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Volumn 57, Issue 2, 2005, Pages 576-591

The transcriptional activator ClgR controls transcription of genes involved in proteolysis and DNA repair in Corynebacterium glutamicum

Author keywords

[No Author keywords available]

Indexed keywords

CLGR PROTEIN; DNA; ENDOPEPTIDASE LA; MITOMYCIN C; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 22144447873     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2005.04710.x     Document Type: Article
Times cited : (47)

References (35)
  • 1
    • 85008585468 scopus 로고
    • Taxonomical studies on glutamic acid producing bacteria
    • Abe, S., Takayama, K., and Kinoshita, S. (1967) Taxonomical studies on glutamic acid producing bacteria. J Gen Appl Microbiol 13: 279-301.
    • (1967) J Gen Appl Microbiol , vol.13 , pp. 279-301
    • Abe, S.1    Takayama, K.2    Kinoshita, S.3
  • 2
    • 0025695556 scopus 로고
    • Molecular cloning, genetic characterization and DNA sequence analysis of the recM region of Bacillus subtilis
    • Alonso, J.C., Shirahige, K., and Ogasawara, N. (1990) Molecular cloning, genetic characterization and DNA sequence analysis of the recM region of Bacillus subtilis. Nucleic Acids Res 18: 6771-6777.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6771-6777
    • Alonso, J.C.1    Shirahige, K.2    Ogasawara, N.3
  • 3
  • 4
    • 2342606509 scopus 로고    scopus 로고
    • ClgR, a novel regulator of clp and Ion expression in Streptomyces
    • Bellier, A., and Mazodier, P. (2004) ClgR, a novel regulator of clp and Ion expression in Streptomyces. J Bacteriol 186: 3238-3248.
    • (2004) J Bacteriol , vol.186 , pp. 3238-3248
    • Bellier, A.1    Mazodier, P.2
  • 5
    • 0032698634 scopus 로고    scopus 로고
    • Transcription activation by catabolite activator protein (CAP)
    • Busby, S., and Ebright, R.H. (1999) Transcription activation by catabolite activator protein (CAP). J Mol Biol 293: 199-213.
    • (1999) J Mol Biol , vol.293 , pp. 199-213
    • Busby, S.1    Ebright, R.H.2
  • 6
    • 0025052104 scopus 로고
    • Cloning of the dapA dapB cluster of the lysine-secreting bacterium Corynebacterium glutamicum
    • Cremer, J., Eggeling, L., and Sahm, H. (1990) Cloning of the dapA dapB cluster of the lysine-secreting bacterium Corynebacterium glutamicum. Mol Gen Genet 220: 478-480.
    • (1990) Mol Gen Genet , vol.220 , pp. 478-480
    • Cremer, J.1    Eggeling, L.2    Sahm, H.3
  • 7
    • 0025912270 scopus 로고
    • A family of Corynebacterium glutamicum/Escherichia coli shuttle vectors for cloning, controlled gene expression, and promoter probing
    • Eikmanns, B.J., Kleinertz, E., Liebl, W., and Sahm, H. (1991) A family of Corynebacterium glutamicum/Escherichia coli shuttle vectors for cloning, controlled gene expression, and promoter probing. Gene 102: 93-98.
    • (1991) Gene , vol.102 , pp. 93-98
    • Eikmanns, B.J.1    Kleinertz, E.2    Liebl, W.3    Sahm, H.4
  • 8
    • 1942519868 scopus 로고    scopus 로고
    • clpC and clpP1P2 gene expression in Corynebacterium glutamicum is controlled by a regulatory network involving the transcriptional regulators ClgR and HspR as well as the ECF sigma factor σH
    • Engels, S., Schweitzer, J.E., Ludwig, C., Bott, M., and Schaffer, S. (2004) clpC and clpP1P2 gene expression in Corynebacterium glutamicum is controlled by a regulatory network involving the transcriptional regulators ClgR and HspR as well as the ECF sigma factor σH. Mol Microbiol 52: 285-302.
    • (2004) Mol Microbiol , vol.52 , pp. 285-302
    • Engels, S.1    Schweitzer, J.E.2    Ludwig, C.3    Bott, M.4    Schaffer, S.5
  • 9
    • 0000075317 scopus 로고
    • Techniques for transformation of E. coli
    • Glover, D.M. (ed.). Oxford: IRL Press
    • Hanahan, D. (1985) Techniques for transformation of E. coli. In DNA Cloning, Vol. 1. Glover, D.M. (ed.). Oxford: IRL Press, pp. 109-135.
    • (1985) DNA Cloning , vol.1 , pp. 109-135
    • Hanahan, D.1
  • 10
    • 0028030082 scopus 로고
    • Mechanisms underlying expression of Tn 10 encoded tetracycline resistance
    • Hillen, W., and Berens, C. (1994) Mechanisms underlying expression of Tn 10 encoded tetracycline resistance. Annu Rev Microbiol 48: 345-369.
    • (1994) Annu Rev Microbiol , vol.48 , pp. 345-369
    • Hillen, W.1    Berens, C.2
  • 11
    • 0032774281 scopus 로고    scopus 로고
