • 35
    • 0028983813 scopus 로고
    • Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing
    • Hellman, U., Wernstedt, C., Gonez, J., Heldin, C. H., Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing. Anal. Biochem. 1995, 224, 451-455.
    • (1995) Anal. Biochem , vol.224 , pp. 451-455
    • Hellman, U.1    Wernstedt, C.2    Gonez, J.3    Heldin, C.H.4
  • 36
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., Cottrell, J. S., Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20, 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 37
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and biossays with tobacco tissue cultures
    • Murashige, T., Skoog, F., A revised medium for rapid growth and biossays with tobacco tissue cultures. Physiol. Plant 1962, 15, 473-497.
    • (1962) Physiol. Plant , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 38
    • 0036665518 scopus 로고    scopus 로고
    • Enrichment of Integral Membrane Proteins for Proteomic Analysis Using Liquid Chromatography-tandem Mass Spectrometry
    • Blonder, J., Goshe, M. B., Moore, R. J., Pasa-Tolic, L., et al., Enrichment of Integral Membrane Proteins for Proteomic Analysis Using Liquid Chromatography-tandem Mass Spectrometry. J. Proteome Res. 2002, 1, 351-360.
    • (2002) J. Proteome Res , vol.1 , pp. 351-360
    • Blonder, J.1    Goshe, M.B.2    Moore, R.J.3    Pasa-Tolic, L.4
  • 39
    • 0020039866 scopus 로고
    • Isolation of Intracellular Membranes by Means of Sodium Carbonate Treatment : Application to Endoplasmic Reticulum
    • Fujiki, Y., Hubbard, A. L., Fowler, S., Lazarow, P. B., Isolation of Intracellular Membranes by Means of Sodium Carbonate Treatment : Application to Endoplasmic Reticulum. J. Cell Biol. 1982, 93, 97-102.
    • (1982) J. Cell Biol , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 40
    • 0024411870 scopus 로고
    • Protein measurement using Bicinchoninic acid: Elimination of interfering substances
    • Brown, R. E., Jarvis, K. L., Hyland, K. J., Protein measurement using Bicinchoninic acid: elimination of interfering substances. Anal. Biochem. 1989, 180, 136-139.
    • (1989) Anal. Biochem , vol.180 , pp. 136-139
    • Brown, R.E.1    Jarvis, K.L.2    Hyland, K.J.3
  • 42
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., Nesvizhskii, A. I., Kolker, E., Aebersold, R., Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 2002, 74, 5383-5392.
    • (2002) Anal. Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 43
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A. I., Keller, A., Kolker, E., Aebersold, R., A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 2003, 75, 4646-4658.
    • (2003) Anal. Chem , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 44
    • 0026823076 scopus 로고
    • Cloning and identification of the Escherichia coli murB DNA sequence, which encodes UDP-N-acetylenolpyruvoylglucosamine reductase
    • Pucci, M. J., Discotto, L. F., Dougherty, T. J., Cloning and identification of the Escherichia coli murB DNA sequence, which encodes UDP-N-acetylenolpyruvoylglucosamine reductase. J. Bacteriol. 1992, 174, 1690-1693.
    • (1992) J. Bacteriol , vol.174 , pp. 1690-1693
    • Pucci, M.J.1    Discotto, L.F.2    Dougherty, T.J.3
  • 45
    • 33745202589 scopus 로고    scopus 로고
    • YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli
    • Malinverni, J. C., Werner, J., Kim, S., Sklar, J. G. et al., YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli. Mol. Microbiol. 2006, 61, 151-164.
    • (2006) Mol. Microbiol , vol.61 , pp. 151-164
    • Malinverni, J.C.1    Werner, J.2    Kim, S.3    Sklar, J.G.4
  • 46
    • 23844507131 scopus 로고    scopus 로고
    • YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli
    • Werner, J., Misra, R., YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli. Mol. Microbiol. 2005, 57, 1450-1459.
