메뉴 건너뛰기




Volumn 1, Issue 1, 1999, Pages 141-148

The catabolite control protein CcpA controls ammonium assimilation in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARBON; CATABOLITE CONTROL PROTEIN, BACTERIA; DNA BINDING PROTEIN; GLUCOSE; GLUTAMATE SYNTHASE; GLUTAMATE SYNTHASE A; QUATERNARY AMMONIUM DERIVATIVE; REPRESSOR PROTEIN;

EID: 0033170575     PISSN: 14641801     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (74)

References (45)
  • 1
    • 0024730354 scopus 로고
    • Positive regulation of glutamate biosynthesis in Bacillus subtilis
    • Bohannon, D.E., and Sonenshein, A.L. 1989. Positive regulation of glutamate biosynthesis in Bacillus subtilis. J. Bacteriol. 171: 4718-4727.
    • (1989) J. Bacteriol. , vol.171 , pp. 4718-4727
    • Bohannon, D.E.1    Sonenshein, A.L.2
  • 2
    • 0021972573 scopus 로고
    • Regulation of Bacillus subtilis glutamate synthase genes by the nitrogen source
    • Bohannon, D.E., Rosenkrantz, M.S., and Sonenshein, A.L. 1985. Regulation of Bacillus subtilis glutamate synthase genes by the nitrogen source. J. Bacteriol. 163: 957-964.
    • (1985) J. Bacteriol. , vol.163 , pp. 957-964
    • Bohannon, D.E.1    Rosenkrantz, M.S.2    Sonenshein, A.L.3
  • 3
    • 0028364161 scopus 로고
    • Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis
    • Deutscher J., Reizer, J., Fischer, C., Galinier, A., Saier Jr., M.H., and Steinmetz, M. 1994. Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis. J. Bacteriol. 176: 3336-3344.
    • (1994) J. Bacteriol. , vol.176 , pp. 3336-3344
    • Deutscher, J.1    Reizer, J.2    Fischer, C.3    Galinier, A.4    Saier, J.5    Steinmetz, M.6
  • 4
    • 0028917215 scopus 로고
    • Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria
    • Deutscher, J., Küster, E., Bergstedt, U., Charrier, V., and Hillen, W. 1995. Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria. Mol. Microbiol. 15: 1049-1053.
    • (1995) Mol. Microbiol. , vol.15 , pp. 1049-1053
    • Deutscher, J.1    Küster, E.2    Bergstedt, U.3    Charrier, V.4    Hillen, W.5
  • 6
    • 0029745668 scopus 로고    scopus 로고
    • Catabolite repression mediated by the catabolite control protein CcpA in staphylococcus xylosus
    • Egeter, O., and Brückner, R. 1996. Catabolite repression mediated by the catabolite control protein CcpA in Staphylococcus xylosus. Mol. Microbiol. 21: 739-749.
    • (1996) Mol. Microbiol. , vol.21 , pp. 739-749
    • Egeter, O.1    Brückner, R.2
  • 7
    • 0026014681 scopus 로고
    • Control of carbon and nitrogen metabolism in Bacillus subtilis
    • Fisher, S.H., and Sonenshein, A.L. 1991. Control of carbon and nitrogen metabolism in Bacillus subtilis. Annu. Rev. Microbiol. 45: 107-135.
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 107-135
    • Fisher, S.H.1    Sonenshein, A.L.2
  • 8
    • 0028293669 scopus 로고
    • Modulation of bacillus subtilis catabolite repression by transition state regulatory protein AbrB
    • Fisher, S.H., Strauch, M.A., Atkinson, M.R., and Wray Jr., L.V. 1994. Modulation of Bacillus subtilis catabolite repression by transition state regulatory protein AbrB. J. Bacteriol. 176: 1903-1912.
