메뉴 건너뛰기




Volumn 24, Issue 4, 1997, Pages 825-837

Role of the transcriptional activator RocR in the arginine-degradation pathway of Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; RNA POLYMERASE;

EID: 0030967333     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1997.3881754.x     Document Type: Article
Times cited : (67)

References (60)
  • 1
    • 0025086410 scopus 로고
    • CUG as a mutant start codon for cat-86 and xyIE in Bacillus subtilis
    • Ambulos, N.J., Smith, T., Mulbry, W., and Lovett, P.S. (1990) CUG as a mutant start codon for cat-86 and xyIE in Bacillus subtilis. Gene 94: 125-128.
    • (1990) Gene , vol.94 , pp. 125-128
    • Ambulos, N.J.1    Smith, T.2    Mulbry, W.3    Lovett, P.S.4
  • 2
    • 0023156843 scopus 로고
    • Characterization of the sacQ genes from Bacillus licheniformis and Bacillus subtilis
    • Amory, A., Kunst, F., Aubert, E., Klier, A., and Rapoport, G. (1987) Characterization of the sacQ genes from Bacillus licheniformis and Bacillus subtilis. J Bacteriol 169: 324-333.
    • (1987) J Bacteriol , vol.169 , pp. 324-333
    • Amory, A.1    Kunst, F.2    Aubert, E.3    Klier, A.4    Rapoport, G.5
  • 3
    • 0025786601 scopus 로고
    • Construction of cloning vectors for Bacillus thuringiensis
    • Arantes, O., and Lereclus, D. (1991) Construction of cloning vectors for Bacillus thuringiensis. Gene 108: 115-119.
    • (1991) Gene , vol.108 , pp. 115-119
    • Arantes, O.1    Lereclus, D.2
  • 4
    • 0029743218 scopus 로고    scopus 로고
    • Modulation of NifA activity by PII in Azospirillum brasilense - Evidence for a regulatory role of the NifA N-terminal domain
    • Arsène, F., Kaminski, P.A., and Elmerich, C. (1996) Modulation of NifA activity by PII in Azospirillum brasilense - evidence for a regulatory role of the NifA N-terminal domain. J Bacteriol 178: 4830-4838.
    • (1996) J Bacteriol , vol.178 , pp. 4830-4838
    • Arsène, F.1    Kaminski, P.A.2    Elmerich, C.3
  • 5
    • 0028363001 scopus 로고
    • Purification and in vitro activity of a truncated form of AnfA
    • Austin, S., and Lambert, J. (1994) Purification and in vitro activity of a truncated form of AnfA. J Biol Chem 269: 18141-18148.
    • (1994) J Biol Chem , vol.269 , pp. 18141-18148
    • Austin, S.1    Lambert, J.2
  • 6
    • 0018409601 scopus 로고
    • Carbon and nitrogen repression of arginine catabolic enzymes in Bacillus subtilis
    • Baumberg, S., and Harwood, C.R. (1979) Carbon and nitrogen repression of arginine catabolic enzymes in Bacillus subtilis. J Bacteriol 137: 189-196.
