메뉴 건너뛰기




Volumn 178, Issue 9, 1996, Pages 2668-2675

Molecular characterization and transcriptional analysis of the putative hydrogenase gene of Clostridium acetobutylicum ATCC 824

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGENASE;

EID: 0029863961     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.9.2668-2675.1996     Document Type: Article
Times cited : (88)

References (53)
  • 1
    • 0025000128 scopus 로고
    • The structure and mechanism of iron-hydrogenases
    • Adams, M. W. W. 1990. The structure and mechanism of iron-hydrogenases. Biochim. Biophys. Acta 1020:115-145
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 115-145
    • Adams, M.W.W.1
  • 4
    • 0021062517 scopus 로고
    • Level of enzymes involved in acetate, butyrate, acetone and butanol formation by Clostridium acetobutylicum
    • Andersch, W., H. Bahl, and G. Gottschalk. 1983. Level of enzymes involved in acetate, butyrate, acetone and butanol formation by Clostridium acetobutylicum. Eur. J. Appl. Microbiol. Biotechnol. 18:327-332.
    • (1983) Eur. J. Appl. Microbiol. Biotechnol. , vol.18 , pp. 327-332
    • Andersch, W.1    Bahl, H.2    Gottschalk, G.3
  • 5
    • 0025360449 scopus 로고
    • Recent developments in the field of iron-sulfur proteins
    • Beinert, H. 1990. Recent developments in the field of iron-sulfur proteins. FASEB J 4:2483-2491.
    • (1990) FASEB J , vol.4 , pp. 2483-2491
    • Beinert, H.1
  • 6
    • 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
  • 7
    • 0024095175 scopus 로고
    • Cloning and expression of Clostridium acetobutylicum phosphotransferase and butyrate kinase genes in Escherichia coli
    • Cary, J. W., D. J. Petersen, E. T. Papoutsakis, and G. N. Bennett. 1988. Cloning and expression of Clostridium acetobutylicum phosphotransferase and butyrate kinase genes in Escherichia coli. J. Bacteriol. 170:4613-4618.
    • (1988) J. Bacteriol. , vol.170 , pp. 4613-4618
    • Cary, J.W.1    Petersen, D.J.2    Papoutsakis, E.T.3    Bennett, G.N.4
  • 8
    • 7144230803 scopus 로고
    • Enzymatic amplification of DNA by PCR
    • F. A. Ausubel, R. Brent, R. E. Kingston, D D. Moore, J. G Seidman, J. A. Smith, and K. Struhl (ed.). Greene Publishing and Wiley Interscience, New York
    • Coen, D. M. 1991. Enzymatic amplification of DNA by PCR, p. 15.1.1-15 1.7. In F. A. Ausubel, R. Brent, R. E. Kingston, D D. Moore, J. G Seidman, J. A. Smith, and K. Struhl (ed.). Current protocols in molecular biology. Greene Publishing and Wiley Interscience, New York.
    • (1991) Current Protocols in Molecular Biology
    • Coen, D.M.1
  • 9
    • 0001936898 scopus 로고
    • Taxonomy of the clostridia wall composition and DNA homologies in Clostridium butyricum and other butyric acid-producing clostridia
    • Cummins, C. S., and J. L. Johnson. 1971. Taxonomy of the clostridia wall composition and DNA homologies in Clostridium butyricum and other butyric acid-producing clostridia. J. Gen. Microbiol. 67:33-46.
    • (1971) J. Gen. Microbiol. , vol.67 , pp. 33-46
    • Cummins, C.S.1    Johnson, J.L.2
  • 11
    • 0021909933 scopus 로고
    • Modulation of acetone-butanol-ethanol fermentation by carbon monoxide and organic acids
    • Datta, R., and J. G. Zeikus. 1985 Modulation of acetone-butanol-ethanol fermentation by carbon monoxide and organic acids. Appl. Environ Microbiol. 49:522-529.
