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Volumn 181, Issue 16, 1999, Pages 4995-5003

Regulation of the lic operon of Bacillus subtilis and characterization of potential phosphorylation sites of the LicR regulator protein by site- directed mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSIDE; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE; REGULATOR PROTEIN;

EID: 0344564161     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.16.4995-5003.1999     Document Type: Article
Times cited : (54)

References (48)
  • 1
    • 0026772662 scopus 로고
    • Regulation of the sacPA operon of Bacillus subtilis: Identification of phosphotransferase system components involved in SacT activity
    • Arnaud, M., P. Vary, M. Zagorec, A. Klier, M. Débarbouillé, P. Postma, and G. Rapoport. 1992. Regulation of the sacPA operon of Bacillus subtilis: identification of phosphotransferase system components involved in SacT activity. J. Bacteriol. 174:3161-3170.
    • (1992) J. Bacteriol. , vol.174 , pp. 3161-3170
    • Arnaud, M.1    Vary, P.2    Zagorec, M.3    Klier, A.4    Débarbouillé, M.5    Postma, P.6    Rapoport, G.7
  • 2
    • 0031711025 scopus 로고    scopus 로고
    • Regulation of the Bacillus subtilis GlcT antiterminator protein by components of the phosphotransferase system
    • Bachem, S., and J. Stülke. 1998. Regulation of the Bacillus subtilis GlcT antiterminator protein by components of the phosphotransferase system. J. Bacteriol. 180:5319-5326.
    • (1998) J. Bacteriol. , vol.180 , pp. 5319-5326
    • Bachem, S.1    Stülke, J.2
  • 3
    • 0030971645 scopus 로고    scopus 로고
    • Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residue
    • Charrier, V., E. Buckley, D. Parsonage, A. Galinier, E. Darbon, M. Jaquinod, E. Forest, J. Deutscher, and A. Claiborne. 1997. Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residue. J. Biol. Chem. 272:14166-14174.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14166-14174
    • Charrier, V.1    Buckley, E.2    Parsonage, D.3    Galinier, A.4    Darbon, E.5    Jaquinod, M.6    Forest, E.7    Deutscher, J.8    Claiborne, A.9
  • 4
    • 0025128602 scopus 로고
    • Induction of levansucrase in Bacillus subtilis: An antitermination mechanism negatively controlled by the phosphotransferase system
    • Crutz, A. M., M. Steinmetz, S. Aymerich, R. Richter, and D. Le Coq. 1990. Induction of levansucrase in Bacillus subtilis: an antitermination mechanism negatively controlled by the phosphotransferase system. J. Bacteriol. 172: 1043-1050.
    • (1990) J. Bacteriol. , vol.172 , pp. 1043-1050
    • Crutz, A.M.1    Steinmetz, M.2    Aymerich, S.3    Richter, R.4    Le Coq, D.5
  • 5
    • 0025301224 scopus 로고
    • The sacT gene regulating the sacPA operon in Bacillus subtilis shares strong homology with transcriptional antiterminators
    • Débarbouillé, M., M. Arnaud, A. Fouet, A. Klier, and G. Rapoport. 1990. The sacT gene regulating the sacPA operon in Bacillus subtilis shares strong homology with transcriptional antiterminators. J. Bacteriol. 172:3966-3973.
    • (1990) J. Bacteriol. , vol.172 , pp. 3966-3973
    • Débarbouillé, M.1    Arnaud, M.2    Fouet, A.3    Klier, A.4    Rapoport, G.5
  • 6
    • 0028917215 scopus 로고
    • Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria
    • Deutscher, J., E. Küster, U. Bergstedt, V. Charrier, and W. Hillen. 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
  • 7
    • 0022979375 scopus 로고
    • Streptococcal phosphoenolpyruvate-sugar phosphotransferase system: Amino acid sequence and site of ATP-dependent phosphorylation of HPr
    • Deutscher, J., B. Pevec, K. Beyreuther, H.-H. Kiltz, and W. Hengstenberg. 1986. Streptococcal phosphoenolpyruvate-sugar phosphotransferase system: amino acid sequence and site of ATP-dependent phosphorylation of HPr. Biochemistry 25:6543-6551.
    • (1986) Biochemistry , vol.25 , pp. 6543-6551
    • Deutscher, J.1    Pevec, B.2    Beyreuther, K.3    Kiltz, H.-H.4    Hengstenberg, W.5
  • 8
    • 0028364161 scopus 로고
    • Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis
    • Deutscher, J., J. Reizer, C. Fischer, A. Galinier, M. H. Saier, and M. Steinmetz. 1994. Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis. J. Bacteriol. 174:3336-3344.