    • (1979) J Bacteriol , vol.137 , pp. 189-196
    • Baumberg, S.1    Harwood, C.R.2
  • 7
    • 0007653647 scopus 로고
    • Biosynthesis of arginine, proline and related compounds
    • Sonenshein, A.L., Hoch, J.A., and Losick, R. (eds). Washington, DC: American Society for Microbiology
    • Baumberg, S., and Klingel, U. (1993) Biosynthesis of arginine, proline and related compounds. In Bacillus subtilis and Other Gram-positive Bacteria: Biochemistry, Physiology and Molecular Genetics. Sonenshein, A.L., Hoch, J.A., and Losick, R. (eds). Washington, DC: American Society for Microbiology, pp. 299-306.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria: Biochemistry, Physiology and Molecular Genetics , pp. 299-306
    • Baumberg, S.1    Klingel, U.2
  • 8
    • 0027958569 scopus 로고
    • The isolated catalytic domain of NifA, a bacterial enhancer-binding protein, activates transcription in vitro: Activation is inhibited by NifL
    • Berger, D.K., Narberhaus, F., and Kustu, S. (1994) The isolated catalytic domain of NifA, a bacterial enhancer-binding protein, activates transcription in vitro: activation is inhibited by NifL. Proc Natl Acad Sci USA 91: 103-107.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 103-107
    • Berger, D.K.1    Narberhaus, F.2    Kustu, S.3
  • 9
    • 0028208257 scopus 로고
    • RocR, a novel regulatory protein controlling arginine utilization in Bacillus subtilis, belongs to the NtrC/NifA family of transcriptional activators
    • Calogero, S., Gardan, R., Glaser, P., Schweizer, J., Rapoport, G., and Débarbouillé, M. (1994) RocR, a novel regulatory protein controlling arginine utilization in Bacillus subtilis, belongs to the NtrC/NifA family of transcriptional activators. J Bacteriol 176: 1234-1241.
    • (1994) J Bacteriol , vol.176 , pp. 1234-1241
    • Calogero, S.1    Gardan, R.2    Glaser, P.3    Schweizer, J.4    Rapoport, G.5    Débarbouillé, M.6
  • 10
    • 0015385368 scopus 로고
    • Non-chromosomal antibiotic resistance in bacteria: Genetic transformation of Escherichia coli by R-factor DNA
    • Cohen, S.N., Chang, A.C.Y., and Hsu, L. (1972) Non-chromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA. Proc Natl Acad Sci USA 69: 2110-2114.
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 2110-2114
    • Cohen, S.N.1    Chang, A.C.Y.2    Hsu, L.3
  • 11
    • 0026529106 scopus 로고
    • Purification and initial characterization of AhrC: The regulator of arginine metabolism genes in Bacillus subtilis
    • Czaplewski, L.G., North, A.K., Smith, M.C.M., Baumberg, S., and Stockley, P.G. (1992) Purification and initial characterization of AhrC: the regulator of arginine metabolism genes in Bacillus subtilis. Mol Microbiol 6: 267-275.
    • (1992) Mol Microbiol , vol.6 , pp. 267-275
    • Czaplewski, L.G.1    North, A.K.2    Smith, M.C.M.3    Baumberg, S.4    Stockley, P.G.5
  • 13
    • 0028244041 scopus 로고
    • Genetic evidence for activation of the positive transcriptional regulator XyIR, a member of the NtrC family of regulators, by effector binding
    • Delgado, A., and Ramos, J.L. (1994) Genetic evidence for activation of the positive transcriptional regulator XyIR, a member of the NtrC family of regulators, by effector binding. J Biol Chem 269: 8059-8062.
    • (1994) J Biol Chem , vol.269 , pp. 8059-8062
    • Delgado, A.1    Ramos, J.L.2
  • 14
    • 0028912178 scopus 로고
    • Single amino acids changes in the signal receptor domain of XyIR resulted in mutants that stimulate transcription in the absence of effectors
    • Delgado, A., Salto, R., Marques, S., and Ramos, J.L. (1995) Single amino acids changes in the signal receptor domain of XyIR resulted in mutants that stimulate transcription in the absence of effectors. J Biol Chem 270: 5144-5150.
    • (1995) J Biol Chem , vol.270 , pp. 5144-5150
    • Delgado, A.1    Salto, R.2    Marques, S.3    Ramos, J.L.4
  • 15
    • 0025783924 scopus 로고
    • Substitutions at a single amino acid residue in the nitrogen-regulated activator protein NtrC differentially influence its activity in response to phosphorylation
    • Dixon, R., Eydmann, T., Henderson, N., and Austin, S. (1991) Substitutions at a single amino acid residue in the nitrogen-regulated activator protein NtrC differentially influence its activity in response to phosphorylation. Mol Microbiol 5: 1657-1667.
