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Volumn 54, Issue 1, 2004, Pages 132-147

Regulation of GlnK activity: Modification, membrane sequestration and proteolysis as regulatory principles in the network of nitrogen control in Corynebacterium glutamicum

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; ENOLASE; GLUTAMATE AMMONIA LIGASE; METHYLAMMONIUM; NITROGEN; PROTEIN AMTB; PROTEIN CLPCP; PROTEIN CLPXP; PROTEIN FTSH; PROTEIN GLND; PROTEIN GLNK; PROTEINASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG;

EID: 4744362881     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2004.04247.x     Document Type: Article
Times cited : (87)

References (47)
  • 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 Microbiol 13: 279-301.
    • (1967) J Gen Microbiol , vol.13 , pp. 279-301
    • Abe, S.1    Takayama, K.2    Kinoshita, S.3
  • 2
    • 0016718064 scopus 로고
    • II regulatory protein and the uridylyltransferase- uridylylremoving enzyme
    • II regulatory protein and the uridylyltransferase-uridylylremoving enzyme. J Biol Chem 250: 6264-6272.
    • (1975) J Biol Chem , vol.250 , pp. 6264-6272
    • Adler, S.P.1    Purich, D.2    Stadtman, E.R.3
  • 4
    • 0035159923 scopus 로고    scopus 로고
    • Glutamate synthase of Corynebacterium glutamicum is not essential for glutamate synthesis and is regulated by the nitrogen status
    • Beckers, G., Nolden, L., and Burkovski, A. (2001) Glutamate synthase of Corynebacterium glutamicum is not essential for glutamate synthesis and is regulated by the nitrogen status. Microbiology 147: 2961-2970.
    • (2001) Microbiology , vol.147 , pp. 2961-2970
    • Beckers, G.1    Nolden, L.2    Burkovski, A.3
  • 5
    • 0033770817 scopus 로고    scopus 로고
    • Control of methionine biosynthesis in Escherichia coli by proteolysis
    • Biran, D., Gur, E., Gollan, L., and Ron, E.Z. (2000) Control of methionine biosynthesis in Escherichia coli by proteolysis. Mol Microbiol 37: 1436-1443.
    • (2000) Mol Microbiol , vol.37 , pp. 1436-1443
    • Biran, D.1    Gur, E.2    Gollan, L.3    Ron, E.Z.4
  • 6
    • 0037678786 scopus 로고    scopus 로고
    • Antagonism of PII signalling by the AmtB protein of Escherichia coli
    • Blauwkamp, T.A., and Ninfa, A.J. (2003) Antagonism of PII signalling by the AmtB protein of Escherichia coli. Mol Microbiol 48: 1017-1028.
    • (2003) Mol Microbiol , vol.48 , pp. 1017-1028
    • Blauwkamp, T.A.1    Ninfa, A.J.2
  • 7
    • 0026564643 scopus 로고
    • Molecular analysis of the Corynebacterium glutamicum gdh gene encoding glutamate dehydrogenase
    • Börmann, E.R., Eikmanns, B.J., and Sahm, H. (1992) Molecular analysis of the Corynebacterium glutamicum gdh gene encoding glutamate dehydrogenase. Mol Microbiol 6:317-326.
    • (1992) Mol Microbiol , vol.6 , pp. 317-326
    • Börmann, E.R.1    Eikmanns, B.J.2    Sahm, H.3
  • 8
    • 0037283417 scopus 로고    scopus 로고
    • I do it my way: Regulation of ammonium uptake and ammonium assimilation in Corynebacterium glutamicum
    • Burkovski, A. (2003a) I do it my way: regulation of ammonium uptake and ammonium assimilation in Corynebacterium glutamicum. Arch Microbiol 179: 83-88.
    • (2003) Arch Microbiol , vol.179 , pp. 83-88
    • Burkovski, A.1
  • 9
    • 0345447496 scopus 로고    scopus 로고
    • Ammonium assimilation and nitrogen control in Corynebacterium glutamicum and its relatives: An example for new regulatory mechanisms in actinomycetes
    • Burkovski, A. (2003b) Ammonium assimilation and nitrogen control in Corynebacterium glutamicum and its relatives: an example for new regulatory mechanisms in actinomycetes. FEMS Microbiol Rev 27: 617-628.
