메뉴 건너뛰기




Volumn 157, Issue 3, 2011, Pages 899-910

Transcriptome response to different carbon sources in Acetobacter aceti

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; ALCOHOL; ALCOHOL DEHYDROGENASE; BACTERIAL DNA; BACTERIAL PROTEIN; CATALASE; CYANIDE; GLUCOSE; OXIDOREDUCTASE; PYRROLOQUINOLINEQUINONE; QUINOL OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SOS PROTEIN; SUPEROXIDE DISMUTASE; TRANSCRIPTOME; TRICARBOXYLIC ACID; UBIQUINONE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 79952253992     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.045906-0     Document Type: Article
Times cited : (59)

References (40)
  • 3
    • 0032900737 scopus 로고    scopus 로고
    • CRITICA: Coding region identification tool invoking comparative analysis
    • Badger, J. H. & Olsen, G. J. (1999). CRITICA: coding region identification tool invoking comparative analysis. Mol Biol Evol 16, 512-524. (Pubitemid 29190958)
    • (1999) Molecular Biology and Evolution , vol.16 , Issue.4 , pp. 512-524
    • Badger, J.H.1    Olsen, G.J.2
  • 4
    • 68949158532 scopus 로고    scopus 로고
    • Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase
    • Bekker, M., de Vries, S., Ter Beek, A., Hellingwerf, K. J. & Teixeira de Mattos, M. J. (2009). Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase. J Bacteriol 191, 5510-5517.
    • (2009) J Bacteriol , vol.191 , pp. 5510-5517
    • Bekker, M.1    De Vries, S.2    Ter Beek, A.3    Hellingwerf, K.J.4    Teixeira De Mattos, M.J.5
  • 5
    • 70449482476 scopus 로고    scopus 로고
    • Complete genome sequence of the sugarcane nitrogen-fixing endophyte Gluconacetobacter diazotrophicus Pal5
    • Bertalan,M., Albano, R., de Pádua, V., Rouws, L., Rojas, C., Hemerly, A., Teixeira, K., Schwab, S., Araujo, J. & other authors (2009). Complete genome sequence of the sugarcane nitrogen-fixing endophyte Gluconacetobacter diazotrophicus Pal5. BMC Genomics 10, 450.
    • (2009) BMC Genomics , vol.10 , pp. 450
    • Albano, R.1    De Pádua, V.2    Rouws, L.3    Rojas, C.4    Hemerly, A.5    Teixeira, K.6    Schwab, S.7    Araujo, J.8
  • 6
    • 0037316303 scopus 로고    scopus 로고
    • A comparison of normalization methods for high density oligonucleotide array data based on variance and bias
    • DOI 10.1093/bioinformatics/19.2.185
    • Bolstad, B. M., Irizarry, R. A., Astrand, M. & Speed, T. P. (2003). A comparison of normalization methods for high density oligonucleotide array data based on variance and bias. Bioinformatics 19, 185-193. (Pubitemid 36181903)
    • (2003) Bioinformatics , vol.19 , Issue.2 , pp. 185-193
    • Bolstad, B.M.1    Irizarry, R.A.2    Astrand, M.3    Speed, T.P.4
  • 7
    • 0027155827 scopus 로고
    • Energetic efficiency of Escherichia coli: Effects of mutations in components of the aerobic respiratory chain
    • Calhoun, M. W., Oden, K. L., Gennis, R. B., Teixeira de Mattos, M. J. & Neijssel, O. M. (1993). Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain. J Bacteriol 175, 3020-3025. (Pubitemid 23148736)
    • (1993) Journal of Bacteriology , vol.175 , Issue.10 , pp. 3020-3025
    • Calhoun, M.W.1    Oden, K.L.2    Gennis, R.B.3    De Mattos, M.J.T.4    Neijssel, O.M.5
  • 8
    • 0348121147 scopus 로고    scopus 로고
    • Purification and characterization of two NAD-dependent alcohol dehydrogenases (ADHs) induced in the quinoprotein ADH-deficient mutant of Acetobacter pasteurianus SKU1108
    • Chinnawirotpisan, P., Matsushita, K., Toyama, H., Adachi, O., Limtong, S. & Theeragool, G. (2003). Purification and characterization of two NAD-dependent alcohol dehydrogenases (ADHs) induced in the quinoprotein ADH-deficient mutant of Acetobacter pasteurianus SKU1108. Biosci Biotechnol Biochem 67, 958-965. (Pubitemid 39251852)