    • (2005) Mol. Microbiol , vol.57 , pp. 1450-1459
    • Werner, J.1    Misra, R.2
  • 47
    • 0025134451 scopus 로고
    • Genetic analysis of an MDR-like export system: The secretion of colicin V
    • Gilson, L., Mahanty, H. K., Kolter, R., Genetic analysis of an MDR-like export system: the secretion of colicin V. Embo J 1990, 9, 3875-3884.
    • (1990) Embo J , vol.9 , pp. 3875-3884
    • Gilson, L.1    Mahanty, H.K.2    Kolter, R.3
  • 48
    • 0035339953 scopus 로고    scopus 로고
    • Driessen, A. J., SecB, a molecular chaperone with two faces. Trends Microbiol. 2001, 9, 193-196.
    • Driessen, A. J., SecB, a molecular chaperone with two faces. Trends Microbiol. 2001, 9, 193-196.
  • 50
    • 0035116079 scopus 로고    scopus 로고
    • SoxR-dependent response to oxidative stress and virulence of Erwinia chrysanthemi: The key role of SufC, an orphan ABC ATPase
    • Nachin, L., El Hassouni, M., Loiseau, L., Expert, D., Barras, F., SoxR-dependent response to oxidative stress and virulence of Erwinia chrysanthemi: the key role of SufC, an orphan ABC ATPase. Mol. Microbiol. 2001, 39, 960-972.
    • (2001) Mol. Microbiol , vol.39 , pp. 960-972
    • Nachin, L.1    El Hassouni, M.2    Loiseau, L.3    Expert, D.4    Barras, F.5
  • 51
    • 0021881068 scopus 로고
    • Nucleotide sequence of the genes involved in phosphate transport and regulation of the phosphate regulon in Escherichia coli
    • Amemura, M., Makino, K., Shinagawa, H., Kobayashi, A., Nakata, A., Nucleotide sequence of the genes involved in phosphate transport and regulation of the phosphate regulon in Escherichia coli. J. Mol. Biol. 1985, 184, 241-250.
    • (1985) J. Mol. Biol , vol.184 , pp. 241-250
    • Amemura, M.1    Makino, K.2    Shinagawa, H.3    Kobayashi, A.4    Nakata, A.5
  • 52
    • 34250218203 scopus 로고    scopus 로고
    • PhoU is a persistence switch involved in persister formation and tolerance to multiple antibiotics and stresses in Escherichia coli
    • Li, Y., Zhang, Y., PhoU is a persistence switch involved in persister formation and tolerance to multiple antibiotics and stresses in Escherichia coli. Antimicrobial Agents Chemother. 2007, 51, 2092-2099.
    • (2007) Antimicrobial Agents Chemother , vol.51 , pp. 2092-2099
    • Li, Y.1    Zhang, Y.2
  • 53
    • 0033569296 scopus 로고    scopus 로고
    • Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 A resolution
    • Abergel, C., Bouveret, E., Claverie, J. M., Brown, K. et al., Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 A resolution. Structure 1999, 7, 1291-1300.
    • (1999) Structure , vol.7 , pp. 1291-1300
    • Abergel, C.1    Bouveret, E.2    Claverie, J.M.3    Brown, K.4
  • 54
    • 0033819377 scopus 로고    scopus 로고
    • Characterization and expression of HmuR, a TonB-dependent hemoglobin receptor of Porphyromonas gingivalis
    • Simpson, W., Olczak, T., Genco, C. A., Characterization and expression of HmuR, a TonB-dependent hemoglobin receptor of Porphyromonas gingivalis. J. Bacteriol. 2000, 182, 5737-5748.
    • (2000) J. Bacteriol , vol.182 , pp. 5737-5748
    • Simpson, W.1    Olczak, T.2    Genco, C.A.3
  • 56
    • 0028310634 scopus 로고
    • Insertion of proteins into membranes. A survey
    • Geli, V., Benedetti, H., Insertion of proteins into membranes. A survey. Subcell. Biochem. 1994, 22, 21-69.
    • (1994) Subcell. Biochem , vol.22 , pp. 21-69
    • Geli, V.1    Benedetti, H.2
  • 57
    • 0033777079 scopus 로고    scopus 로고
    • Nitrogenase: Standing at the crossroads
    • Rees, D. C., Howard, J. B., Nitrogenase: standing at the crossroads. Curr. Opin. Chem. Biol. 2000, 4, 559-566.