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 617-628
    • Burkovski, A.1
  • 10
    • 0037083882 scopus 로고    scopus 로고
    • Membrane sequestration of the signal transduction protein GlnK by the ammonium transporter AmtB
    • Coutts, G., Thomas, G., Blakey, D., and Merrick, M. (2002) Membrane sequestration of the signal transduction protein GlnK by the ammonium transporter AmtB. EMBO J 21: 536-545.
    • (2002) EMBO J , vol.21 , pp. 536-545
    • Coutts, G.1    Thomas, G.2    Blakey, D.3    Merrick, M.4
  • 11
    • 0025052104 scopus 로고
    • Cloning the dapA dapB cluster of the lysine-secreting bacterium Corynebacterium glutamicum
    • Cremer, J., Eggeling, L., and Sahm, H. (1990) Cloning 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
  • 12
    • 0032169271 scopus 로고    scopus 로고
    • Conservation of gene order: A fingerprint of proteins that physically interact
    • Dandekar, T., Snel, B., Huynen, M., and Bork, P. (1998) Conservation of gene order: a fingerprint of proteins that physically interact. Trends Biochem Sci 23: 324-328.
    • (1998) Trends Biochem Sci , vol.23 , pp. 324-328
    • Dandekar, T.1    Snel, B.2    Huynen, M.3    Bork, P.4
  • 13
    • 0344875060 scopus 로고    scopus 로고
    • Ammonium utilization in Bacillus subtilis: Transport and regulatory functions of NrgA and NrgB
    • Detsch, C., and Stülke, J. (2003) Ammonium utilization in Bacillus subtilis: transport and regulatory functions of NrgA and NrgB. Microbiology 140: 3289-3297.
    • (2003) Microbiology , vol.140 , pp. 3289-3297
    • Detsch, C.1    Stülke, J.2
  • 15
    • 0032950276 scopus 로고    scopus 로고
    • Regulation of nitrogen metabolism in Bacillus subtilis: Vive la différence!
    • Fisher, S.H. (1999) Regulation of nitrogen metabolism in Bacillus subtilis: vive la différence! Mol Microbiol 32: 223-232.
    • (1999) Mol Microbiol , vol.32 , pp. 223-232
    • Fisher, S.H.1
  • 16
    • 0033118230 scopus 로고    scopus 로고
    • Regulation by proteolysis: Developmental switches
    • Gottesman, S. (1999) Regulation by proteolysis: developmental switches. Curr Opin Microbiol 2: 142-147.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 142-147
    • Gottesman, S.1
  • 17
    • 0025295967 scopus 로고
    • Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants
    • Grant, S.N.G., Jessee, J., Bloom, F.R., and Hanahan, D. (1990) Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants. Proc Natl Acad Sci USA 87: 4645-4649.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4645-4649
    • Grant, S.N.G.1    Jessee, J.2    Bloom, F.R.3    Hanahan, D.4
  • 18
    • 0032429448 scopus 로고    scopus 로고
    • Mapping and identification of Corynebacterium glutamicum proteins by two-dimensional gel electrophoresis and microsequencing
    • Hermann, T., Wersch, G., Uhlemann, E.-M., Schmid, R., and Burkovski, A. (1998) Mapping and identification of Corynebacterium glutamicum proteins by two-dimensional gel electrophoresis and microsequencing. Electrophoresis 19: 3217-3221.
    • (1998) Electrophoresis , vol.19 , pp. 3217-3221
    • Hermann, T.1    Wersch, G.2    Uhlemann, E.-M.3    Schmid, R.4    Burkovski, A.5
  • 19
    • 0033995823 scopus 로고    scopus 로고
    • Two-dimensional electrophoretic analysis of Corynebacterium glutamicum membrane fraction and surface proteins
    • Hermann, T., Finkemeier, M., Pfefferle, W., Wersch, G., Krämer, R., and Burkovski, A. (2000) Two-dimensional electrophoretic analysis of Corynebacterium glutamicum membrane fraction and surface proteins. Electrophoresis 21: 654-659.