    • (1991) Mol Microbiol , vol.5 , pp. 1657-1667
    • Dixon, R.1    Eydmann, T.2    Henderson, N.3    Austin, S.4
  • 16
    • 0025190798 scopus 로고
    • The function of isolated domains and chimaeric proteins constructed from the transcriptional activators NifA and NtrC of Klebsiella pneumoniae
    • Drummond, M.H., Contreras, A., and Mitchenall, L.A. (1990) The function of isolated domains and chimaeric proteins constructed from the transcriptional activators NifA and NtrC of Klebsiella pneumoniae. Mol Microbiol 4: 29-37.
    • (1990) Mol Microbiol , vol.4 , pp. 29-37
    • Drummond, M.H.1    Contreras, A.2    Mitchenall, L.A.3
  • 17
    • 0029063837 scopus 로고
    • Activation of the transcriptional regulator XyIR of Pseudomonas putida by release of repression between functional domains
    • Fernandez, S., de Lorenzo, V., and Pérez-Martin, J. (1995) Activation of the transcriptional regulator XyIR of Pseudomonas putida by release of repression between functional domains. Mol Microbiol 16: 205-213.
    • (1995) Mol Microbiol , vol.16 , pp. 205-213
    • Fernandez, S.1    De Lorenzo, V.2    Pérez-Martin, J.3
  • 18
    • 0028108941 scopus 로고
    • Genetic regulation of nitrogen fixation in rhizobia
    • Fischer, H.M. (1994) Genetic regulation of nitrogen fixation in rhizobia. Microbiol Rev 58: 352-386.
    • (1994) Microbiol Rev , vol.58 , pp. 352-386
    • Fischer, H.M.1
  • 19
    • 0001033092 scopus 로고
    • Utilization of amino acids and other nitrogen-containing compounds
    • Sonenshein, A.L., Hoch, J.A., and Losick, R. (eds). Washington, DC: American Society for Microbiology
    • Fisher, S.H. (1993) Utilization of amino acids and other nitrogen-containing compounds. In Bacillus subtilis and Other Gram-positive Bacteria: Biochemistry, Physiology and Molecular Genetics. Sonenshein, A.L., Hoch, J.A., and Losick, R. (eds). Washington, DC: American Society for Microbiology, pp. 221-228.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria: Biochemistry, Physiology and Molecular Genetics , pp. 221-228
    • Fisher, S.H.1
  • 20
    • 0029016807 scopus 로고
    • Constitutive forms of the enhancer-binding protein NtrC: Evidence that essential oligomerization determinants lie in the central activation domain
    • Flashner, Y., Weiss, D.S., Keener, J., and Kustu, S. (1995) Constitutive forms of the enhancer-binding protein NtrC: evidence that essential oligomerization determinants lie in the central activation domain. J Mol Biol 249: 700-713.
    • (1995) J Mol Biol , vol.249 , pp. 700-713
    • Flashner, Y.1    Weiss, D.S.2    Keener, J.3    Kustu, S.4
  • 21
    • 0029035341 scopus 로고
    • Expression of the rocDEF operon involved in arginine catabolism in Bacillus subtilis
    • Gardan, R., Rapoport, G., and Débarbouillé, M. (1995) Expression of the rocDEF operon involved in arginine catabolism in Bacillus subtilis. J Mol Biol 249: 843-856.
    • (1995) J Mol Biol , vol.249 , pp. 843-856
    • Gardan, R.1    Rapoport, G.2    Débarbouillé, M.3
  • 23
    • 0028286432 scopus 로고
    • Rhizobium meliloti DctD, a sigma 54-dependent transcriptional activator, may be negatively controlled by a subdomain in the C-terminal end of its two-component receiver module
    • Gu, B., Lee, J.H., Hoover, T.R., Scholl, D., and Nixon, B.T. (1994) Rhizobium meliloti DctD, a sigma 54-dependent transcriptional activator, may be negatively controlled by a subdomain in the C-terminal end of its two-component receiver module. Mol Microbiol 13: 51-66.