    • (2000) Curr. Opin. Chem. Biol , vol.4 , pp. 559-566
    • Rees, D.C.1    Howard, J.B.2
  • 58
    • 0028126007 scopus 로고
    • Nitrogenase and biological nitrogen fixation
    • Kim, J., Rees, D., Nitrogenase and biological nitrogen fixation. Biochemistry 1994, 33, 389-397.
    • (1994) Biochemistry , vol.33 , pp. 389-397
    • Kim, J.1    Rees, D.2
  • 59
    • 0030839934 scopus 로고    scopus 로고
    • Cell colonization and infection thread formation in sugar cane roots by Acetobacter diazotrophicus
    • Bellone, C. H., De Bellone, S. D. V. C., Pedraza, R. O., Monzon, M. A., Cell colonization and infection thread formation in sugar cane roots by Acetobacter diazotrophicus. Soil Biology & Biochemistry 1997, 29, 965-967.
    • (1997) Soil Biology & Biochemistry , vol.29 , pp. 965-967
    • Bellone, C.H.1    De Bellone, S.D.V.C.2    Pedraza, R.O.3    Monzon, M.A.4
  • 60
    • 0034460606 scopus 로고    scopus 로고
    • Characterization of a major cluster of nif, fix, and associated genes in a sugarcane endophyte, Acetobacter diazotrophicus
    • Lee, S., Reth, A., Meletzus, D., Sevilla, M., Kennedy, C., Characterization of a major cluster of nif, fix, and associated genes in a sugarcane endophyte, Acetobacter diazotrophicus. J. Bacteriol. 2000, 182, 7088-7091.
    • (2000) J. Bacteriol , vol.182 , pp. 7088-7091
    • Lee, S.1    Reth, A.2    Meletzus, D.3    Sevilla, M.4    Kennedy, C.5
  • 61
    • 0026335765 scopus 로고
    • Characterization of a novel Azorhizobium caulinodans ORS571 two-component regulatory system, NtrY/NtrX, involved in nitrogen fixation and metabolism
    • Pawlowski, K., Klosse, U., de Bruijn, F. J., Characterization of a novel Azorhizobium caulinodans ORS571 two-component regulatory system, NtrY/NtrX, involved in nitrogen fixation and metabolism. Mol. Gen. Genet. 1991, 231, 124-138.
    • (1991) Mol. Gen. Genet , vol.231 , pp. 124-138
    • Pawlowski, K.1    Klosse, U.2    de Bruijn, F.J.3
  • 62
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U., Molecular chaperones in cellular protein folding. Nature 1996, 381, 571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 63
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick, J. P., Hartl, F. U., Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 1993, 62, 349-384.
    • (1993) Annu. Rev. Biochem , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 64
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar, S. W., Kolter, R., SurA assists the folding of Escherichia coli outer membrane proteins. J. Bacteriol. 1996, 178, 1770-1773.
    • (1996) J. Bacteriol , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 65
    • 0024044382 scopus 로고
    • Ancient heat shock gene is dispensable
    • Bardwell, J. C., Craig, E. A., Ancient heat shock gene is dispensable. J. Bacteriol. 1988, 170, 2977-2983.
    • (1988) J. Bacteriol , vol.170 , pp. 2977-2983
    • Bardwell, J.C.1    Craig, E.A.2
  • 66
    • 0032840055 scopus 로고    scopus 로고
    • HtpG is essential for the thermal stress management in cyanobacteria
    • Tanaka, N., Nakamoto, H., HtpG is essential for the thermal stress management in cyanobacteria. FEBS Lett. 1999, 458, 117-123.
    • (1999) FEBS Lett , vol.458 , pp. 117-123
    • Tanaka, N.1    Nakamoto, H.2
  • 67
    • 0041909570 scopus 로고    scopus 로고
    • Bacterial cold shock responses
    • Weber, M. H., Marahiel, M. A., Bacterial cold shock responses. Sci. Progr. 2003, 86, 9-75.
