메뉴 건너뛰기




Volumn 85, Issue 2, 2012, Pages 213-224

Control of glutamate homeostasis in Bacillus subtilis: A complex interplay between ammonium assimilation, glutamate biosynthesis and degradation

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; CARBON; CHAPERONE; DNA; GLUTAMATE AMMONIA LIGASE; GLUTAMATE DEHYDROGENASE; GLUTAMATE SYNTHASE; GLUTAMIC ACID; NITROGEN; TRANSCRIPTION FACTOR;

EID: 84863594395     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2012.08105.x     Document Type: Review
Times cited : (136)

References (108)
  • 1
    • 0035105144 scopus 로고    scopus 로고
    • II signal transduction proteins, pivotal players in microbial nitrogen control
    • II signal transduction proteins, pivotal players in microbial nitrogen control. Microbiol Mol Biol Rev 65: 80-105.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 80-105
    • Arcondéguy, T.1    Jack, R.2    Merrick, M.3
  • 2
    • 0026067217 scopus 로고
    • Identification of genes and gene products whose expression is activated during nitrogen-limited growth in Bacillus subtilis
    • Atkinson, M.R., and Fisher, S.H. (1991) Identification of genes and gene products whose expression is activated during nitrogen-limited growth in Bacillus subtilis. J Bacteriol 173: 23-27.
    • (1991) J Bacteriol , vol.173 , pp. 23-27
    • Atkinson, M.R.1    Fisher, S.H.2
  • 3
    • 0029939231 scopus 로고    scopus 로고
    • The Mfd protein of Bacillus subtilis 168 is involved in both transcription-coupled DNA repair and DNA recombination
    • Ayora, S., Rojo, F., Ogasawara, N., Nakai, S., and Alonso, J.C. (1996) The Mfd protein of Bacillus subtilis 168 is involved in both transcription-coupled DNA repair and DNA recombination. J Mol Biol 256: 301-318.
    • (1996) J Mol Biol , vol.256 , pp. 301-318
    • Ayora, S.1    Rojo, F.2    Ogasawara, N.3    Nakai, S.4    Alonso, J.C.5
  • 4
    • 0036035079 scopus 로고    scopus 로고
    • Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon
    • Baichoo, N., Wang, T., Ye, R., and Helmann, J.D. (2002) Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon. Mol Microbiol 45: 1613-1629.
    • (2002) Mol Microbiol , vol.45 , pp. 1613-1629
    • Baichoo, N.1    Wang, T.2    Ye, R.3    Helmann, J.D.4
  • 5
    • 0029620995 scopus 로고
    • Mutations in GltC that increase Bacillus subtilis gltA expression
    • Belitsky, B.R., and Sonenshein, A.L. (1995) Mutations in GltC that increase Bacillus subtilis gltA expression. J Bacteriol 177: 5696-5700.
    • (1995) J Bacteriol , vol.177 , pp. 5696-5700
    • Belitsky, B.R.1    Sonenshein, A.L.2
  • 6
    • 0031756184 scopus 로고    scopus 로고
    • Role and regulation of Bacillus subtilis glutamate dehydrogenase genes
    • Belitsky, B.R., and Sonenshein, A.L. (1998) Role and regulation of Bacillus subtilis glutamate dehydrogenase genes. J Bacteriol 180: 6298-6305.
    • (1998) J Bacteriol , vol.180 , pp. 6298-6305
    • Belitsky, B.R.1    Sonenshein, A.L.2
  • 7
    • 0033621091 scopus 로고    scopus 로고
    • An enhancer element located downstream of the major glutamate dehydrogenase gene of Bacillus subtilis
    • Belitsky, B.R., and Sonenshein, A.L. (1999) An enhancer element located downstream of the major glutamate dehydrogenase gene of Bacillus subtilis. Proc Natl Acad Sci USA 96: 10290-10295.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10290-10295