    • (2000) Electrophoresis , vol.21 , pp. 654-659
    • Hermann, T.1    Finkemeier, M.2    Pfefferle, W.3    Wersch, G.4    Krämer, R.5    Burkovski, A.6
  • 21
    • 0036430005 scopus 로고    scopus 로고
    • The GlnD and GlnK homologues of Streptomyces coelicolor A3(2) are functionally dissimilar to their nitrogen regulatory system counterparts from enteric bacteria
    • Hesketh, A., Fink, D., Gust, B., Rexer, H.-U., Scheel, B., Chater, K., et al. (2002) The GlnD and GlnK homologues of Streptomyces coelicolor A3(2) are functionally dissimilar to their nitrogen regulatory system counterparts from enteric bacteria. Mol Microbiol 48: 319-330.
    • (2002) Mol Microbiol , vol.48 , pp. 319-330
    • Hesketh, A.1    Fink, D.2    Gust, B.3    Rexer, H.-U.4    Scheel, B.5    Chater, K.6
  • 22
    • 0030884625 scopus 로고    scopus 로고
    • Isolation of the Corynebacterium glutamicum glnA gene encoding glutamine synthetase I
    • Jakoby, M., Tesch, M., Sahm, H., Krämer, R., and Burkovski, A. (1997) Isolation of the Corynebacterium glutamicum glnA gene encoding glutamine synthetase I. FEMS Microbiol Lett 154: 81-88.
    • (1997) FEMS Microbiol Lett , vol.154 , pp. 81-88
    • Jakoby, M.1    Tesch, M.2    Sahm, H.3    Krämer, R.4    Burkovski, A.5
  • 23
    • 0345129980 scopus 로고    scopus 로고
    • Nitrogen regulation in Corynebacterium glutamicum: Isolation of genes involved and biochemical characterization of corresponding proteins
    • Jakoby, M., Krämer, R., and Burkovski, A. (1999) Nitrogen regulation in Corynebacterium glutamicum: isolation of genes involved and biochemical characterization of corresponding proteins. FEMS Microbiol Lett 173: 303-310.
    • (1999) FEMS Microbiol Lett , vol.173 , pp. 303-310
    • Jakoby, M.1    Krämer, R.2    Burkovski, A.3
  • 24
    • 0033865395 scopus 로고    scopus 로고
    • AmtR, a global repressor in the nitrogen regulation system of Corynebacterium glutamicum
    • Jakoby, M., Nolden, L., Meier-Wagner, J., Krämer, R., and Burkovski, A. (2000) AmtR, a global repressor in the nitrogen regulation system of Corynebacterium glutamicum. Mol Microbiol 37: 964-977.
    • (2000) Mol Microbiol , vol.37 , pp. 964-977
    • Jakoby, M.1    Nolden, L.2    Meier-Wagner, J.3    Krämer, R.4    Burkovski, A.5
  • 25
    • 1542275558 scopus 로고    scopus 로고
    • Ammonium sensing in E. coli: The role of the ammonium transporter AmtB and AmtB-GlnK complex formation
    • Javelle, A., Seven, E., Thornton, J., and Merrick, M. (2004) Ammonium sensing in E. coli: the role of the ammonium transporter AmtB and AmtB-GlnK complex formation. J Biol Chem 279: 8530-8538.
    • (2004) J Biol Chem , vol.279 , pp. 8530-8538
    • Javelle, A.1    Seven, E.2    Thornton, J.3    Merrick, M.4
  • 26
    • 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
  • 27
    • 0030613795 scopus 로고    scopus 로고
    • Synergistic roles of HsIVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli
    • Kanemori, M., Nishihara, K., Yanagi, H., and Yura, T. (1997) Synergistic roles of HsIVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli. J Bacteriol 179: 7219-7225.
    • (1997) J Bacteriol , vol.179 , pp. 7219-7225
    • Kanemori, M.1    Nishihara, K.2    Yanagi, H.3    Yura, T.4
  • 28
    • 0027164654 scopus 로고
    • Isoleucine synthesis in Corynebacterium glutamicum: Molecular analysis of the ilvB-ilvN-ilvC operon
    • Keilhauer, C., Eggeling, L., and Sahm, H. (1993) Isoleucine synthesis in Corynebacterium glutamicum: molecular analysis of the ilvB-ilvN-ilvC operon. J Bacteriol 175: 5595-5603.
