메뉴 건너뛰기




Volumn 146, Issue 1, 2000, Pages 97-105

Changes in protein synthesis during the adaptation of Bacillus subtilis to anaerobic growth conditions

Author keywords

Anaerobic growth; Bacillus subtilis; Stress response; Two dimensional gel electrophoresis

Indexed keywords

BACTERIAL PROTEIN; CARBON; DIHYDROLIPOAMIDE DEHYDROGENASE; FLAVOHEMOGLOBIN; FRUCTOSE BISPHOSPHATE ALDOLASE; GLUCOSIDE; GLYCEROL KINASE; HEMOGLOBIN; INOSITOL; LACTATE DEHYDROGENASE; MELIBIOSE; NITRATE; NITRATE REDUCTASE; OXYGEN; PHOSPHATE ACETYLTRANSFERASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 0033972849     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-146-1-97     Document Type: Article
Times cited : (44)

References (33)
  • 2
    • 0000190996 scopus 로고    scopus 로고
    • Fermentation
    • Edited by F. C. Neidhardt and others. Washington, DC: American Society for Microbiology
    • Böck, A. & Sawers, G. (1996). Fermentation. In Escherichia coli and Salmonella, Cellular and Molecular Biology, pp. 262-282. Edited by F. C. Neidhardt and others. Washington, DC: American Society for Microbiology.
    • (1996) Escherichia Coli and Salmonella, Cellular and Molecular Biology , pp. 262-282
    • Böck, A.1    Sawers, G.2
  • 3
    • 0028844507 scopus 로고
    • Anaerobic transcription activation in Bacillus subtilis: Identification of distinct FNR-dependent and independent regulatory mechanisms
    • Cruz-Ramos, H., Boursier, L., Moszer, I., Kunst, F., Danchin, A. & Glaser, P. (1995). Anaerobic transcription activation in Bacillus subtilis: identification of distinct FNR-dependent and independent regulatory mechanisms. EMBO J 14, 5984-5994.
    • (1995) EMBO J , vol.14 , pp. 5984-5994
    • Cruz-Ramos, H.1    Boursier, L.2    Moszer, I.3    Kunst, F.4    Danchin, A.5    Glaser, P.6
  • 4
    • 0032450017 scopus 로고    scopus 로고
    • Co-regulation of lipoamide dehydrogenase and 2-oxoglutarate dehydrogenase synthesis in Escherichia coli: Characterisation of an ArcA binding site in the lpd promoter
    • Cunningham, L., Georgellis, D., Green, J. & Guest, J. R. (1998). Co-regulation of lipoamide dehydrogenase and 2-oxoglutarate dehydrogenase synthesis in Escherichia coli: characterisation of an ArcA binding site in the lpd promoter. FEMS Microbiol Lett 169, 403-408.
    • (1998) FEMS Microbiol Lett , vol.169 , pp. 403-408
    • Cunningham, L.1    Georgellis, D.2    Green, J.3    Guest, J.R.4
  • 5
    • 0014197885 scopus 로고
    • Purification and properties of glycerol kinase from Escherichia coli
    • Hayashi, S.-L. & Lin, E. C. C. (1967). Purification and properties of glycerol kinase from Escherichia coli. J Biol Chem 242, 1030-1035.
    • (1967) J Biol Chem , vol.242 , pp. 1030-1035
    • Hayashi, S.-L.1    Lin, E.C.C.2
  • 6
    • 0029153686 scopus 로고
    • The anaerobic life of Bacillus subtilis. Cloning and characterization, of the genes encoding the respiratory nitrate reductase system
    • Hoffmann, T., Troup, B., Szabo, A., Hungerer, C. & Jahn, D. (1995). The anaerobic life of Bacillus subtilis. Cloning and characterization, of the genes encoding the respiratory nitrate reductase system. FEMS Microbiol Lett 131, 219-225.
    • (1995) FEMS Microbiol Lett , vol.131 , pp. 219-225
    • Hoffmann, T.1    Troup, B.2    Szabo, A.3    Hungerer, C.4    Jahn, D.5
  • 7
    • 0031963258 scopus 로고    scopus 로고
    • Ammonification in Bacillus subtilis utilizing dissimilatory nitrite reductase is dependent on resDE
    • Hoffmann, T., Frankenberg, N., Marino, M. & Jahn, D. (1998). Ammonification in Bacillus subtilis utilizing dissimilatory nitrite reductase is dependent on resDE. J Bacteriol 180, 186-189.
    • (1998) J Bacteriol , vol.180 , pp. 186-189