    • (1985) Appl. Environ Microbiol. , vol.49 , pp. 522-529
    • Datta, R.1    Zeikus, J.G.2
  • 12
    • 0021245317 scopus 로고
    • Cyclic AMP receptor protein, role in transcription activation
    • DeCrombrugghe, B., S. Busby, and H. Buc. 1984. Cyclic AMP receptor protein, role in transcription activation. Science 224:831-838
    • (1984) Science , vol.224 , pp. 831-838
    • DeCrombrugghe, B.1    Busby, S.2    Buc, H.3
  • 13
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the Vax
    • Devereux, J., P. Haeberli, and O. Smithies. 1984 A comprehensive set of sequence analysis programs for the Vax. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 14
    • 0022077020 scopus 로고
    • Agitation and pressure effects on acetone-butanol fermentation
    • Doremus, M. G., J. C. Linden, and A. R. Moreira. 1984 Agitation and pressure effects on acetone-butanol fermentation. Biotechnol. Bioeng 27: 852-860
    • (1984) Biotechnol. Bioeng , vol.27 , pp. 852-860
    • Doremus, M.G.1    Linden, J.C.2    Moreira, A.R.3
  • 15
    • 0023410817 scopus 로고
    • Role of glutamic acid-181 in DNA-sequence recognition by the catabolic gene activator protein (CAP) of Escherichia coli altered DNA-sequence-recognition properties of [Va1181]CAP and [Leu181]CAP
    • Ebright, R. H., A. Kolb, H. Buc, T. A. Kunkel, J. S. Krakow, and J. Beckwith, 1087. Role of glutamic acid-181 in DNA-sequence recognition by the catabolic gene activator protein (CAP) of Escherichia coli altered DNA-sequence-recognition properties of [Va1181]CAP and [Leu181]CAP. Proc. Natl. Acad. Sci. USA 84:6083-6087.
    • (1087) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6083-6087
    • Ebright, R.H.1    Kolb, A.2    Buc, H.3    Kunkel, T.A.4    Krakow, J.S.5    Beckwith, J.6
  • 16
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., D. J. Osguthorpe, and B. Robson. 1978. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol 120:97-120.
    • (1978) J. Mol. Biol , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 17
    • 0026531061 scopus 로고
    • mRNA analysis of the adc gene region of Clostridium acetobutylicum during the shift to solventogenesis
    • Gerischer, U., and P. Dürre. 1992. mRNA analysis of the adc gene region of Clostridium acetobutylicum during the shift to solventogenesis. J. Bacteriol. 174:426-433.
    • (1992) J. Bacteriol. , vol.174 , pp. 426-433
    • Gerischer, U.1    Dürre, P.2
  • 18
    • 0028791403 scopus 로고
    • Regulation of metabolic shifts in Clostridium acetobutylicum ATCC
    • Girbal, L., C. Croux, I. Vasconcelos, and P. Soucaille. 1995. Regulation of metabolic shifts in Clostridium acetobutylicum ATCC FEMS Microbiol. Rev. 17:287-297.
    • (1995) FEMS Microbiol. Rev. , vol.17 , pp. 287-297
    • Girbal, L.1    Croux, C.2    Vasconcelos, I.3    Soucaille, P.4
  • 19
    • 0028907367 scopus 로고
    • How neutral red modified carbon and electron flow in Clostridium acetobutylicum grown in chemostat culture at neutral pH
    • Girbal, L., I. Vasconcelos, S. Saint-Amans, and P. Soucaille. 1995. How neutral red modified carbon and electron flow in Clostridium acetobutylicum grown in chemostat culture at neutral pH. FEMS Microbiol. Rev. 16:151-162.
    • (1995) FEMS Microbiol. Rev. , vol.16 , pp. 151-162
    • Girbal, L.1    Vasconcelos, I.2    Saint-Amans, S.3    Soucaille, P.4
  • 20
    • 0028095470 scopus 로고
    • Transmembrane pH of Clostridium acetobutylicum is inverted (more acidic inside) when the in vivo activity of hydrogenase is decreased
    • Girbal, L., I. Vasconcelos, and P. Soucaille. 1994. Transmembrane pH of Clostridium acetobutylicum is inverted (more acidic inside) when the in vivo activity of hydrogenase is decreased. J. Bacteriol. 176:6146-6147.
    • (1994) J. Bacteriol. , vol.176 , pp. 6146-6147
    • Girbal, L.1    Vasconcelos, I.2    Soucaille, P.3
  • 21
    • 37049233709 scopus 로고
    • Biological formation of molecular hydrogen
    • Gray, C. T., and H. Gest. 1965 Biological formation of molecular hydrogen. Science 148:186-192.