    • (2003) Bioscience, Biotechnology and Biochemistry , vol.67 , Issue.5 , pp. 958-965
    • Chinnawirotpisan, P.1    Matsushita, K.2    Toyama, H.3    Adachi, O.4    Limtong, S.5    Theeragool, G.6
  • 9
    • 0030915436 scopus 로고    scopus 로고
    • The cioAB genes from Pseudomonas aeruginosa code for a novel cyanide- insensitive terminal oxidase related to the cytochrome bd quinol oxidases
    • Cunningham, L., Pitt, M. & Williams, H. D. (1997). The cioAB genes from Pseudomonas aeruginosa code for a novel cyanide-insensitive terminal oxidase related to the cytochrome bd quinol oxidases. Mol Microbiol 24, 579-591. (Pubitemid 27241705)
    • (1997) Molecular Microbiology , vol.24 , Issue.3 , pp. 579-591
    • Cunningham, L.1    Pitt, M.2    Williams, H.D.3
  • 11
    • 0037210588 scopus 로고    scopus 로고
    • Biochemistry and biotechnological applications of Gluconobacter strains
    • Deppenmeier, U., Hoffmeister, M. & Prust, C. (2002). Biochemistry and biotechnological applications of Gluconobacter strains. Appl Microbiol Biotechnol 60, 233-242.
    • (2002) Appl Microbiol Biotechnol , vol.60 , pp. 233-242
    • Deppenmeier, U.1    Hoffmeister, M.2    Prust, C.3
  • 12
    • 0024416873 scopus 로고
    • Control of carbon flux to acetate excretion during growth of Escherichia coli in batch and continuous cultures
    • el-Mansi, E. M. & Holms, W. H. (1989). Control of carbon flux to acetate excretion during growth of Escherichia coli in batch and continuous cultures. J Gen Microbiol 135, 2875-2883.
    • (1989) J Gen Microbiol , vol.135 , pp. 2875-2883
    • El-Mansi, E.M.1    Holms, W.H.2
  • 15
    • 43149085041 scopus 로고    scopus 로고
    • De novo bacterial genome sequencing: Millions of very short reads assembled on a desktop computer
    • DOI 10.1101/gr.072033.107
    • Hernandez, D., François, P., Farinelli, L., Osteras, M. & Schrenzel, J. (2008). De novo bacterial genome sequencing: millions of very short reads assembled on a desktop computer. Genome Res 18, 802-809. (Pubitemid 351645070)
    • (2008) Genome Research , vol.18 , Issue.5 , pp. 802-809
    • Hernandez, D.1    Francois, P.2    Farinelli, L.3    Osteras, M.4    Schrenzel, J.5
  • 19
    • 0022401025 scopus 로고
    • The inhibition of acetate oxidation by ethanol in Acetobacter aceti
    • DOI 10.1007/BF00411251
    • Jucker, W. & Ettlinger, L. (1985). The inhibition of acetate oxidation by ethanol in Acetobacter aceti. Arch Microbiol 143, 283-289. (Pubitemid 16170885)
    • (1985) Archives of Microbiology , vol.143 , Issue.3 , pp. 283-289
    • Jucker, W.1    Ettlinger, L.2
  • 20
    • 0031018070 scopus 로고    scopus 로고
    • Characterization of the genes encoding the three-component membrane- bound alcohol dehydrogenase from Gluconobacter suboxydans and their expression in Acetobacter pasteurianus
    • Kondo, K. & Horinouchi, S. (1997). Characterization of the genes encoding the three-component membrane-bound alcohol dehydrogenase from Gluconobacter suboxydans and their expression in Acetobacter pasteurianus. Appl Environ Microbiol 63, 1131-1138. (Pubitemid 27098506)
    • (1997) Applied and Environmental Microbiology , vol.63 , Issue.3 , pp. 1131-1138
    • Kondo, K.1    Horinouchi, S.2
  • 21
    • 0000581636 scopus 로고
    • Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle
    • Kornberg, H. L. & Krebs, H. A. (1957). Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle. Nature 179, 988-991.