    • Hoffmann, T.1    Frankenberg, N.2    Marino, M.3    Jahn, D.4
  • 8
    • 0024584265 scopus 로고
    • Cloning of the glycerol kinase gene of Bacillus subtilis
    • Holmberg, C. & Rutberg, B. (1989). Cloning of the glycerol kinase gene of Bacillus subtilis. FEMS Microbiol Lett 58, 151-155.
    • (1989) FEMS Microbiol Lett , vol.58 , pp. 151-155
    • Holmberg, C.1    Rutberg, B.2
  • 9
    • 0025647659 scopus 로고
    • Glycerol catabolism in Bacillus subtilis: Nucleotide sequence of the genes encoding glycerol kinase (glpK) and glycerol-3-phosphate dehydrogenase (glpD)
    • Holmberg, C., Beijer, L., Ruthberg, B. & Ruthberg, L. (1990). Glycerol catabolism in Bacillus subtilis: nucleotide sequence of the genes encoding glycerol kinase (glpK) and glycerol-3-phosphate dehydrogenase (glpD). J Gen Microbiol 136, 2367-2375.
    • (1990) J Gen Microbiol , vol.136 , pp. 2367-2375
    • Holmberg, C.1    Beijer, L.2    Ruthberg, B.3    Ruthberg, L.4
  • 10
    • 0028907495 scopus 로고
    • Catabolite repression in Bacillus subtilis: A global regulatory mechanism for the Gram-positive bacteria?
    • Hueck, C. J. & Hillen, W. (1995). Catabolite repression in Bacillus subtilis: a global regulatory mechanism for the Gram-positive bacteria? Mol Microbiol 15, 395-401.
    • (1995) Mol Microbiol , vol.15 , pp. 395-401
    • Hueck, C.J.1    Hillen, W.2
  • 11
    • 0032483005 scopus 로고    scopus 로고
    • NADP, corepressor for the Bacillus catabolite control protein CcpA
    • Kim, J. H., Voskuil, M. I. & Chambliss, G. H. (1998). NADP, corepressor for the Bacillus catabolite control protein CcpA. Proc Natl Acad Sci USA 95, 9590-9595.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9590-9595
    • Kim, J.H.1    Voskuil, M.I.2    Chambliss, G.H.3
  • 12
    • 0029916568 scopus 로고    scopus 로고
    • Transcriptional analysis of bglPH expression in Bacillus subtilis: Evidence for two distinct pathways mediating carbon catabolite repression
    • Krüger, S., Gert, S. & Hecker, M. (1996). Transcriptional analysis of bglPH expression in Bacillus subtilis: evidence for two distinct pathways mediating carbon catabolite repression. J Bacteriol 178, 2637-2644.
    • (1996) J Bacteriol , vol.178 , pp. 2637-2644
    • Krüger, S.1    Gert, S.2    Hecker, M.3
  • 13
    • 0029967350 scopus 로고    scopus 로고
    • Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis
    • LaCelle, M., Kumano, M., Kurita, K., Yamane, K., Zuber, P. & Nakano, M. M. (1996). Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis. J Bacteriol 178, 3803-3808.
    • (1996) J Bacteriol , vol.178 , pp. 3803-3808
    • Lacelle, M.1    Kumano, M.2    Kurita, K.3    Yamane, K.4    Zuber, P.5    Nakano, M.M.6
  • 14
    • 0023650644 scopus 로고
    • Nucleotide sequence of the melA gene, coding for alpha-galactosidase in Escherichia coli K-12
    • Liljeström, P. L. & Liljeström, P. (1987). Nucleotide sequence of the melA gene, coding for alpha-galactosidase in Escherichia coli K-12. Nucleic Acids Res 15, 2213-2220.
    • (1987) Nucleic Acids Res , vol.15 , pp. 2213-2220
    • Liljeström, P.L.1    Liljeström, P.2
  • 15
    • 0028859554 scopus 로고
    • Two different mechanisms mediate catabolite repression on the Bacillus subtilis levanase operon
    • Martin-Verstraete, I., Stülke, J., Klier, A. & Rapoport, G. (1995). Two different mechanisms mediate catabolite repression on the Bacillus subtilis levanase operon. J Bacteriol 177, 6919-6927.
    • (1995) J Bacteriol , vol.177 , pp. 6919-6927
    • Martin-Verstraete, I.1    Stülke, J.2    Klier, A.3    Rapoport, G.4
  • 16
    • 0030997843 scopus 로고    scopus 로고
    • FNR-dependent repression of ndh gene expression requires two upstream FNR-binding sites