    • (1965) Science , vol.148 , pp. 186-192
    • Gray, C.T.1    Gest, H.2
  • 22
    • 0021112792 scopus 로고
    • Thiol reactivity of the nitrogenase Fe-protein from Azotobacter vinelandii
    • Hausinger, R. P., and J. B. Howard. 1983 Thiol reactivity of the nitrogenase Fe-protein from Azotobacter vinelandii. J. Biol. Chem. 258:13486-13492.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13486-13492
    • Hausinger, R.P.1    Howard, J.B.2
  • 23
    • 0022970603 scopus 로고
    • Acetone-butanol fermentation revisited
    • Jones, D. T., and D. R. Woods. 1986. Acetone-butanol fermentation revisited. Microbiol. Rev. 50:484-524.
    • (1986) Microbiol. Rev. , vol.50 , pp. 484-524
    • Jones, D.T.1    Woods, D.R.2
  • 25
    • 0021148147 scopus 로고
    • Control of carbon and electron flow in Clostridium acetobutylicum fermentations; utilization of carbon monoxide to inhibit hydrogen production and to enhance butanol yields
    • Kim, B. H., P. Bellows, R. Datta, and J. G. Zeikus. 1984. Control of carbon and electron flow in Clostridium acetobutylicum fermentations; utilization of carbon monoxide to inhibit hydrogen production and to enhance butanol yields. Appl. Environ. Microbiol. 46:764-770.
    • (1984) Appl. Environ. Microbiol. , vol.46 , pp. 764-770
    • Kim, B.H.1    Bellows, P.2    Datta, R.3    Zeikus, J.G.4
  • 26
    • 2142801696 scopus 로고
    • Importance of hydrogen metabolism in regulation of solventogenesis by Clostridium acetobutylicum
    • Kim, B. H., and J. G. Zeikus. 1985. Importance of hydrogen metabolism in regulation of solventogenesis by Clostridium acetobutylicum. Dev Ind. Microbiol 26:549-556.
    • (1985) Dev Ind. Microbiol , vol.26 , pp. 549-556
    • Kim, B.H.1    Zeikus, J.G.2
  • 27
    • 0029077725 scopus 로고
    • Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans
    • Malki, S., I. Saimmaine, G. De Luca, M. Rousset, Z. Dermoun, and J. P. Belaich. 1995. Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans. J. Bacteriol. 177:2628-2636.
    • (1995) J. Bacteriol. , vol.177 , pp. 2628-2636
    • Malki, S.1    Saimmaine, I.2    De Luca, G.3    Rousset, M.4    Dermoun, Z.5    Belaich, J.P.6
  • 28
    • 0021964512 scopus 로고
    • The effect of CO on growth and product formation in batch cultures of Clostridium acetobutylicum
    • Meyer, C. L., J. K. McLaughlin, and E. T. Papoutsakis. 1985. The effect of CO on growth and product formation in batch cultures of Clostridium acetobutylicum. Biotechnol. Lett 7:37-42.
    • (1985) Biotechnol. Lett , vol.7 , pp. 37-42
    • Meyer, C.L.1    McLaughlin, J.K.2    Papoutsakis, E.T.3
  • 29
    • 85047671987 scopus 로고
    • Carbon monoxide gassing leads to alcohol production and butyrate uptake without acetone formation in continuous cultures of Clostridium acetobutylicum
    • Meyer, C. L., J. W. Roos, and E. T. Papoutsakis. 1986. Carbon monoxide gassing leads to alcohol production and butyrate uptake without acetone formation in continuous cultures of Clostridium acetobutylicum. Appl. Microbiol. Biotechnol. 24:159-167.
    • (1986) Appl. Microbiol. Biotechnol. , vol.24 , pp. 159-167
    • Meyer, C.L.1    Roos, J.W.2    Papoutsakis, E.T.3
  • 30
    • 0001700223 scopus 로고
    • Sequence of a 10.5 kbp fragment of Clostridium pasteurianum genomic DNA encompassing the hydrogenase I gene and two spore germination genes
    • Meyer, J. 1995. Sequence of a 10.5 kbp fragment of Clostridium pasteurianum genomic DNA encompassing the hydrogenase I gene and two spore germination genes. Anaerobe 1:169-174.