    • (1994) J. Bacteriol. , vol.174 , pp. 3336-3344
    • Deutscher, J.1    Reizer, J.2    Fischer, C.3    Galinier, A.4    Saier, M.H.5    Steinmetz, M.6
  • 9
    • 0020851355 scopus 로고
    • ATP-dependent, protein kinase-catalyzed phosphorylation of a seryl residue in HPr, a phosphoryl carrier protein of the phosphotransferase system in Streptococcus pyogenes
    • Deutscher, J., and M. H. Saier. 1983. ATP-dependent, protein kinase-catalyzed phosphorylation of a seryl residue in HPr, a phosphoryl carrier protein of the phosphotransferase system in Streptococcus pyogenes. Proc. Natl. Acad. Sci, USA 80:6790-6794.
    • (1983) Proc. Natl. Acad. Sci, USA , vol.80 , pp. 6790-6794
    • Deutscher, J.1    Saier, M.H.2
  • 12
    • 0032900617 scopus 로고    scopus 로고
    • Phosphorylation and functional properties of the IIA domain of the lactose transport protein of Streptococcus thermophilus
    • Gunnewijk, M. G. W., P. W. Postma, and B. Poolman. 1999. Phosphorylation and functional properties of the IIA domain of the lactose transport protein of Streptococcus thermophilus. J. Bacteriol. 181:632-641.
    • (1999) J. Bacteriol. , vol.181 , pp. 632-641
    • Gunnewijk, M.G.W.1    Postma, P.W.2    Poolman, B.3
  • 13
    • 0026033650 scopus 로고
    • Catabolite repression of alpha-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacI and galR repressors
    • Henkin, T. M., F. J. Grundy, W. L. Nicholson, and G. H. Chambliss. 1991. Catabolite repression of alpha-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacI 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
  • 14
    • 0028907495 scopus 로고
    • Catabolite repression in Bacillus subtilis: A global regulatory mechanism for Gram-positive bacteria?
    • Hueck, C. J., and W. Hillen. 1995. Catabolite repression in Bacillus subtilis: a global regulatory mechanism for Gram-positive bacteria? Mol. Microbiol. 15:395-401.
    • (1995) Mol. Microbiol. , vol.15 , pp. 395-401
    • Hueck, C.J.1    Hillen, W.2
  • 15
    • 0028086366 scopus 로고
    • Analysis of a cis-active sequence mediating catabolite repression in Gram-positive bacteria
    • Hueck, C. J., W. Hillen, and M. H. Saier. 1994. Analysis of a cis-active sequence mediating catabolite repression in Gram-positive bacteria. Res. Microbiol. 145:503-518.
    • (1994) Res. Microbiol. , vol.145 , pp. 503-518
    • Hueck, C.J.1    Hillen, W.2    Saier, M.H.3
  • 16
    • 0028264818 scopus 로고
    • Catabolite repression of the Bacillus subtilis xyl operon involves a cis element functional in the context of an unrelated sequence, and glucose exerts additional xylR-dependent repression
    • Kraus, A., C. Hueck, D. Gärtner, and W. Hillen. 1994. Catabolite repression of the Bacillus subtilis xyl operon involves a cis element functional in the context of an unrelated sequence, and glucose exerts additional xylR-dependent repression. J. Bacteriol. 176:1738-1745.
    • (1994) J. Bacteriol. , vol.176 , pp. 1738-1745
    • Kraus, A.1    Hueck, C.2    Gärtner, D.3    Hillen, W.4
  • 17
    • 0029916568 scopus 로고    scopus 로고
    • Transcriptional analysis of the bglPH expression in Bacillus subtilis: Evidence for two distinct pathways mediating carbon catabolite repression
    • Krüger, S., S. Gertz, and M. Hecker. 1996. Transcriptional analysis of the 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
  • 18
    • 0029619251 scopus 로고
    • Regulation of the putative bglPH operon for aryl-β-glucoside utilization in Bacillus subtilis
    • Krüger, S., and M. Hecker. 1995. Regulation of the putative bglPH operon for aryl-β-glucoside utilization in Bacillus subtilis. J. Bacteriol. 177:5590-5597.