    • (1993) J Bacteriol , vol.175 , pp. 5595-5603
    • Keilhauer, C.1    Eggeling, L.2    Sahm, H.3
  • 29
    • 0028944577 scopus 로고
    • Structure of the gluABCD cluster encoding the glutamate uptake system of Corynebacterium glutamicum
    • Kronemeyer, W., Peekhaus, N., Krämer, R., Sahm, H., and Eggeling, L. (1995) Structure of the gluABCD cluster encoding the glutamate uptake system of Corynebacterium glutamicum. J Bacteriol 177: 1152-1158.
    • (1995) J Bacteriol , vol.177 , pp. 1152-1158
    • Kronemeyer, W.1    Peekhaus, N.2    Krämer, R.3    Sahm, H.4    Eggeling, L.5
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0035154822 scopus 로고    scopus 로고
    • Multiplicity of ammonium uptake systems in Corynebacterium glutamicum: Role of Amt and AmtB
    • Meier-Wagner, J., Nolden, L., Jakoby, M., Siewe, R., Krämer, R., and Burkovski, A. (2001) Multiplicity of ammonium uptake systems in Corynebacterium glutamicum: role of Amt and AmtB. Microbiology 147: 135-143.
    • (2001) Microbiology , vol.147 , pp. 135-143
    • Meier-Wagner, J.1    Nolden, L.2    Jakoby, M.3    Siewe, R.4    Krämer, R.5    Burkovski, A.6
  • 32
    • 0035041240 scopus 로고    scopus 로고
    • Molecular analysis of the cytochrome bc1-aa3 branch of the Corynebacterium glutamicum respiratory chain containing an unusual diheme cytochrome c1
    • Niebisch, A., and Bott, M. (2001) Molecular analysis of the cytochrome bc1-aa3 branch of the Corynebacterium glutamicum respiratory chain containing an unusual diheme cytochrome c1. Arch Microbiol 175: 282-294.
    • (2001) Arch Microbiol , vol.175 , pp. 282-294
    • Niebisch, A.1    Bott, M.2
  • 33
    • 0035838555 scopus 로고    scopus 로고
    • Glutamine synthetases in Corynebacterium glutamicum: Transcriptional control and regulation of activity
    • Nolden, L., Farwick, M., Krämer, R., and Burkovski, A. (2001a) Glutamine synthetases in Corynebacterium glutamicum: transcriptional control and regulation of activity. FEMS Microbiol Lett 201: 91-98.
    • (2001) FEMS Microbiol Lett , vol.201 , pp. 91-98
    • Nolden, L.1    Farwick, M.2    Krämer, R.3    Burkovski, A.4
  • 34
    • 0035726152 scopus 로고    scopus 로고
    • Sensing nitrogen limitation in Corynebacterium glutamicum: The role of glnK and glnd
    • Nolden, L., Ngouoto-Nkili, C.-E., Bendt, A.K., Krämer, R., and Burkovski, A. (2001b) Sensing nitrogen limitation in Corynebacterium glutamicum: the role of glnK and glnd. Mol Microbiol 42: 1281-1295.
    • (2001) Mol Microbiol , vol.42 , pp. 1281-1295
    • Nolden, L.1    Ngouoto-Nkili, C.-E.2    Bendt, A.K.3    Krämer, R.4    Burkovski, A.5
  • 35
    • 0037022970 scopus 로고    scopus 로고
    • Nitrogen assimilation in Corynebacterium diphtheriae: Pathways and regulatory cascades
    • Nolden, L., Beckers, G., and Burkovski, A. (2002) Nitrogen assimilation in Corynebacterium diphtheriae: pathways and regulatory cascades. FEMS Microbiol Lett 208: 287-293.