    • (1995) Anaerobe , vol.1 , pp. 169-174
    • Meyer, J.1
  • 31
    • 0026040877 scopus 로고
    • Primary structure of hydrogenase I from Clostridium pasteurianum
    • Meyer, J., and J. Gagnon. 1991 Primary structure of hydrogenase I from Clostridium pasteurianum. Biochemistry 30:9697-9704
    • (1991) Biochemistry , vol.30 , pp. 9697-9704
    • Meyer, J.1    Gagnon, J.2
  • 32
    • 0027343044 scopus 로고
    • Cloning, structure, and expression of acid and solvent pathway genes of Clostridium acetobutylicum
    • D. R. Woods (ed.), Butterwoth-Heinemann, Stoneham, Mass.
    • Papoutsakis, E. T., and G. N. Bennett. 1993. Cloning, structure, and expression of acid and solvent pathway genes of Clostridium acetobutylicum, p. 157-199. In D. R. Woods (ed.), The clostridia and biotechnology. Butterwoth-Heinemann, Stoneham, Mass.
    • (1993) The Clostridia and Biotechnology , pp. 157-199
    • Papoutsakis, E.T.1    Bennett, G.N.2
  • 33
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W. R., and D. J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85:2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 34
    • 9244250939 scopus 로고
    • Metabolic flexibility of Clostridium acetobutylicum in response to methyl viologen addition
    • Peguin, S., G. Goma, P. Delorme, and P. Soucaille. 1994. Metabolic flexibility of Clostridium acetobutylicum in response to methyl viologen addition. Appl. Microbiol. Biotechnol. 41:450-459.
    • (1994) Appl. Microbiol. Biotechnol. , vol.41 , pp. 450-459
    • Peguin, S.1    Goma, G.2    Delorme, P.3    Soucaille, P.4
  • 35
    • 0028893691 scopus 로고
    • Modulation of carbon and electron flow in Clostridium acetobutylicum by iron limitation and methyl viologen addition
    • Peguin, S., and P. Soucaille. 1995. Modulation of carbon and electron flow in Clostridium acetobutylicum by iron limitation and methyl viologen addition. Appl. Environ. Microbiol. 61:403-405.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 403-405
    • Peguin, S.1    Soucaille, P.2
  • 36
    • 0025813273 scopus 로고
    • Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon
    • Quinn, C. L., B. T. Stephenson, and R. L. Switzer. 1991. Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon J. Biol. Chem. 266:9113-9127.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9113-9127
    • Quinn, C.L.1    Stephenson, B.T.2    Switzer, R.L.3
  • 37
    • 0023260421 scopus 로고
    • Altered electron flow in continuous culture of Clostridium acetobutylicum induced by viologen dyes
    • Rao, G., and R. Mutharasan. 1987. Altered electron flow in continuous culture of Clostridium acetobutylicum induced by viologen dyes. Appl. Environ. Microbiol. 53:1232-1235.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 1232-1235
    • Rao, G.1    Mutharasan, R.2
  • 38
    • 0018588890 scopus 로고
    • Regulatory sequences involved in the promotion and termination of RNA transcription
    • Rosenberg, M., and D. Court. 1979 Regulatory sequences involved in the promotion and termination of RNA transcription. Annu. Rev Genet. 13: 319-353.
    • (1979) Annu. Rev Genet. , vol.13 , pp. 319-353
    • Rosenberg, M.1    Court, D.2
  • 41
    • 0028821460 scopus 로고
    • Characterization and expression of the hydrogenase-encoding gene from Clostridium acetobutylicum P262
    • Santangelo, J. D., P. Dürre, and D. R. Woods. 1995. Characterization and expression of the hydrogenase-encoding gene from Clostridium acetobutylicum P262. Microbiology 141:171-180.
    • (1995) Microbiology , vol.141 , pp. 171-180
    • Santangelo, J.D.1    Dürre, P.2    Woods, D.R.3
  • 42
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E. M. 1975. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98:503-517.