    • (1957) Nature , vol.179 , pp. 988-991
    • Kornberg, H.L.1    Krebs, H.A.2
  • 22
    • 77954289367 scopus 로고    scopus 로고
    • Metabolic engineering of Gluconobacter oxydans for improved growth rate and growth yield on glucose by elimination of gluconate formation
    • Krajewski, V., Simic, P., Mouncey, N. J., Bringer, S., Sahm, H. & Bott, M. (2010). Metabolic engineering of Gluconobacter oxydans for improved growth rate and growth yield on glucose by elimination of gluconate formation. Appl Environ Microbiol 76, 4369-4376.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 4369-4376
    • Krajewski, V.1    Simic, P.2    Mouncey, N.J.3    Bringer, S.4    Sahm, H.5    Bott, M.6
  • 23
    • 0029075136 scopus 로고
    • Isolation and characterization of the proton-translocating NADH: Ubiquinone oxidoreductase from Escherichia coli
    • Leif, H., Sled, V. D., Ohnishi, T., Weiss, H. & Friedrich, T. (1995). Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli. Eur J Biochem 230, 538-548.
    • (1995) Eur J Biochem , vol.230 , pp. 538-548
    • Leif, H.1    Sled, V.D.2    Ohnishi, T.3    Weiss, H.4    Friedrich, T.5
  • 24
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from microorganisms
    • Marmur, J. (1961). A procedure for the isolation of deoxyribonucleic acid from microorganisms. J Mol Biol 3, 208-218.
    • (1961) J Mol Biol , vol.3 , pp. 208-218
    • Marmur, J.1
  • 25
    • 85004631371 scopus 로고
    • Effect of extracellular pH on the respiratory chain and energetics of Gluconobacter suboxydans
    • Matsushita, K., Nagatani, Y., Shinagawa, E., Adachi, O. & Ameyama, M. (1989). Effect of extracellular pH on the respiratory chain and energetics of Gluconobacter suboxydans. Agric Biol Chem 53, 2895-2902.
    • (1989) Agric Biol Chem , vol.53 , pp. 2895-2902
    • Matsushita, K.1    Nagatani, Y.2    Shinagawa, E.3    Adachi, O.4    Ameyama, M.5
  • 26
    • 68649114125 scopus 로고    scopus 로고
    • Biochemical and spectroscopic properties of cyanide-insensitive quinol oxidase from Gluconobacter oxydans
    • Mogi, T., Ano, Y., Nakatsuka, T., Toyama, H., Muroi, A., Miyoshi, H., Migita, C. T., Ui, H., Shiomi, K. & other authors (2009). Biochemical and spectroscopic properties of cyanide-insensitive quinol oxidase from Gluconobacter oxydans. J Biochem 146, 263-271.
    • (2009) J Biochem , vol.146 , pp. 263-271
    • Mogi, T.1    Ano, Y.2    Nakatsuka, T.3    Toyama, H.4    Muroi, A.5    Miyoshi, H.6    Migita, C.T.7    Ui, H.8    Shiomi, K.9
  • 27
    • 47249128194 scopus 로고    scopus 로고
    • A specialized citric acid cycle requiring succinyl-coenzyme A (CoA):Acetate CoA-transferase (AarC) confers acetic acid resistance on the acidophile Acetobacter aceti
    • DOI 10.1128/JB.00405-08
    • Mullins, E. A., Francois, J. A. & Kappock, T. J. (2008). A specialized citric acid cycle requiring succinyl-coenzyme A (CoA) : acetate CoA-transferase (AarC) confers acetic acid resistance on the acidophile Acetobacter aceti. J Bacteriol 190, 4933-4940. (Pubitemid 351991061)
    • (2008) Journal of Bacteriology , vol.190 , Issue.14 , pp. 4933-4940
    • Mullins, E.A.1    Francois, J.A.2    Kappock, T.J.3
  • 28
    • 2942525951 scopus 로고    scopus 로고
    • Enhanced expression of aconitase raises acetic acid resistance in Acetobacter aceti
    • DOI 10.1016/j.femsle.2004.05.007, PII S0378109704003453
    • Nakano, S., Fukaya, M. & Horinouchi, S. (2004). Enhanced expression of aconitase raises acetic acid resistance in Acetobacter aceti. FEMS Microbiol Lett 235, 315-322. (Pubitemid 38746778)
    • (2004) FEMS Microbiology Letters , vol.235 , Issue.2 , pp. 315-322
    • Nakano, S.1    Fukaya, M.2    Horinouchi, S.3
  • 30
    • 55049126117 scopus 로고    scopus 로고
    • Hydrogen peroxide resistance of Acetobacter pasteurianus NBRC3283 and its relationship to acetic acid fermentation
    • Okamoto-Kainuma, A., Ehata, Y., Ikeda, M., Osono, T., Ishikawa, M., Kaga, T. & Koizumi, Y. (2008). Hydrogen peroxide resistance of Acetobacter pasteurianus NBRC3283 and its relationship to acetic acid fermentation. Biosci Biotechnol Biochem 72, 2526-2534.