    • (1994) Mol Microbiol , vol.13 , pp. 51-66
    • Gu, B.1    Lee, J.H.2    Hoover, T.R.3    Scholl, D.4    Nixon, B.T.5
  • 24
    • 0017379984 scopus 로고
    • Arginine hydroxamate-resistant mutants of Bacillus subtilis with altered control of arginine metabolism
    • Harwood, C.R., and Baumberg, S. (1977) Arginine hydroxamate-resistant mutants of Bacillus subtilis with altered control of arginine metabolism. J Gen Microbiol 100: 177-188.
    • (1977) J Gen Microbiol , vol.100 , pp. 177-188
    • Harwood, C.R.1    Baumberg, S.2
  • 25
    • 0029875231 scopus 로고    scopus 로고
    • Azotobacter vinelandii NifL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via a redox-sensitive switch
    • Hill, S., Austin, S., Eydmann, T., Jones, T., and Dixon, R. (1996) Azotobacter vinelandii NifL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via a redox-sensitive switch. Proc Natl Acad Sci USA 93: 2143-2148.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2143-2148
    • Hill, S.1    Austin, S.2    Eydmann, T.3    Jones, T.4    Dixon, R.5
  • 27
    • 0029044907 scopus 로고
    • Effector-mediated stimulation of ATPase activity by the sigma 54-dependent transcriptional activator FhIA from Escherichia coli
    • Hopper, S., and Bock, A. (1995) Effector-mediated stimulation of ATPase activity by the sigma 54-dependent transcriptional activator FhIA from Escherichia coli. J Bacteriol 177: 2798-2803.
    • (1995) J Bacteriol , vol.177 , pp. 2798-2803
    • Hopper, S.1    Bock, A.2
  • 28
    • 0024687595 scopus 로고
    • The central domain of Rhizobium meliloti NifA is sufficient to activate transcription from the R. meliloti nifH promoter
    • Huala, E., and Ausubel, F.M. (1989) The central domain of Rhizobium meliloti NifA is sufficient to activate transcription from the R. meliloti nifH promoter. J Bacteriol 171: 3354-3365.
    • (1989) J Bacteriol , vol.171 , pp. 3354-3365
    • Huala, E.1    Ausubel, F.M.2
  • 29
    • 0026532670 scopus 로고
    • The central domain of Rhizobium leguminosarum DctD functions independently to activate transcription
    • Huala, E., Stigter, J., and Ausubel, P.M. (1992) The central domain of Rhizobium leguminosarum DctD functions independently to activate transcription. J Bacteriol 174: 1428-1431.
    • (1992) J Bacteriol , vol.174 , pp. 1428-1431
    • Huala, E.1    Stigter, J.2    Ausubel, P.M.3
  • 30
    • 0029094338 scopus 로고
    • A binding site for activation by the Bacillus subtilis AhrC protein, a repressor/activator of arginine metabolism
    • Klingel, U., Miller, C.M., North, A.K., Stockley, P.G., and Baumberg, S. (1995) A binding site for activation by the Bacillus subtilis AhrC protein, a repressor/activator of arginine metabolism. Mol Gen Genet 248: 329-340.
    • (1995) Mol Gen Genet , vol.248 , pp. 329-340
    • Klingel, U.1    Miller, C.M.2    North, A.K.3    Stockley, P.G.4    Baumberg, S.5
  • 31
    • 0027162310 scopus 로고
    • Glutamate at the site of phosphorylation of nitrogen-regulatory protein NtrC mimics aspartyl-phosphate and activates the protein
    • Klose, K.E., Weiss, D.S., and Kustu, S. (1993) Glutamate at the site of phosphorylation of nitrogen-regulatory protein NtrC mimics aspartyl-phosphate and activates the protein. J Mol Biol 232: 67-78.