    • (1994) J. Bacteriol. , vol.176 , pp. 1903-1912
    • Fisher, S.H.1    Strauch, M.A.2    Atkinson, M.R.3    Wray, J.4
  • 9
    • 0028827880 scopus 로고
    • Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr
    • Fujita, Y., Miwa, Y., Galinier, A., and Deutscher, J. 1995. Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr. Mol. Microbiol. 17: 953-960.
    • (1995) Mol. Microbiol. , vol.17 , pp. 953-960
    • Fujita, Y.1    Miwa, Y.2    Galinier, A.3    Deutscher, J.4
  • 12
    • 0024444204 scopus 로고
    • Phospho-enolpyruvate:Sugar phosphotransferase system of Bacillus subtilis: Nucleotide sequence of ptsX, ptsH and the 5′-end of ptsl and evidence for a pfsH/operon
    • Gonzy-Tréboul, G., Zagorec, M., Rain-Guion, M.C., and Steinmetz, M. 1989. Phospho-enolpyruvate:sugar phosphotransferase system of Bacillus subtilis: nucleotide sequence of ptsX, ptsH and the 5′-end of ptsl and evidence for a pfsH/operon. Mol. Microbiol. 3: 103-112.
    • (1989) Mol. Microbiol. , vol.3 , pp. 103-112
    • Gonzy-Tréboul, G.1    Zagorec, M.2    Rain-Guion, M.C.3    Steinmetz, M.4
  • 13
    • 0031557402 scopus 로고    scopus 로고
    • Cooperative and non-cooperative DNA binding modes of catabolite control protein CcpA from Bacillus megaterium result from sensing two different signals
    • Gösseringer, R., Küster, E., Galinier, A., Deutscher, J., and Hillen, W. 1997. Cooperative and non-cooperative DNA binding modes of catabolite control protein CcpA from Bacillus megaterium result from sensing two different signals. J. Mol. Biol. 266: 665-676.
    • (1997) J. Mol. Biol. , vol.266 , pp. 665-676
    • Gösseringer, R.1    Küster, E.2    Galinier, A.3    Deutscher, J.4    Hillen, W.5
  • 14
    • 0027377245 scopus 로고
    • Regulation of the Bacillus subtilis acetate kinase gene by CcpA
    • Grundy, F.J., Waters, D.A., Allen, S.H., and Henkin, T.M. 1993. Regulation of the Bacillus subtilis acetate kinase gene by CcpA. J. Bacteriol. 175: 7348-7355.
    • (1993) J. Bacteriol. , vol.175 , pp. 7348-7355
    • Grundy, F.J.1    Waters, D.A.2    Allen, S.H.3    Henkin, T.M.4
  • 15
    • 0030057004 scopus 로고    scopus 로고
    • The role of the CcpA transcriptional regulator in carbon metabolism in Bacillus subtilis
    • Henkin, T.M. 1996. The role of the CcpA transcriptional regulator in carbon metabolism in Bacillus subtilis. FEMS Microbiol. L. 135: 9-15.
    • (1996) FEMS Microbiol. L. , vol.135 , pp. 9-15
    • Henkin, T.M.1
  • 16
    • 0026033650 scopus 로고
    • Catabolite repression of α-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacl and GalR repressors
    • Henkin, T.M., Grundy, F.J., Nicholson, W.L., and Chambliss, G.H. 1991. Catabolite repression of α-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli Lacl and GalR repressors. Mol. Microbiol. 5: 575-584.
    • (1991) Mol. Microbiol. , vol.5 , pp. 575-584
    • Henkin, T.M.1    Grundy, F.J.2    Nicholson, W.L.3    Chambliss, G.H.4
  • 17
    • 0028907495 scopus 로고
    • Catabolite repression in Bacillus subtilis: A global regulatory mechanism for the Gram-positive bacteria?