    • Construction and application of new Corynebacterium glutamicum vectors
    • Jakoby, M., Ngouto-Nkili, C.E., and Burkovski, A. (1999) Construction and application of new Corynebacterium glutamicum vectors. Biotechnol Techniques 13: 437-441.
    • (1999) Biotechnol Techniques , vol.13 , pp. 437-441
    • Jakoby, M.1    Ngouto-Nkili, C.E.2    Burkovski, A.3
  • 12
    • 0038690474 scopus 로고    scopus 로고
    • Regulation by proteolysis in bacterial cells
    • Jenal, U., and Hengge-Aronis, R. (2003) Regulation by proteolysis in bacterial cells. Curr Opin Microbiol 6: 163-172.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 163-172
    • Jenal, U.1    Hengge-Aronis, R.2
  • 13
    • 0025785770 scopus 로고
    • Protease II from Escherichia coli, sequencing and expression of the enzyme gene and characterization of the expressed enzyme
    • Kanatani, A., Masuda, T., Shimoda, T., Misoka, F., Lin, X.S., Yoshimoto, T., and Tsuru, D. (1991) Protease II from Escherichia coli, sequencing and expression of the enzyme gene and characterization of the expressed enzyme. J Biochem (Tokyo) 110: 315-320.
    • (1991) J Biochem (Tokyo) , vol.110 , pp. 315-320
    • Kanatani, A.1    Masuda, T.2    Shimoda, T.3    Misoka, F.4    Lin, X.S.5    Yoshimoto, T.6    Tsuru, D.7
  • 14
    • 0029910627 scopus 로고    scopus 로고
    • A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY
    • Kihara, A., Akiyama, Y., and Ito, K. (1996) A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY. EMBO J 15: 6122-6131.
    • (1996) EMBO J , vol.15 , pp. 6122-6131
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 15
    • 0032431906 scopus 로고    scopus 로고
    • The first gene of the Bacillus subtilis clpC operon, ctsR, encodes a negative regulator of its own operon and other class III heat shock genes
    • Krüger, E., and Hecker, M. (1998) The first gene of the Bacillus subtilis clpC operon, ctsR, encodes a negative regulator of its own operon and other class III heat shock genes. J Bacteriol 180: 6681-6688.
    • (1998) J Bacteriol , vol.180 , pp. 6681-6688
    • Krüger, E.1    Hecker, M.2
  • 16
    • 0035865140 scopus 로고    scopus 로고
    • Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor
    • Krüger, E., Zühlke, D., Witt, E., Ludwig, H., and Hecker, M. (2001) Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor. EMBO J 20: 852-863.
    • (2001) EMBO J , vol.20 , pp. 852-863
    • Krüger, E.1    Zühlke, D.2    Witt, E.3    Ludwig, H.4    Hecker, M.5
  • 17
    • 0037883611 scopus 로고    scopus 로고
    • Global expression profiling and physiological characterization of Corynebacterium glutamicum grown in the presence of L-valine
    • Lange, C., Rittmann, D., Wendisch, V.F., Bott, M., and Sahm, H. (2003) Global expression profiling and physiological characterization of Corynebacterium glutamicum grown in the presence of L-valine. Appl Environ Microbiol 69: 2521-2532.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 2521-2532
    • Lange, C.1    Rittmann, D.2    Wendisch, V.F.3    Bott, M.4    Sahm, H.5
  • 18
    • 0037295566 scopus 로고    scopus 로고
    • Crystal structure of YbaB from Haemophilus influenzae (HI0442), a protein of unknown function coexpressed with the recombinational DNA repair protein RecR
    • Lim, K., Tempczyk, A., Parsons, J.F., Bonander, N., Toedt, J., Kelman, Z., et al. (2003) Crystal structure of YbaB from Haemophilus influenzae (HI0442), a protein of unknown function coexpressed with the recombinational DNA repair protein RecR. Proteins 50: 375-379.
    • (2003) Proteins , vol.50 , pp. 375-379
    • Lim, K.1    Tempczyk, A.2    Parsons, J.F.3    Bonander, N.4    Toedt, J.5    Kelman, Z.6
  • 19
    • 0038392868 scopus 로고    scopus 로고
    • RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: A universal step of recombinational repair
    • Morimatsu, K., and Kowalczykowski, S.C. (2003) RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: a universal step of recombinational repair. Mol Cell 11: 1337-1347.
    • (2003) Mol Cell , vol.11 , pp. 1337-1347
    • Morimatsu, K.1    Kowalczykowski, S.C.2
  • 20
    • 1242318677 scopus 로고    scopus 로고
    • Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress
    • Mostertz, J., Scharf, C., Hecker, M., and Homuth, G. (2004) Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress. Microbiology 150: 497-512.
    • (2004) Microbiology , vol.150 , pp. 497-512