    • (1993) J Mol Biol , vol.232 , pp. 67-78
    • Klose, K.E.1    Weiss, D.S.2    Kustu, S.3
  • 33
    • 0026670606 scopus 로고
    • A defined amino acid exchange close to the putative nucleotide binding site is responsible for an oxygen-tolerant variant of the Rhizobium meliloti NifA protein
    • Krey, R., Puhler, A., and Klipp, W. (1992) A defined amino acid exchange close to the putative nucleotide binding site is responsible for an oxygen-tolerant variant of the Rhizobium meliloti NifA protein. Mol Gen Genet 234: 433-441.
    • (1992) Mol Gen Genet , vol.234 , pp. 433-441
    • Krey, R.1    Puhler, A.2    Klipp, W.3
  • 34
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., Roberts, J.D., and Zakour, R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol 154: 367-382.
    • (1987) Methods Enzymol , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 35
    • 0000885909 scopus 로고
    • Signal transduction network controlling degradative enzyme synthesis and competence in Bacillus subtilis
    • Piggot, P.J., Moran, Jr, C.P., and Youngman, P. (eds). Washington, DC: American Society for Microbiology
    • Kunst, F., Msadek, T., and Rapoport, G. (1994) Signal transduction network controlling degradative enzyme synthesis and competence in Bacillus subtilis. In Regulation of Bacterial Differentiation. Piggot, P.J., Moran, Jr, C.P., and Youngman, P. (eds). Washington, DC: American Society for Microbiology, pp. 1-20.
    • (1994) Regulation of Bacterial Differentiation , pp. 1-20
    • Kunst, F.1    Msadek, T.2    Rapoport, G.3
  • 36
    • 0014320881 scopus 로고
    • Regulation of arginine and proline catabolism in Bacillus licheniformis
    • Laishley, E.J., and Bernlohr, R.W. (1966) Regulation of arginine and proline catabolism in Bacillus licheniformis. J Bacteriol 96: 322-329.
    • (1966) J Bacteriol , vol.96 , pp. 322-329
    • Laishley, E.J.1    Bernlohr, R.W.2
  • 37
    • 0026515270 scopus 로고
    • spbA locus ensures the segregational stability of pTH1030, a novel type of Grampositive replicon
    • Lereclus, D., and Arantes, O. (1992) spbA locus ensures the segregational stability of pTH1030, a novel type of Grampositive replicon. Mol Microbiol 6: 35-46.
    • (1992) Mol Microbiol , vol.6 , pp. 35-46
    • Lereclus, D.1    Arantes, O.2
  • 38
    • 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
  • 39
    • 0028038196 scopus 로고
    • Interactions of wild-type and truncated LevR of Bacillus subtilis with the upstream activating sequence of the levanase operon
    • Martin-Verstraete, I., Débarbouillé, M., Klier, A., and Rapoport, G. (1994) Interactions of wild-type and truncated LevR of Bacillus subtilis with the upstream activating sequence of the levanase operon. J Mol Biol 241: 178-192.
    • (1994) J Mol Biol , vol.241 , pp. 178-192
    • Martin-Verstraete, I.1    Débarbouillé, M.2    Klier, A.3    Rapoport, G.4
  • 40
    • 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
  • 41
    • 0003785155 scopus 로고
    • Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 42
    • 0027262522 scopus 로고
    • Alterations of highly conserved residues in the regulatory domain of nitrogen regulator I (NtrC) of Escherichia coli
    • Moore, J.B., Shiau, S.P., and Reitzer, L.J. (1993) Alterations of highly conserved residues in the regulatory domain of nitrogen regulator I (NtrC) of Escherichia coli. J Bacteriol 175: 2692-2701.