    • Meng, W., Green, J. & Guest, J. R. (1997). FNR-dependent repression of ndh gene expression requires two upstream FNR-binding sites. Microbiology 143, 1521-1532.
    • (1997) Microbiology , vol.143 , pp. 1521-1532
    • Meng, W.1    Green, J.2    Guest, J.R.3
  • 17
    • 0030955228 scopus 로고    scopus 로고
    • Testosterone regulated expression of enzymes involved in steroid and aromatic hydrocarbon catabolism in Comamonas testosteroni
    • Moebius, E., Jahn, M., Schmid, R., Jahn, D. & Maser, E. (1997). Testosterone regulated expression of enzymes involved in steroid and aromatic hydrocarbon catabolism in Comamonas testosteroni. J Bacteriol 179, 5951-5955.
    • (1997) J Bacteriol , vol.179 , pp. 5951-5955
    • Moebius, E.1    Jahn, M.2    Schmid, R.3    Jahn, D.4    Maser, E.5
  • 18
    • 0028935455 scopus 로고
    • Subtilist: A relational database for the Bacillus subtilis genome
    • Moszer, I., Glaser, P. & Danchin, A. (1995). SubtiList: a relational database for the Bacillus subtilis genome. Microbiology 141, 261-268.
    • (1995) Microbiology , vol.141 , pp. 261-268
    • Moszer, I.1    Glaser, P.2    Danchin, A.3
  • 19
    • 0031727390 scopus 로고    scopus 로고
    • Anaerobic growth of a "strict aerobe" (Bacillus subtilis)
    • Nakano, M. M. & Zuber, P. (1998). Anaerobic growth of a "strict aerobe" (Bacillus subtilis). Annu Rev Microbiol 52, 165-190.
    • (1998) Annu Rev Microbiol , vol.52 , pp. 165-190
    • Nakano, M.M.1    Zuber, P.2
  • 20
    • 0029889199 scopus 로고    scopus 로고
    • Two-component regulatory proteins ResD-ResF. Are required for transcriptional activation of fur upon oxygen limitation in Bacillus subtilis
    • Nakano, M. M., Zuber, P., Glaser, P., Danchin, A. & Hulett, M. (1996). Two-component regulatory proteins ResD-ResF. are required for transcriptional activation of fur upon oxygen limitation in Bacillus subtilis. J Bacteriol 178, 3796-3802.
    • (1996) J Bacteriol , vol.178 , pp. 3796-3802
    • Nakano, M.M.1    Zuber, P.2    Glaser, P.3    Danchin, A.4    Hulett, M.5
  • 21
    • 0030700663 scopus 로고    scopus 로고
    • Characterization of anaerobic fermentative growth in Bacillus subtilis: Identification of fermentation end products and genes required for the growth
    • Nakano, M. M., Dailly, Y. P., Zuber, P. & Clark, D. P. (1997). Characterization of anaerobic fermentative growth in Bacillus subtilis: identification of fermentation end products and genes required for the growth. J Bacteriol 179, 6749-6755.
    • (1997) J Bacteriol , vol.179 , pp. 6749-6755
    • Nakano, M.M.1    Dailly, Y.P.2    Zuber, P.3    Clark, D.P.4
  • 22
    • 0031691173 scopus 로고    scopus 로고
    • Nitrogen and oxygen regulation of Bacillus subtilis nasDEF encoding NADH-dependent nitrite reductase by TnrA and ResDE
    • Nakano, M. M., Hoffmann, T., Zhu, Y. & Jahn, D. (1998). Nitrogen and oxygen regulation of Bacillus subtilis nasDEF encoding NADH-dependent nitrite reductase by TnrA and ResDE. J Bacteriol 180, 5344-5350.
    • (1998) J Bacteriol , vol.180 , pp. 5344-5350
    • Nakano, M.M.1    Hoffmann, T.2    Zhu, Y.3    Jahn, D.4
  • 23
    • 0019859835 scopus 로고
    • Role of inducer exclusion in preferential utilization of glucose over melibiose in diauxic growth of Escherichia coli
    • Okada, T., Ueyama, K., Niiya, S., Kanazawa, H., Futai, M. & Tsuchiya, T. (1981). Role of inducer exclusion in preferential utilization of glucose over melibiose in diauxic growth of Escherichia coli. J Bacteriol 146, 1030-1037.
    • (1981) J Bacteriol , vol.146 , pp. 1030-1037
    • Okada, T.1    Ueyama, K.2    Niiya, S.3    Kanazawa, H.4    Futai, M.5    Tsuchiya, T.6
  • 24
    • 0028177225 scopus 로고