    • Hueck, C.J., and 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
  • 18
    • 0029113013 scopus 로고
    • Cloning, expression and functional analyses of the catabolite control protein CcpA from Bacillus megaterium
    • Hueck, C.J., Kraus, A., Schmiedel, D., and Hillen, W. 1995. Cloning, expression and functional analyses of the catabolite control protein CcpA from Bacillus megaterium. Mol. Microbiol. 16: 855-864.
    • (1995) Mol. Microbiol. , vol.16 , pp. 855-864
    • Hueck, C.J.1    Kraus, A.2    Schmiedel, D.3    Hillen, W.4
  • 19
    • 0030725260 scopus 로고    scopus 로고
    • Binding of the catabolite repressor protein CcpA to its DNA target is regulated by phosphorylation of its corepressor HPr
    • Jones, B.E., Dossonnet, V., Küster, E., Hillen, W., Deutscher, J., and Klevit, R.E. 1997. Binding of the catabolite repressor protein CcpA to its DNA target is regulated by phosphorylation of its corepressor HPr. J. Biol. Chem. 272: 26530-26535.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26530-26535
    • Jones, B.E.1    Dossonnet, V.2    Küster, E.3    Hillen, W.4    Deutscher, J.5    Klevit, R.E.6
  • 20
    • 0032483005 scopus 로고    scopus 로고
    • NADP, corepressor for the Bacillus subtilis catabolite control protein CcpA
    • Kim, J.H., Voskuil, M.I., and Chambliss, G.H. 1998. NADP, corepressor for the Bacillus subtilis 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
  • 21
    • 0027365675 scopus 로고
    • Catabolite repression of ß-glucanase synthesis in Bacillus subtilis
    • Krüger, S., Stülke, J., and Hecker, M. 1993. Catabolite repression of ß-glucanase synthesis in Bacillus subtilis. J. Gen. Microbiol. 139: 2047-2054.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2047-2054
    • Krüger, S.1    Stülke, J.2    Hecker, M.3
  • 22
    • 0029916568 scopus 로고    scopus 로고
    • Transcriptional analysis of bglPH expression in Bacillus subtilis: Evidence for two distinct pathways mediating carbon catabolite repression
    • Krüger, S., Gertz, S., and 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    Gertz, S.2    Hecker, M.3
  • 23
    • 0029006115 scopus 로고
    • Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis
    • Kunst, F., and Rapoport G. 1995. Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis. J. Bacteriol. 177: 2403-2407.
    • (1995) J. Bacteriol. , vol.177 , pp. 2403-2407
    • Kunst, F.1    Rapoport, G.2
  • 24
    • 0028330705 scopus 로고
    • Regulation of xylanolytic enzymes in Bacillus subtilis
    • Lindner, C., Stülke, J., and Hecker, M. 1994. Regulation of xylanolytic enzymes in Bacillus subtilis. Microbiol. 140: 753-757.
    • (1994) Microbiol. , vol.140 , pp. 753-757
    • Lindner, C.1    Stülke, J.2    Hecker, M.3
  • 26
    • 0025142206 scopus 로고
    • Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating the expression of the operon
    • Martin-Verstraete, I., Débarbouillé, M., Klier, A., and Rapoport, G. 1990. Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating the expression of the operon. J. Mol. Biol. 214: 657-671.
    • (1990) J. Mol. Biol. , vol.214 , pp. 657-671
    • Martin-Verstraete, I.1    Débarbouillé, M.2    Klier, A.3    Rapoport, G.4
  • 27
    • 0026721820 scopus 로고
    • Mutagenesis of the Bacillus subtilis "-12, -24" promoter of the levanase operon and evidence for the existence of an upstream activating sequence
    • Martin-Verstraete, I., Débarbouillé, M., Klier, A., and Rapoport, G. 1992. Mutagenesis of the Bacillus subtilis "-12, -24" promoter of the levanase operon and evidence for the existence of an upstream activating sequence. J. Mol. Biol. 226: 85-99.