    • (2002) FEMS Microbiol Lett , vol.208 , pp. 287-293
    • Nolden, L.1    Beckers, G.2    Burkovski, A.3
  • 36
    • 1642369829 scopus 로고    scopus 로고
    • ClpA and ClpX ATPases bind simultaneously to opposite ends of ClpP peptidase to form active hybrid complexes
    • Ortega, J., Lee, H.S., Maurizi, M.R., and Steven, A.C. (2004) ClpA and ClpX ATPases bind simultaneously to opposite ends of ClpP peptidase to form active hybrid complexes. J Struct Biol 146: 217-226.
    • (2004) J Struct Biol , vol.146 , pp. 217-226
    • Ortega, J.1    Lee, H.S.2    Maurizi, M.R.3    Steven, A.C.4
  • 38
    • 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
  • 39
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • Schaffner, W., and Weissmann, C. (1973) A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal Biochem 52: 502-514.
    • (1973) Anal Biochem , vol.52 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2
  • 40
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 10O 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 10O kDa. Anal Biochem 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 41
    • 0029989297 scopus 로고    scopus 로고
    • Functional and genetic characterization of the (methyl) ammonium uptake carrier of Corynebacterium glutamicum
    • Siewe, R.M., Weil, B., Burkovski, A., Eikmanns, B.J., Eikmanns, M., and Krämer, R. (1996) Functional and genetic characterization of the (methyl) ammonium uptake carrier of Corynebacterium glutamicum. J Biol Chem 271: 5398-5403.
    • (1996) J Biol Chem , vol.271 , pp. 5398-5403
    • Siewe, R.M.1    Weil, B.2    Burkovski, A.3    Eikmanns, B.J.4    Eikmanns, M.5    Krämer, R.6
  • 43
    • 0025288731 scopus 로고
    • Quantitative analysis of Tn10 Tet repressor binding to a complete set of tet operator mutants
    • Sizemore, C., Wissmann, A., Gulland, U., and Hillen, W. (1990) Quantitative analysis of Tn10 Tet repressor binding to a complete set of tet operator mutants. Nucleic Acids Res 18: 2875-2880.
    • (1990) Nucleic Acids Res , vol.18 , pp. 2875-2880
    • Sizemore, C.1    Wissmann, A.2    Gulland, U.3    Hillen, W.4
  • 45
    • 0037294258 scopus 로고    scopus 로고
    • GltS, the sodium-coupled L-glutamate uptake system of Corynebacterium glutamicum: Identification of the corresponding gene and impact on L-glutamate production
    • Trötschel, C., Kandirali, S., Diaz-Achirica, P., Meinhardt, A., Morbach, S., Krämer, R., and Burkovski, A. (2003) GltS, the sodium-coupled L-glutamate uptake system of Corynebacterium glutamicum: identification of the corresponding gene and impact on L-glutamate production. Appl Microbiol Biotechnol 60: 738-742.
    • (2003) Appl Microbiol Biotechnol , vol.60 , pp. 738-742
    • Trötschel, C.1    Kandirali, S.2    Diaz-Achirica, P.3    Meinhardt, A.4    Morbach, S.5    Krämer, R.6    Burkovski, A.7
  • 46
    • 0037216549 scopus 로고    scopus 로고
    • Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coil
    • Weichart, D., Querfurth, N., Dreger, M., and Hengge-Aronis, R. (2003) Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coil. J Bacteriol 185: 115-125.
    • (2003) J Bacteriol , vol.185 , pp. 115-125
    • Weichart, D.1    Querfurth, N.2    Dreger, M.3    Hengge-Aronis, R.4
  • 47
    • 0025995751 scopus 로고
    • Selection for Tn10 tet repressor binding to tet operator in Escherichia coli: Isolation of temperature-sensitive mutants and combinatorial mutagenesis in the DNA binding motif
    • Wissmann, A., Wray, L.V., Jr, Somaggio, U., Baumeister, R., Geissendorfer, M., and Hillen, W. (1991) Selection for Tn10 tet repressor binding to tet operator in Escherichia coli: isolation of temperature-sensitive mutants and combinatorial mutagenesis in the DNA binding motif. Genetics 128: 225-232.
    • (1991) Genetics , vol.128 , pp. 225-232
    • Wissmann, A.1    Wray Jr., L.V.2    Somaggio, U.3    Baumeister, R.4    Geissendorfer, M.5    Hillen, W.6


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