    • Mostertz, J.1    Scharf, C.2    Hecker, M.3    Homuth, G.4
  • 22
    • 0034888480 scopus 로고    scopus 로고
    • Structural and functional characterization of the recR gene of Streptomyces
    • Pelaez, A.I., Ribas-Aparicio, R.M., Gomez, A., and Rodicio, M.R. (2001) Structural and functional characterization of the recR gene of Streptomyces. Mol Genet Genomics 265: 663-672.
    • (2001) Mol Genet Genomics , vol.265 , pp. 663-672
    • Pelaez, A.I.1    Ribas-Aparicio, R.M.2    Gomez, A.3    Rodicio, M.R.4
  • 23
    • 0141532928 scopus 로고    scopus 로고
    • DNA array analysis of gene expression in response to UV irradiation in Escherichia coli
    • Quillardet, P., Rouffaud, M.A., and Bouige, P. (2003) DNA array analysis of gene expression in response to UV irradiation in Escherichia coli. Res Microbiol 154: 559-572.
    • (2003) Res Microbiol , vol.154 , pp. 559-572
    • Quillardet, P.1    Rouffaud, M.A.2    Bouige, P.3
  • 24
    • 0032035329 scopus 로고    scopus 로고
    • Positive activation of gene expression
    • Rhodius, V.A., and Busby, S.J. (1998) Positive activation of gene expression. Curr Opin Microbiol 1: 152-159.
    • (1998) Curr Opin Microbiol , vol.1 , pp. 152-159
    • Rhodius, V.A.1    Busby, S.J.2
  • 26
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • Schäfer, A., Tauch, A., Jäger, W., Kalinowski, J., Thierbach, G., and Pühler, A. (1994) Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145: 69-73.
    • (1994) Gene , vol.145 , pp. 69-73
    • Schäfer, A.1    Tauch, A.2    Jäger, W.3    Kalinowski, J.4    Thierbach, G.5    Pühler, A.6
  • 27
    • 0035689950 scopus 로고    scopus 로고
    • A high-resolution reference map for cytoplasmic and membrane-associated proteins of Corynebacterium glutamicum
    • Schaffer, S., Weil, B., Nguyen, V.D., Dongmann, G., Günther, K., Nickolaus, M., et al. (2001) A high-resolution reference map for cytoplasmic and membrane-associated proteins of Corynebacterium glutamicum. Electrophoresis 22: 4404-4422.
    • (2001) Electrophoresis , vol.22 , pp. 4404-4422
    • Schaffer, S.1    Weil, B.2    Nguyen, V.D.3    Dongmann, G.4    Günther, K.5    Nickolaus, M.6
  • 28
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 29
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger, H., and von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Biochem 199: 223-231.
    • (1991) Anal Biochem , vol.199 , pp. 223-231
    • Schägger, H.1    Von Jagow, G.2
  • 30
    • 0033814033 scopus 로고    scopus 로고
    • Use of the Strep-Tag and streptavidin for detection and purification of recombinant proteins
    • Skerra, A., and Schmidt, T.G. (2000) Use of the Strep-Tag and streptavidin for detection and purification of recombinant proteins. Methods Enzymol 326: 271-304.
    • (2000) Methods Enzymol , vol.326 , pp. 271-304
    • Skerra, A.1    Schmidt, T.G.2
  • 31
    • 4744362881 scopus 로고    scopus 로고
    • Regulation of GlnK activity: Modification, membrane sequestration and proteolysis as regulatory principles in the network of nitrogen control in Corynebacterium glutamicum
    • Strösser, J., Lüdke, A., Schaffer, S., Krämer, R., Burkovski, A. (2004) Regulation of GlnK activity: modification, membrane sequestration and proteolysis as regulatory principles in the network of nitrogen control in Corynebacterium glutamicum. Mol Microbiol 54: 132-147.
    • (2004) Mol Microbiol , vol.54 , pp. 132-147
    • Strösser, J.1    Lüdke, A.2    Schaffer, S.3    Krämer, R.4    Burkovski, A.5
  • 32
    • 0001590871 scopus 로고    scopus 로고
    • The SPFH domain: Implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins
    • Tavernarakis, N., Driscoll, M., Kyrpides, N.C. (1999) The SPFH domain: implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins. Trends Biochem Sci 24: 425-427.
    • (1999) Trends Biochem Sci , vol.24 , pp. 425-427
    • Tavernarakis, N.1    Driscoll, M.2    Kyrpides, N.C.3
  • 33
    • 0035029482 scopus 로고    scopus 로고
    • Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol
    • Tomoyasu, T., Mogk, A., Langen, H., Goloubinoff, P., and Bukau, B. (2001) Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol Microbiol 40: 397-413.
    • (2001) Mol Microbiol , vol.40 , pp. 397-413
    • Tomoyasu, T.1    Mogk, A.2    Langen, H.3    Goloubinoff, P.4    Bukau, B.5


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