    • (2008) Biosci Biotechnol Biochem , vol.72 , pp. 2526-2534
    • Okamoto-Kainuma, A.1    Ehata, Y.2    Ikeda, M.3    Osono, T.4    Ishikawa, M.5    Kaga, T.6    Koizumi, Y.7
  • 32
    • 0024962043 scopus 로고
    • Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli
    • Puustinen, A., Finel, M., Virkki, M. & Wikström, M. (1989). Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli. FEBS Lett 249, 163-167.
    • (1989) FEBS Lett , vol.249 , pp. 163-167
    • Puustinen, A.1    Finel, M.2    Virkki, M.3    Wikström, M.4
  • 36
    • 41549113464 scopus 로고    scopus 로고
    • Distinct physiological roles of two membrane-bound dehydrogenases responsible for D-sorbitol oxidation in Gluconobacter frateurii
    • DOI 10.1271/bbb.70720
    • Soemphol, W., Adachi, O., Matsushita, K. & Toyama, H. (2008). Distinct physiological roles of two membrane-bound dehydrogenases responsible for D-sorbitol oxidation in Gluconobacter frateurii. Biosci Biotechnol Biochem 72, 842-850. (Pubitemid 351463697)
    • (2008) Bioscience, Biotechnology and Biochemistry , vol.72 , Issue.3 , pp. 842-850
    • Soemphol, W.1    Adachi, O.2    Matsushita, K.3    Toyama, H.4
  • 37
    • 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., Okumura, H., Kawamura, Y., Nishiyama, M., Horinouchi, S. & Beppu, T. (1991). Cloning and sequencing of the gene cluster encoding two subunits of membrane-bound alcohol-dehydrogenase from Acetobacter polyoxogenes. Biochim Biophys Acta 1088, 292-300.
    • (1991) Biochim Biophys Acta , vol.1088 , pp. 292-300
    • Tamaki, T.1    Fukaya, M.2    Takemura, H.3    Tayama, K.4    Okumura, H.5    Kawamura, Y.6    Nishiyama, M.7    Horinouchi, S.8    Beppu, T.9
  • 39
    • 77952890162 scopus 로고    scopus 로고
    • Alcohol dehydrogenase of acetic acid bacteria: Structure, mode of action, and applications in biotechnology
    • Yakushi, T. & Matsushita, K. (2010). Alcohol dehydrogenase of acetic acid bacteria: structure, mode of action, and applications in biotechnology. Appl Microbiol Biotechnol 86, 1257-1265.
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 1257-1265
    • Yakushi, T.1    Matsushita, K.2
  • 40
    • 33846409026 scopus 로고    scopus 로고
    • Molecular characterization of the membrane-bound quinol peroxidase functionally connected to the respiratory chain
    • DOI 10.1111/j.1742-4658.2006.05637.x
    • Yamada, H., Takashima, E. & Konishi, K. (2007). Molecular characterization of the membrane-bound quinol peroxidase functionally connected to the respiratory chain. FEBS J 274, 853-866. (Pubitemid 46144044)
    • (2007) FEBS Journal , vol.274 , Issue.3 , pp. 853-866
    • Yamada, H.1    Takashima, E.2    Konishi, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.