    • (1992) J. Mol. Biol. , vol.226 , pp. 85-99
    • Martin-Verstraete, I.1    Débarbouillé, M.2    Klier, A.3    Rapoport, G.4
  • 28
    • 0028859554 scopus 로고
    • Two different mechanisms mediate catabolite repression of the Bacillus subtilis levanase operon
    • Martin-Verstraete, I., Stülke, J., Klier, A., and Rapoport, G. 1995. Two different mechanisms mediate catabolite repression of 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
  • 29
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Miller, J. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.1
  • 30
    • 0028099341 scopus 로고
    • Possible function and some properties of the CcpA protein of Bacillus subtilis
    • Miwa, Y., Saikawa, M., and Fujita, Y. 1994. Possible function and some properties of the CcpA protein of Bacillus subtilis. Microbiol. 140: 2567-2575.
    • (1994) Microbiol. , vol.140 , pp. 2567-2575
    • Miwa, Y.1    Saikawa, M.2    Fujita, Y.3
  • 31
    • 0030899835 scopus 로고    scopus 로고
    • Catabolite repression of the Bacillus subtilis gnt operon exerted by two catabolite-responsive elements
    • Miwa, Y., Nagura, K., Eguchi, S., Fukuda, H., Deutscher, J., and Fujita, Y. 1997. Catabolite repression of the Bacillus subtilis gnt operon exerted by two catabolite-responsive elements. Mol. Microbiol. 23: 1203-1213.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1203-1213
    • Miwa, Y.1    Nagura, K.2    Eguchi, S.3    Fukuda, H.4    Deutscher, J.5    Fujita, Y.6
  • 32
    • 0030660143 scopus 로고    scopus 로고
    • Catabolite repression in lactobacillus casei ATCC 393 is mediated by CcpA
    • Monedero, V., Gosalbes, M.J., and Perez-Martinez, G. 1997. Catabolite repression in Lactobacillus casei ATCC 393 is mediated by CcpA. J. Bacteriol. 179: 6657-6664.
    • (1997) J. Bacteriol. , vol.179 , pp. 6657-6664
    • Monedero, V.1    Gosalbes, M.J.2    Perez-Martinez, G.3
  • 33
    • 0030700663 scopus 로고    scopus 로고
    • Characterization of anaerobic fermentative growth of Bacillus subtilis: Identification of fermentation end products and genes required for growth
    • Nakano, M.N., Dailly, Y.P., Zuber, P., and Clark, D.P. 1997. Characterization of anaerobic fermentative growth of Bacillus subtilis: identification of fermentation end products and genes required for growth. J. Bacteriol. 179: 6749-6755.
    • (1997) J. Bacteriol. , vol.179 , pp. 6749-6755
    • Nakano, M.N.1    Dailly, Y.P.2    Zuber, P.3    Clark, D.P.4
  • 34
    • 0021768691 scopus 로고
    • Catabolite repression of inositol dehydrogenase and gluconate kinase syntheses in Bacillus subtilis
    • Nihashi, J.I., and Fujita, Y. 1984. Catabolite repression of inositol dehydrogenase and gluconate kinase syntheses in Bacillus subtilis. Biochim. Biophys. Acta. 798: 88-95.
    • (1984) Biochim. Biophys. Acta. , vol.798 , pp. 88-95
    • Nihashi, J.I.1    Fujita, Y.2
  • 38
    • 0018973548 scopus 로고
    • Genetics and physiology of the rel system of Bacillus subtilis
    • Smith, I., Paress, P., Cabane, K., and Dubnau, E. 1980. Genetics and physiology of the rel system of Bacillus subtilis. Mol. Gen. Genet. 178: 271-279.
    • (1980) Mol. Gen. Genet. , vol.178 , pp. 271-279
    • Smith, I.1    Paress, P.2    Cabane, K.3    Dubnau, E.4
  • 39
    • 0028809520 scopus 로고
    • AbrB modulates expression and catabolite repression of a Bacillus subtilis ribose transport operon
    • Strauch, M.A. 1995. AbrB modulates expression and catabolite repression of a Bacillus subtilis ribose transport operon. J. Bacteriol. 177: 6727-6731.