    • (2003) Sci. Progr , vol.86 , pp. 9-75
    • Weber, M.H.1    Marahiel, M.A.2
  • 70
    • 0036033601 scopus 로고    scopus 로고
    • The gene bolA regulates dacA (PBP5), dacC (PBP6) and ampC (AmpC), promoting normal morphology in Escherichia coli
    • Santos, J. M., Lobo, M., Matos, A. P., De Pedro, M. A., Arraiano, C. M., The gene bolA regulates dacA (PBP5), dacC (PBP6) and ampC (AmpC), promoting normal morphology in Escherichia coli. Mol. Microbiol. 2002, 45, 1729-1740.
    • (2002) Mol. Microbiol , vol.45 , pp. 1729-1740
    • Santos, J.M.1    Lobo, M.2    Matos, A.P.3    De Pedro, M.A.4    Arraiano, C.M.5
  • 71
    • 0032512051 scopus 로고    scopus 로고
    • The genome sequence of Rickettsia prowazekiī and the origin of mitochondria
    • Andersson, S. G., Zomorodipour, A., Andersson, J. O., Sicheritz-Ponten, T. et al., The genome sequence of Rickettsia prowazekiī and the origin of mitochondria. Nature 1998, 396, 133-140.
    • (1998) Nature , vol.396 , pp. 133-140
    • Andersson, S.G.1    Zomorodipour, A.2    Andersson, J.O.3    Sicheritz-Ponten, T.4
  • 72
    • 0029257384 scopus 로고    scopus 로고
    • Keller, M., Roxlau, A., Weng, W. M., Schmidt, M. et al., Molecular analysis of the Rhizobium meliloti mucR gene regulating the biosynthesis of the exopolysaccharides succinoglycan and galactoglucan. Mol- Plant Microbe Interact-1995, 8, 267-277.
    • Keller, M., Roxlau, A., Weng, W. M., Schmidt, M. et al., Molecular analysis of the Rhizobium meliloti mucR gene regulating the biosynthesis of the exopolysaccharides succinoglycan and galactoglucan. Mol- Plant Microbe Interact-1995, 8, 267-277.
  • 73
    • 0031973432 scopus 로고    scopus 로고
    • Succinoglycan production by Rhizobium meliloti is regulated through the ExoS-Chvl two-component regulatory system
    • Cheng, H. P., Walker, G. C., Succinoglycan production by Rhizobium meliloti is regulated through the ExoS-Chvl two-component regulatory system. J. Bacteriol. 1998, 180, 20-26.
    • (1998) J. Bacteriol , vol.180 , pp. 20-26
    • Cheng, H.P.1    Walker, G.C.2
  • 74
    • 0025863496 scopus 로고
    • Glucose metabolism and gluconic acid production by Acetobacter diazotrophicus
    • Attwood, M. M., van Dijken, J. P., Pronk, J. T., Glucose metabolism and gluconic acid production by Acetobacter diazotrophicus. J. Ferment. Bioeng. 1991, 72, 101-105.
    • (1991) J. Ferment. Bioeng , vol.72 , pp. 101-105
    • Attwood, M.M.1    van Dijken, J.P.2    Pronk, J.T.3
  • 75
    • 33644616684 scopus 로고    scopus 로고
    • Glucose metabolism in batch and continuous cultures of Gluconacetobacter diazotrophicus PAL 3
    • Luna, M. F., Bernardelli, C. E., Galar, M. L., Boiardi, J. L., Glucose metabolism in batch and continuous cultures of Gluconacetobacter diazotrophicus PAL 3. Curr Microbiol 2006, 52, 163-168.
    • (2006) Curr Microbiol , vol.52 , pp. 163-168
    • Luna, M.F.1    Bernardelli, C.E.2    Galar, M.L.3    Boiardi, J.L.4
  • 76
    • 0028826244 scopus 로고
    • Metabolic characterization of Acetobacter diazotrophicus
    • Alvarez, B., Martínez-Drets, G., Metabolic characterization of Acetobacter diazotrophicus. Can. J. Microbiol. 1995, 41, 918-924.