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-517
    • Southern, E.M.1
  • 43
    • 0024655902 scopus 로고
    • Hydγ, a gene from Desulfovibrio vulgaris (Hildenborough) encodes a polypeptide homologous to the periplasmic hydrogenase
    • Stokkermans, J., W. van Dongen, A. Kaan, W. van den Berg, and C. Veeger. 1989. hydγ, a gene from Desulfovibrio vulgaris (Hildenborough) encodes a polypeptide homologous to the periplasmic hydrogenase. FEMS Microbiol Lett 58:217-222
    • (1989) FEMS Microbiol Lett , vol.58 , pp. 217-222
    • Stokkermans, J.1    Van Dongen, W.2    Kaan, A.3    Van Den Berg, W.4    Veeger, C.5
  • 45
    • 0015963265 scopus 로고
    • The reaction of the iron-sulfur protein hydrogenase with carbon monoxide
    • Thauer, R. K., B. Käufer, M. Zähringer, and K. Jungermann. 1974. The reaction of the iron-sulfur protein hydrogenase with carbon monoxide. Eur. J Biochem. 42:447-452.
    • (1974) Eur. J Biochem. , vol.42 , pp. 447-452
    • Thauer, R.K.1    Käufer, B.2    Zähringer, M.3    Jungermann, K.4
  • 46
    • 0028201690 scopus 로고
    • Regulation of carbon and electron flow in Clostridium acetobutylicum grown in chemostat culture at neutral pH on mixtures of glucose and glycerol
    • Vasconcelos, I., L. Girbal, and P. Soucaille. 1994. Regulation of carbon and electron flow in Clostridium acetobutylicum grown in chemostat culture at neutral pH on mixtures of glucose and glycerol. J. Bacteriol. 176:1443-1450.
    • (1994) J. Bacteriol. , vol.176 , pp. 1443-1450
    • Vasconcelos, I.1    Girbal, L.2    Soucaille, P.3
  • 47
    • 0021804386 scopus 로고
    • Nucleotide sequence of the gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough)
    • Voordouw, G., and S. Brenner. 1985. Nucleotide sequence of the gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough). Eur J. Biochem. 148:515-520
    • (1985) Eur J. Biochem. , vol.148 , pp. 515-520
    • Voordouw, G.1    Brenner, S.2
  • 48
    • 0023091332 scopus 로고
    • Purification and characterization of Desulfovibrio vulgaris (Hildenborough) hydrogenase expressed in Escherichia coli
    • Voordouw, G., W. R. Hagen, K. M. Krüse-Wolters, A. van Berkel-Arts, and C. Veeger. 1987. Purification and characterization of Desulfovibrio vulgaris (Hildenborough) hydrogenase expressed in Escherichia coli. Eur J. Biochem. 162:31-36.
    • (1987) Eur J. Biochem. , vol.162 , pp. 31-36
    • Voordouw, G.1    Hagen, W.R.2    Krüse-Wolters, K.M.3    Van Berkel-Arts, A.4    Veeger, C.5
  • 49
    • 0024322748 scopus 로고
    • Organization of the genes encoding [Fe] hydrogenase in Desulfovibrio vulgaris subsp. oxamicus Monticello
    • Voordouw, G., J. D. Strang, and F. R. Wilson. 1989. Organization of the genes encoding [Fe] hydrogenase in Desulfovibrio vulgaris subsp. oxamicus Monticello. J. Bacteriol 171:3881-3889.
    • (1989) J. Bacteriol , vol.171 , pp. 3881-3889
    • Voordouw, G.1    Strang, J.D.2    Wilson, F.R.3
  • 50
    • 0027167618 scopus 로고
    • Microbial hydrogenases: Primary structure, classification, signatures and phylogeny
    • Wu, L.-F., and M. A. Mandrand. 1993. Microbial hydrogenases: primary structure, classification, signatures and phylogeny. FEMS Microbiol. Rev. 104:243-270.
    • (1993) FEMS Microbiol. Rev. , vol.104 , pp. 243-270
    • Wu, L.-F.1    Mandrand, M.A.2
  • 51
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 52
    • 0021880189 scopus 로고
    • Effect of increased hydrogen partial pressure on the acetone butanol fermentation by Clostridium acetobutylicum
    • Yerushalmi, L., B. Volesky, and T. Szczesny. 1985. Effect of increased hydrogen partial pressure on the acetone butanol fermentation by Clostridium acetobutylicum. Appl Microbiol Biotechnol. 22:103-107.
    • (1985) Appl Microbiol Biotechnol. , vol.22 , pp. 103-107
    • Yerushalmi, L.1    Volesky, B.2    Szczesny, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.