    • The pdhR-aceEF-lpd operon of Escherichia coli expresses the pyruvate dehydrogenase complex
    • Quail, M. A., Haydon, D. J. & Guest, J. R. (1994). The pdhR-aceEF-lpd operon of Escherichia coli expresses the pyruvate dehydrogenase complex. Mol Microbiol 12, 95-104.
    • (1994) Mol Microbiol , vol.12 , pp. 95-104
    • Quail, M.A.1    Haydon, D.J.2    Guest, J.R.3
  • 25
    • 0028022830 scopus 로고
    • Gene structure and amino acid sequences of alcohol dehydrogenases of Bacillus stearothermophilus
    • Robinson, G. A., Bailey, C. J. & Dowds, B. C. A. (1994). Gene structure and amino acid sequences of alcohol dehydrogenases of Bacillus stearothermophilus. Biochim Biophys Acta 1218, 432-434.
    • (1994) Biochim Biophys Acta , vol.1218 , pp. 432-434
    • Robinson, G.A.1    Bailey, C.J.2    Dowds, B.C.A.3
  • 26
    • 0031708867 scopus 로고    scopus 로고
    • Changes in protein expression as a consequence of heme depletion in Escherichia coli
    • Rompf, A., Schmid, R. & Jahn, D. (1998). Changes in protein expression as a consequence of heme depletion in Escherichia coli. Curr Microbiol 37, 226-230.
    • (1998) Curr Microbiol , vol.37 , pp. 226-230
    • Rompf, A.1    Schmid, R.2    Jahn, D.3
  • 27
    • 0026409298 scopus 로고
    • Blue native gel electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger, H. & von Jagow, G. (1991). Blue native gel electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Riochem 199, 223-231.
    • (1991) Anal Riochem , vol.199 , pp. 223-231
    • Schägger, H.1    Von Jagow, G.2
  • 28
    • 0030985597 scopus 로고    scopus 로고
    • Identification of vegetative proteins for a two-dimensional protein index of Bacillus subtilis
    • Schmid, R., Bernhardt, J., Antelmann, H., Völker, A., Mach, H., Völker, U. & Hecker, M. (1997). Identification of vegetative proteins for a two-dimensional protein index of Bacillus subtilis. Microbiology 143, 991-998.
    • (1997) Microbiology , vol.143 , pp. 991-998
    • Schmid, R.1    Bernhardt, J.2    Antelmann, H.3    Völker, A.4    Mach, H.5    Völker, U.6    Hecker, M.7
  • 29
    • 0014429554 scopus 로고
    • Chemical characterisation of D-lactate dehydrogenase from Escherichia coli B
    • Tarmy, E. M. & Kaplan, N. O. (1968). Chemical characterisation of D-lactate dehydrogenase from Escherichia coli B. J Biol Chem 243, 2579-2586.
    • (1968) J Biol Chem , vol.243 , pp. 2579-2586
    • Tarmy, E.M.1    Kaplan, N.O.2
  • 30
    • 0032538629 scopus 로고    scopus 로고
    • The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-α-glucosidase
    • Thompson, J., Pikis, A., Ruvinov, S. B., Henrissant, B., Yamamoto, H. & Sekuchi, J. (1998). The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-α-glucosidase. J Biol Chem 273, 27347-27356.
    • (1998) J Biol Chem , vol.273 , pp. 27347-27356
    • Thompson, J.1    Pikis, A.2    Ruvinov, S.B.3    Henrissant, B.4    Yamamoto, H.5    Sekuchi, J.6
  • 31
    • 0020345765 scopus 로고
    • Fructose-1,6-bisphosphate aldolase from Bacillus subtilis
    • Ujita, S. & Kimura, K. (1982). Fructose-1,6-bisphosphate aldolase from Bacillus subtilis. Methods Enzymol 90, 235-241.
    • (1982) Methods Enzymol , vol.90 , pp. 235-241
    • Ujita, S.1    Kimura, K.2
  • 33
    • 0030877591 scopus 로고    scopus 로고
    • Organization and transcription of the myo-inositol operon, iol, of Bacillus subtilis
    • Yoshida, K.-I., Aoyama, D., Ishio, I., Shibayama, T. & Fujita, Y. (1997). Organization and transcription of the myo-inositol operon, iol, of Bacillus subtilis. J Bacteriol 179, 4591-4598.
    • (1997) J Bacteriol , vol.179 , pp. 4591-4598
    • Yoshida, K.-I.1    Aoyama, D.2    Ishio, I.3    Shibayama, T.4    Fujita, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.