    • Belitsky, B.R.1    Sonenshein, A.L.2
  • 8
    • 2442649038 scopus 로고    scopus 로고
    • Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase
    • Belitsky, B.R., and Sonenshein, A.L. (2004) Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase. J Bacteriol 186: 3399-3407.
    • (2004) J Bacteriol , vol.186 , pp. 3399-3407
    • Belitsky, B.R.1    Sonenshein, A.L.2
  • 9
    • 0029412081 scopus 로고
    • Sites required for GltC-dependent regulation of Bacillus subtilis glutamate synthase expression
    • Belitsky, B.R., Janssen, P.J., and Sonenshein, A.L. (1995) Sites required for GltC-dependent regulation of Bacillus subtilis glutamate synthase expression. J Bacteriol 177: 5686-5695.
    • (1995) J Bacteriol , vol.177 , pp. 5686-5695
    • Belitsky, B.R.1    Janssen, P.J.2    Sonenshein, A.L.3
  • 10
    • 0033758755 scopus 로고    scopus 로고
    • Role of TnrA in nitrogen source-dependent repression of Bacillus subtilis glutamate synthase gene expression
    • Belitsky, B.R., Wray, L.V., Jr, Fisher, S.H., Bohannon, D.F., and Sonenshein, A.L. (2000) Role of TnrA in nitrogen source-dependent repression of Bacillus subtilis glutamate synthase gene expression. J Bacteriol 182: 5939-5947.
    • (2000) J Bacteriol , vol.182 , pp. 5939-5947
    • Belitsky, B.R.1    Wray Jr., L.V.2    Fisher, S.H.3    Bohannon, D.F.4    Sonenshein, A.L.5
  • 11
    • 2442669092 scopus 로고    scopus 로고
    • CcpA-dependent regulation of Bacillus subtilis glutamate dehydrogenase gene expression
    • Belitsky, B.R., Kim, H.-J., and Sonenshein, A.L. (2004) CcpA-dependent regulation of Bacillus subtilis glutamate dehydrogenase gene expression. J Bacteriol 186: 3392-3398.
    • (2004) J Bacteriol , vol.186 , pp. 3392-3398
    • Belitsky, B.R.1    Kim, H.-J.2    Sonenshein, A.L.3
  • 12
    • 68049100110 scopus 로고    scopus 로고
    • Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli
    • Bennett, B.D., Kimball, E.H., Gao, M., Osterhout, R., Van Dien, S.J., and Rabinowitz, J.D. (2009) Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli. Nat Chem Biol 5: 593-599.
    • (2009) Nat Chem Biol , vol.5 , pp. 593-599
    • Bennett, B.D.1    Kimball, E.H.2    Gao, M.3    Osterhout, R.4    Van Dien, S.J.5    Rabinowitz, J.D.6
  • 13
    • 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
  • 15
    • 0036838142 scopus 로고    scopus 로고
    • Roles of PucR, GlnR, and TnrA in regulating expression of the Bacillus subtilis ure P3 promoter
    • Brandenburg, J.L., Wray, L.V., Jr, Beier, L., Jarmer, H., Saxild, H.H., and Fisher, S.H. (2002) Roles of PucR, GlnR, and TnrA in regulating expression of the Bacillus subtilis ure P3 promoter. J Bacteriol 184: 6060-6064.
    • (2002) J Bacteriol , vol.184 , pp. 6060-6064
    • Brandenburg, J.L.1    Wray Jr., L.V.2    Beier, L.3    Jarmer, H.4    Saxild, H.H.5    Fisher, S.H.6
  • 16
    • 80053613797 scopus 로고    scopus 로고
    • Osmotically controlled synthesis of the compatible solute proline is critical for cellular defense of Bacillus subtilis against high osmolarity
    • Brill, J., Hoffmann, T., Bleisteiner, M., and Bremer, E. (2011) Osmotically controlled synthesis of the compatible solute proline is critical for cellular defense of Bacillus subtilis against high osmolarity. J Bacteriol 193: 5334-5346.