    • (1993) J Bacteriol , vol.175 , pp. 2692-2701
    • Moore, J.B.1    Shiau, S.P.2    Reitzer, L.J.3
  • 43
    • 0027340543 scopus 로고
    • 54 bacterial enhancer-binding protein family: Mechanism of action and phylogenetic relationship of their functional domains
    • 54 bacterial enhancer-binding protein family: mechanism of action and phylogenetic relationship of their functional domains. J Bacteriol 175: 6067-6074.
    • (1993) J Bacteriol , vol.175 , pp. 6067-6074
    • Morett, E.1    Segovia, L.2
  • 44
    • 0018976017 scopus 로고
    • Map locations of some mutations conferring resistance to arginine hydroxamate in Bacillus subtilis 168
    • Mountain, A., and Baumberg, S. (1980) Map locations of some mutations conferring resistance to arginine hydroxamate in Bacillus subtilis 168. Mol Gen Genet 178: 691-701.
    • (1980) Mol Gen Genet , vol.178 , pp. 691-701
    • Mountain, A.1    Baumberg, S.2
  • 45
    • 0025164975 scopus 로고
    • Signal transduction pathway controlling synthesis of a class of degradative enzymes in Bacillus subtilis: Expression of the regulatory genes and analysis of mutations in degS and degU
    • Msadek, T., Kunst, F., Henner, D., Klier, A., Rapoport, G., and Dedonder, R. (1990) Signal transduction pathway controlling synthesis of a class of degradative enzymes in Bacillus subtilis: expression of the regulatory genes and analysis of mutations in degS and degU. J Bacteriol 172: 824-834.
    • (1990) J Bacteriol , vol.172 , pp. 824-834
    • Msadek, T.1    Kunst, F.2    Henner, D.3    Klier, A.4    Rapoport, G.5    Dedonder, R.6
  • 46
    • 0023461268 scopus 로고
    • Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction
    • Mullis, K.B., and Faloona, F.A. (1987) Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction. Methods Enzymol 155: 335-350.
    • (1987) Methods Enzymol , vol.155 , pp. 335-350
    • Mullis, K.B.1    Faloona, F.A.2
  • 47
    • 0038566311 scopus 로고    scopus 로고
    • Genetic evidence for interdomain regulation of the phenol-responsive sigma 54-dependent activator DmpR
    • Ng, L.C., O'Neill, E., and Shingler, V. (1996) Genetic evidence for interdomain regulation of the phenol-responsive sigma 54-dependent activator DmpR. J Biol Chem 271: 17281-17286.
    • (1996) J Biol Chem , vol.271 , pp. 17281-17286
    • Ng, L.C.1    O'Neill, E.2    Shingler, V.3
  • 48
    • 0024401032 scopus 로고
    • Nucleotide sequence of a Bacillus subtilis arginine regulatory gene and homology of its product to the Escherichia coli arginine repressor
    • North, A.K., Smith, M.C.M., and Baumberg, S. (1989) Nucleotide sequence of a Bacillus subtilis arginine regulatory gene and homology of its product to the Escherichia coli arginine repressor. Gene 80: 29-38.
    • (1989) Gene , vol.80 , pp. 29-38
    • North, A.K.1    Smith, M.C.M.2    Baumberg, S.3
  • 49
    • 0029073435 scopus 로고
    • The amino terminal domain of the prokaryotic enhancer-binding protein XyIR is a specific intramolecular repressor
    • Pérez-Martin, J., and de Lorenzo, V. (1995) The amino terminal domain of the prokaryotic enhancer-binding protein XyIR is a specific intramolecular repressor. Proc Natl Acad Sci USA 92: 9392-9396.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9392-9396
    • Pérez-Martin, J.1    De Lorenzo, V.2
  • 52
    • 0017681196 scopus 로고
    • DNA sequencing with chain terminating inhibitors
    • Sanger, F., Nicklen, S., and Coulson, A.R. (1977) DNA sequencing with chain terminating inhibitors. Proc Natl Acad Sci USA 74: 5463-5467.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5463-5467
    • Sanger, F.1    Nicklen, S.2    Coulson, A.R.3
  • 53
    • 9344269892 scopus 로고    scopus 로고
    • Iron is required to relieve inhibitory effects of NifL on transcriptional activation by NifA in Klebsiella pneumoniae
    • Schmitz, R.A., He, L.H., and Kustu, S. (1996) Iron is required to relieve inhibitory effects of NifL on transcriptional activation by NifA in Klebsiella pneumoniae. J Bacteriol 178: 4679-4687.