    • (1995) Can. J. Microbiol , vol.41 , pp. 918-924
    • Alvarez, B.1    Martínez-Drets, G.2
  • 77
    • 0014374541 scopus 로고
    • The occurrence of the Entner-Doudoroff pathway in bacteria
    • Kersters, K., De Ley, J., The occurrence of the Entner-Doudoroff pathway in bacteria. Antonie van Leeuwenhoek 1968, 34, 393-408.
    • (1968) Antonie van Leeuwenhoek , vol.34 , pp. 393-408
    • Kersters, K.1    De Ley, J.2
  • 78
    • 13844297220 scopus 로고    scopus 로고
    • Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans
    • Prust, C., Hoffmeister, M., Liesegang, H., Wiezer, A. et al., Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans. Nat. Biotechnol. 2005, 23, 195-200.
    • (2005) Nat. Biotechnol , vol.23 , pp. 195-200
    • Prust, C.1    Hoffmeister, M.2    Liesegang, H.3    Wiezer, A.4
  • 79
    • 42549160768 scopus 로고    scopus 로고
    • De Ley, J., Gillis, M., Swings, J., Family VI. Acetobacteraceae. In: Bergey's Manual of Systematic Bacteriology, Williams & Williams, Baltimore, MD 1984, pp. 2268-2285.
    • De Ley, J., Gillis, M., Swings, J., Family VI. Acetobacteraceae. In: Bergey's Manual of Systematic Bacteriology, Williams & Williams, Baltimore, MD 1984, pp. 2268-2285.
  • 80
    • 0347818601 scopus 로고
    • The dissimilation of glucose and gluconate by Acetobacter xylinum. 1. The origin and the fate of triose phosphate
    • White, G. A., Wang, C. H., The dissimilation of glucose and gluconate by Acetobacter xylinum. 1. The origin and the fate of triose phosphate. Biochem. J. 1964, 90, 408-423.
    • (1964) Biochem. J , vol.90 , pp. 408-423
    • White, G.A.1    Wang, C.H.2
  • 81
    • 0015465291 scopus 로고
    • Nonfunctional tricarboxylic acid cycle and the mechanism of glutamate biosynthesis in Acetobacter suboxydans
    • Greenfield, S., Claus, G. W., Nonfunctional tricarboxylic acid cycle and the mechanism of glutamate biosynthesis in Acetobacter suboxydans. J. Bacteriol. 1972, 112, 1295-1301.
    • (1972) J. Bacteriol , vol.112 , pp. 1295-1301
    • Greenfield, S.1    Claus, G.W.2
  • 83
    • 42549151382 scopus 로고    scopus 로고
    • Sievers, M., Swings, J., Genus VIII. Gluconacetobacter, in: Garrity, G. M, (Ed.), Bergey's Manual of Systematic Bacteriology, Springer-Verlag, New York 2005, pp. 72-77.
    • Sievers, M., Swings, J., Genus VIII. Gluconacetobacter, in: Garrity, G. M, (Ed.), Bergey's Manual of Systematic Bacteriology, Springer-Verlag, New York 2005, pp. 72-77.
  • 84
    • 33751511740 scopus 로고    scopus 로고
    • Respiratory system of Gluconacetobacter diazotrophicus PAL5 Evidence for a cyanide-sensitive cytochrome bb and cyanide-resistant cytochrome ba quinol oxidases
    • Gonzalez, B., Martinez, S., Chavez, J. L., Lee, S. et al., Respiratory system of Gluconacetobacter diazotrophicus PAL5 Evidence for a cyanide-sensitive cytochrome bb and cyanide-resistant cytochrome ba quinol oxidases. Biochim. Biophys. Acta 2006, 1757, 1614-1622.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1614-1622
    • Gonzalez, B.1    Martinez, S.2    Chavez, J.L.3    Lee, S.4
  • 85
    • 0026081956 scopus 로고
    • Cloning and sequencing of the gene cluster encoding two subunits of membrane-bound alcohol dehydrogenase from Acetobacter polyoxogenes
    • Tamaki, T., Fukaya, M., Takemura, H., Tayama, K. et al., Cloning and sequencing of the gene cluster encoding two subunits of membrane-bound alcohol dehydrogenase from Acetobacter polyoxogenes. Biochim. Biophys. Acta 1991, 1088, 292-300.