    • (1995) J. Bacteriol. , vol.177 , pp. 6727-6731
    • Strauch, M.A.1
  • 40
    • 0027524789 scopus 로고
    • Temporal activation of ß-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool
    • Stülke, J., Hanschke, R., and Hecker, M. 1993. Temporal activation of ß-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool. J. Gen. Microbiol. 139: 2041-2045.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2041-2045
    • Stülke, J.1    Hanschke, R.2    Hecker, M.3
  • 41
    • 0030742667 scopus 로고    scopus 로고
    • Induction of the bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GIcT
    • Stülke, J., Martin-Verstraete, I., Zagorec, M., Rose, M., Klier, A., and Rapoport, G. 1997. Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GIcT. Mol. Microbiol. 25: 65-78.
    • (1997) Mol. Microbiol. , vol.25 , pp. 65-78
    • Stülke, J.1    Martin-Verstraete, I.2    Zagorec, M.3    Rose, M.4    Klier, A.5    Rapoport, G.6
  • 42
    • 0031808469 scopus 로고    scopus 로고
    • PRD -a protein domain involved in PTS-dependent induction and catabolite repression of catabolic operons in bacteria
    • Stülke, J., Arnaud, M., Rapoport, G., and Martin-Verstraete, I. 1998. PRD -a protein domain involved in PTS-dependent induction and catabolite repression of catabolic operons in bacteria. Mol. Microbiol. 28: 865-874.
    • (1998) Mol. Microbiol. , vol.28 , pp. 865-874
    • Stülke, J.1    Arnaud, M.2    Rapoport, G.3    Martin-Verstraete, I.4
  • 43
    • 0029015369 scopus 로고
    • Characterization of the proton/glutamate symport protein of Bacillus subtilis and its functional expression in Escherichia coli
    • Tolner, B., Ubbink-Kok, T., Poolman, B., and Konings, W.N. 1995. Characterization of the proton/glutamate symport protein of Bacillus subtilis and its functional expression in Escherichia coli. J. Bacteriol. 177:2863-2869.
    • (1995) J. Bacteriol. , vol.177 , pp. 2863-2869
    • Tolner, B.1    Ubbink-Kok, T.2    Poolman, B.3    Konings, W.N.4
  • 44
    • 0028205413 scopus 로고
    • Catabolite repression of the Bacillus subtilis hut operon requires a cis-acting site located downstream of the transcription initiation site
    • Wray, L.W., Jr., Pettengill, F.K., and Fisher, S.H. 1994. Catabolite repression of the Bacillus subtilis hut operon requires a cis-acting site located downstream of the transcription initiation site. J. Bacteriol. 176: 1894-1902.
    • (1994) J. Bacteriol. , vol.176 , pp. 1894-1902
    • Wray L.W., Jr.1    Pettengill, F.K.2    Fisher, S.H.3
  • 45
    • 0017034780 scopus 로고
    • Genetic mapping of the alsA, alsR, thyA, kauA, and citD markers in Bacillus subtilis
    • Schlesinger, D. (ed.). Washington, D.C.: American Society for Microbiology
    • Zahler, S.A., Benjamin, L.G., Glatz, B.S., Winter, P.F., and Goldstein, B.J. 1976. Genetic mapping of the alsA, alsR, thyA, kauA, and citD markers in Bacillus subtilis. In Microbiology-1976: Schlesinger, D. (ed.). Washington, D.C.: American Society for Microbiology, pp. 35-43.
    • (1976) Microbiology-1976 , pp. 35-43
    • Zahler, S.A.1    Benjamin, L.G.2    Glatz, B.S.3    Winter, P.F.4    Goldstein, B.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.