    • (1996) J Bacteriol , vol.178 , pp. 4679-4687
    • Schmitz, R.A.1    He, L.H.2    Kustu, S.3
  • 54
    • 0029670970 scopus 로고    scopus 로고
    • Signal sensing by sigma 54-dependent regulators: Derepression as a control mechanism
    • Shingler, V. (1996) Signal sensing by sigma 54-dependent regulators: derepression as a control mechanism. Mol Microbiol 19: 409-416.
    • (1996) Mol Microbiol , vol.19 , pp. 409-416
    • Shingler, V.1
  • 55
    • 0028325759 scopus 로고
    • Sensing of aromatic compounds by the DmpR transcriptional activator of phenol-catabolizing Pseudomonas sp. strain CF600
    • Shingler, V., and Moore, T. (1994) Sensing of aromatic compounds by the DmpR transcriptional activator of phenol-catabolizing Pseudomonas sp. strain CF600. J Bacteriol 176: 1555-1560.
    • (1994) J Bacteriol , vol.176 , pp. 1555-1560
    • Shingler, V.1    Moore, T.2
  • 56
    • 0029132191 scopus 로고
    • Direct regulation of the ATPase activity of the transcriptional activator DmpR by aromatic compounds
    • Shingler, V., and Pavel, H. (1995) Direct regulation of the ATPase activity of the transcriptional activator DmpR by aromatic compounds. Mol Microbiol 17: 505-513.
    • (1995) Mol Microbiol , vol.17 , pp. 505-513
    • Shingler, V.1    Pavel, H.2
  • 57
    • 0028783423 scopus 로고
    • The HPr protein of the phosphotransferase system links induction and catabolite repression of the Bacillus subtilis levanase operon
    • Stülke, J., Martin-Verstraete, I., Charrier, V., Klier, A., Deutscher, J., and Rapoport, G. (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
  • 58
    • 0020604683 scopus 로고
    • Nucleotide sequence of the Streptococcus faecalis plasmid gene encoding the 3′5′-aminoglycoside phosphotransferase type III
    • Trieu-Cuot, P., and Courvalin, P. (1983) Nucleotide sequence of the Streptococcus faecalis plasmid gene encoding the 3′5′-aminoglycoside phosphotransferase type III. Gene 23: 331-341.
    • (1983) Gene , vol.23 , pp. 331-341
    • Trieu-Cuot, P.1    Courvalin, P.2
  • 59
    • 0024720211 scopus 로고
    • Mutations in the gInG gene of Escherichia coli that result in increased activity of nitrogen regulator I
    • Weglenski, P., Ninfa, A.J., Ueno, N.S., and Magasanik, B. (1989) Mutations in the gInG gene of Escherichia coli that result in increased activity of nitrogen regulator I. J Bacteriol 171: 4479-4485.
    • (1989) J Bacteriol , vol.171 , pp. 4479-4485
    • Weglenski, P.1    Ninfa, A.J.2    Ueno, N.S.3    Magasanik, B.4
  • 60
    • 0024403543 scopus 로고
    • The Q-linker: A class of interdomain sequences found in bacterial multi-domain regulatory protein
    • Wootton, J.C., and Drummond, M.H. (1989) The Q-linker: a class of interdomain sequences found in bacterial multi-domain regulatory protein. Protein Eng 2: 535-543.
    • (1989) Protein Eng , vol.2 , pp. 535-543
    • Wootton, J.C.1    Drummond, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.