    • (1991) Biochim. Biophys. Acta , vol.1088 , pp. 292-300
    • Tamaki, T.1    Fukaya, M.2    Takemura, H.3    Tayama, K.4
  • 86
    • 0030849308 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of the acetaldehyde dehydrogenase complex from Acetobacter europaeus
    • Thurner, C., Vela, C., Thony-Meyer, L., Meile, L., Teuber, M., Biochemical and genetic characterization of the acetaldehyde dehydrogenase complex from Acetobacter europaeus. Arch. Microbiol. 1997, 168, 81-91.
    • (1997) Arch. Microbiol , vol.168 , pp. 81-91
    • Thurner, C.1    Vela, C.2    Thony-Meyer, L.3    Meile, L.4    Teuber, M.5
  • 87
    • 0032545706 scopus 로고    scopus 로고
    • Cloning, sequence and expression of a linear plasmid-based and a chromosomal homolog of chloroacetaldehyde dehydrogenase-encoding genes in Xanthobacter autotrophicus GJ10
    • Bergeron, H., Labbe, D., Turmel, C., Lau, P. C., Cloning, sequence and expression of a linear plasmid-based and a chromosomal homolog of chloroacetaldehyde dehydrogenase-encoding genes in Xanthobacter autotrophicus GJ10. Gene 1998, 207, 9-18.
    • (1998) Gene , vol.207 , pp. 9-18
    • Bergeron, H.1    Labbe, D.2    Turmel, C.3    Lau, P.C.4
  • 88
    • 0023129665 scopus 로고
    • Genetic and structural analysis of the Rhizobium meliloti fixA, fixB, fixC, and fixX genes
    • Earl, C. D., Ronson, C. W., Ausubel, F. M., Genetic and structural analysis of the Rhizobium meliloti fixA, fixB, fixC, and fixX genes. J. Bacteriol. 1987, 169, 1127-1136.
    • (1987) J. Bacteriol , vol.169 , pp. 1127-1136
    • Earl, C.D.1    Ronson, C.W.2    Ausubel, F.M.3
  • 89
    • 0021736002 scopus 로고
    • Gluconoacetobacter, a new subgenus comprising the acetate-oxidizing acetic acid bacteria with ubiquinone-10 in the genus Acetobacter
    • Yamada, Y., Kondo, K., Gluconoacetobacter, a new subgenus comprising the acetate-oxidizing acetic acid bacteria with ubiquinone-10 in the genus Acetobacter. J. Gen. Appl. Microbiol. 1984, 30, 297-303.
    • (1984) J. Gen. Appl. Microbiol , vol.30 , pp. 297-303
    • Yamada, Y.1    Kondo, K.2
  • 90
    • 0034571905 scopus 로고    scopus 로고
    • Ubiquinone. Biosynthesis of quinone ring and its isoprenoid side chain. Intracellular localization
    • Szkopinska, A., Ubiquinone. Biosynthesis of quinone ring and its isoprenoid side chain. Intracellular localization. Acta Biochimica Polonica 2000, 47, 469-480.
    • (2000) Acta Biochimica Polonica , vol.47 , pp. 469-480
    • Szkopinska, A.1
  • 91
    • 0027337396 scopus 로고
    • Characterization of a cytochrome a1 that functions as a ubiquinol oxidase in Acetobacter aceti
    • Fukaya, M., Tayama, K., Tamaki, T., Ebisuya, H. et al., Characterization of a cytochrome a1 that functions as a ubiquinol oxidase in Acetobacter aceti. J. Bacteriol. 1993, 175, 4307-4314.
    • (1993) J. Bacteriol , vol.175 , pp. 4307-4314
    • Fukaya, M.1    Tayama, K.2    Tamaki, T.3    Ebisuya, H.4


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