    • (1995) J. Bacteriol. , vol.177 , pp. 5590-5597
    • Krüger, S.1    Hecker, M.2
  • 19
    • 0027365675 scopus 로고
    • Catabolite repression of β-glucanase synthesis in Bacillus subtilis
    • Krüger, S., J. Stülke, and M. Hecker. 1993. Catabolite repression of β-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
  • 21
    • 0029006115 scopus 로고
    • Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis
    • Kunst, F., and G. Rapoport. 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
  • 22
    • 0025643362 scopus 로고
    • A general method for rapid site-directed mutagenesis using the polymerase chain reaction
    • Landt, O., H.-P. Grunert, and U. Hahn. 1990. A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene 96:125-128.
    • (1990) Gene , vol.96 , pp. 125-128
    • Landt, O.1    Grunert, H.-P.2    Hahn, U.3
  • 23
    • 0028986940 scopus 로고
    • New β-glucoside (bgl) genes in Bacillus subtilis: The bglP gene product has both transport and regulatory functions, similar to those of BglF, its Escherichia coli homolog
    • Le Coq, D., C. Lindner, S. Krüger, M. Steinmetz, and J. Stülke. 1995. New β-glucoside (bgl) genes in Bacillus subtilis: the bglP gene product has both transport and regulatory functions, similar to those of BglF, its Escherichia coli homolog. J. Bacteriol. 177:1527-1535.
    • (1995) J. Bacteriol. , vol.177 , pp. 1527-1535
    • Le Coq, D.1    Lindner, C.2    Krüger, S.3    Steinmetz, M.4    Stülke, J.5
  • 24
    • 0026515270 scopus 로고
    • SpbA locus ensures the segregational stability of pTh1030, a novel type of Gram-positive replicon
    • Lereclus, D., and O. Arantes. 1992. spbA locus ensures the segregational stability of pTH1030, a novel type of Gram-positive replicon. Mol. Microbiol. 6:35-46.
    • (1992) Mol. Microbiol. , vol.6 , pp. 35-46
    • Lereclus, D.1    Arantes, O.2
  • 25
    • 0032905438 scopus 로고    scopus 로고
    • Regulation of the activity of the Bacillus subtilis antiterminator LicT by PEP-dependent, enzyme I- and HPr-catalyzed phosphorylation
    • Lindner, C., A. Galinier, M. Hecker, and J. Deutscher. 1999. Regulation of the activity of the Bacillus subtilis antiterminator LicT by PEP-dependent, enzyme I- and HPr-catalyzed phosphorylation. Mol. Microbiol. 3:995-1006.
    • (1999) Mol. Microbiol. , vol.3 , pp. 995-1006
    • Lindner, C.1    Galinier, A.2    Hecker, M.3    Deutscher, J.4
  • 26
    • 0020058862 scopus 로고
    • Physical and genetic characterization of symbiotic and auxotrophic mutants of Rhizobium meliloti induced by transposon Tn5 mutagenesis
    • Maede, H. M., S. R. Long, G. B. Ruvkun, S. E. Brown, and F. M. Ausubel. 1982. Physical and genetic characterization of symbiotic and auxotrophic mutants of Rhizobium meliloti induced by transposon Tn5 mutagenesis. J. Bacteriol. 149:114-122.
    • (1982) J. Bacteriol. , vol.149 , pp. 114-122
    • Maede, H.M.1    Long, S.R.2    Ruvkun, G.B.3    Brown, S.E.4    Ausubel, F.M.5
  • 27
  • 28
    • 0025142206 scopus 로고
    • Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating the expression of the operon
    • Martin-Verstraete, I., M. Débarbouillé, A. Klier, and G. Rapoport. 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
  • 29
    • 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., M. Débarbouillé, A. Klier, and G. Rapoport. 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
  • 30
    • 0028859554 scopus 로고
    • Two different mechanisms mediate catabolite repression of the Bacillus subtilis levanase operon
    • Martin-Verstraete, I., J. Stülke, A. Klier, and G. Rapoport. 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
  • 31
    • 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
  • 32
    • 0028935455 scopus 로고
    • Subtilist: A relational database for the Bacillus subtilis genome
    • Moszer, I., P. Glaser, and A. Danchin. 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
  • 33
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate:Carbohydrate phosphotransferase systems of bacteria
    • Postma, P. W., J. W. Lengeler, and G. R. Jacobson. 1993. Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 57:543-594.
    • (1993) Microbiol. Rev. , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 36
    • 0024554141 scopus 로고
    • Protein phosphorylation and allosteric control of inducer exclusion and catabolite repression by the bacterial phosphoenolpyruvate: Sugar phosphotransferase system
    • Saier, M. H. 1989. Protein phosphorylation and allosteric control of inducer exclusion and catabolite repression by the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Microbiol. Rev. 53:109-120.
    • (1989) Microbiol. Rev. , vol.53 , pp. 109-120
    • Saier, M.H.1
  • 37
    • 0026546539 scopus 로고
    • Proposed uniform nomenclature for the proteins and the protein domains of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system
    • Saier, M. H., and J. Reizer. 1992. Proposed uniform nomenclature for the proteins and the protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. J. Bacteriol. 174:1433-1438.
    • (1992) J. Bacteriol. , vol.174 , pp. 1433-1438
    • Saier, M.H.1    Reizer, J.2
  • 40
    • 0029971285 scopus 로고    scopus 로고
    • LicT, a Bacillus subtilis transcriptional antiterminator protein of the bg1g family
    • Schnetz, K., J. Stülke, S. Gertz, S. Krüger, M. Krieg, M. Hecker, and B. Rak. 1996. LicT, a Bacillus subtilis transcriptional antiterminator protein of the Bg1G family. J. Bacteriol. 178:1971-1979.
    • (1996) J. Bacteriol. , vol.178 , pp. 1971-1979
    • Schnetz, K.1    Stülke, J.2    Gertz, S.3    Krüger, S.4    Krieg, M.5    Hecker, M.6    Rak, B.7
  • 41
    • 0001954586 scopus 로고
    • Carbohydrate catabolism: Pathways, enzymes, genetic regulation, and evolution
    • A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), American Society for Microbiology, Washington, D.C.
    • Steinmetz, M. 1993. Carbohydrate catabolism: pathways, enzymes, genetic regulation, and evolution, p. 157-170. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and other gram-positive bacteria: biochemistry, physiology, and molecular genetics. American Society for Microbiology, Washington, D.C.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria: Biochemistry, Physiology, and Molecular Genetics , pp. 157-170
    • Steinmetz, M.1
  • 42
    • 0031808469 scopus 로고    scopus 로고
    • PRD - A protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria
    • Stülke, J., M. Arnaud, G. Rapoport, and I. Martin-Verstraete. 1998. PRD - a protein domain involved in PTS-dependent induction and carbon 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
    • 0027524789 scopus 로고
    • Temporal activation of β-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool
    • Stülke, J., R. Hanschke, and M. Hecker. 1993. Temporal activation of β-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
  • 44
    • 0028783423 scopus 로고
    • The HPr protein of the phosphotransferase system links induction and catabolite repression of the Bacillus subtilis levanase operon
    • Stülke, J., I. Martin-Verstraete, V. Charrier, A. Klier, J. Deutscher, and G. Rapoport. 1995. The HPr protein of the phosphotransferase system links induction and catabolite repression of the Bacillus subtilis levanase operon. J. Bacteriol. 177:6928-6936.
    • (1995) J. Bacteriol. , vol.177 , pp. 6928-6936
    • Stülke, J.1    Martin-Verstraete, I.2    Charrier, V.3    Klier, A.4    Deutscher, J.5    Rapoport, G.6
  • 45
    • 0030742667 scopus 로고    scopus 로고
    • Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GlcT
    • Stülke, J., I. Martin-Verstraete, M. Zagorec, M. Rose, A. Klier, and G. Rapoport. 1997. Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GlcT. 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
  • 46
    • 0344329740 scopus 로고    scopus 로고
    • Unpublished results
    • Tobisch, S. Unpublished results.
    • Tobisch, S.1
  • 47
    • 0031032671 scopus 로고    scopus 로고
    • Identification and characterization of a new β-glucoside utilization system in Bacillus subtilis
    • Tobisch, S., P. Glaser, S. Krüger, and M. Hecker. 1997. Identification and characterization of a new β-glucoside utilization system in Bacillus subtilis. J. Bacteriol. 179:496-506.
    • (1997) J. Bacteriol. , vol.179 , pp. 496-506
    • Tobisch, S.1    Glaser, P.2    Krüger, S.3    Hecker, M.4
  • 48
    • 0030758035 scopus 로고    scopus 로고
    • Multiple phosphorylation of SacY, a Bacillus subtilis antiterminator negatively controlled by the phosphotransferase system
    • Tortosa, P., S. Aymerich, C. Lindner, M. H. Saier, J. Reizer, and D. Le Coq. 1997. Multiple phosphorylation of SacY, a Bacillus subtilis antiterminator negatively controlled by the phosphotransferase system. J. Biol. Chem. 272: 17230-17237.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17230-17237
    • Tortosa, P.1    Aymerich, S.2    Lindner, C.3    Saier, M.H.4    Reizer, J.5    Le Coq, D.6


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