    • (2011) J Bacteriol , vol.193 , pp. 5334-5346
    • Brill, J.1    Hoffmann, T.2    Bleisteiner, M.3    Bremer, E.4
  • 18
    • 0029882155 scopus 로고    scopus 로고
    • Autogenous regulation of the Bacillus subtilis glnRA operon
    • Brown, S.W., and Sonenshein, A.L. (1996) Autogenous regulation of the Bacillus subtilis glnRA operon. J Bacteriol 178: 2450-2454.
    • (1996) J Bacteriol , vol.178 , pp. 2450-2454
    • Brown, S.W.1    Sonenshein, A.L.2
  • 19
    • 77950571124 scopus 로고    scopus 로고
    • Role of GlnR in acid-mediated repression of genes encoding proteins involved in glutamine and glutamate metabolism in Streptococcus mutans
    • Chen, P.M., Chen, Y.Y.M., Yu, S.L., Sher, S., Lai, C.H., and Chia, J.S. (2010) Role of GlnR in acid-mediated repression of genes encoding proteins involved in glutamine and glutamate metabolism in Streptococcus mutans. Appl Environ Microbiol 76: 2478-2486.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 2478-2486
    • Chen, P.M.1    Chen, Y.Y.M.2    Yu, S.L.3    Sher, S.4    Lai, C.H.5    Chia, J.S.6
  • 20
    • 25144520372 scopus 로고    scopus 로고
    • Regulation of sigL expression by the catabolite control protein CcpA involves roadblock mechanism in Bacillus subtilis: potential connection between carbon and nitrogen metabolism
    • Choi, S.K., and Saier, M.H., Jr (2005) Regulation of sigL expression by the catabolite control protein CcpA involves roadblock mechanism in Bacillus subtilis: potential connection between carbon and nitrogen metabolism. J Bacteriol 187: 6856-6861.
    • (2005) J Bacteriol , vol.187 , pp. 6856-6861
    • Choi, S.K.1    Saier Jr., M.H.2
  • 21
    • 38449095243 scopus 로고    scopus 로고
    • Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression
    • Commichau, F.M., and Stülke, J. (2008) Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression. Mol Microbiol 67: 692-702.
    • (2008) Mol Microbiol , vol.67 , pp. 692-702
    • Commichau, F.M.1    Stülke, J.2
  • 22
    • 33645878600 scopus 로고    scopus 로고
    • Regulatory links between carbon and nitrogen metabolism
    • Commichau, F.M., Forchhammer, K., and Stülke, J. (2006) Regulatory links between carbon and nitrogen metabolism. Curr Opin Microbiol 9: 167-172.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 167-172
    • Commichau, F.M.1    Forchhammer, K.2    Stülke, J.3
  • 23
    • 34447569343 scopus 로고    scopus 로고
    • A regulatory protein-protein interaction governs glutamate biosynthesis in Bacillus subtilis: the glutamate dehydrogenase RocG moonlights in controlling the transcription factor GltC
    • Commichau, F.M., Herzberg, C., Tripal, P., Valerius, O., and Stülke, J. (2007a) A regulatory protein-protein interaction governs glutamate biosynthesis in Bacillus subtilis: the glutamate dehydrogenase RocG moonlights in controlling the transcription factor GltC. Mol Microbiol 65: 642-654.
    • (2007) Mol Microbiol , vol.65 , pp. 642-654
    • Commichau, F.M.1    Herzberg, C.2    Tripal, P.3    Valerius, O.4    Stülke, J.5
  • 25
    • 47049089928 scopus 로고    scopus 로고
    • Glutamate metabolism in Bacillus subtilis: gene expression and enzyme activities evolved to avoid futile cycles and to allow rapid responses to perturbations of the system
    • Commichau, F.M., Gunka, K., Landmann, J.J., and Stülke, J. (2008) Glutamate metabolism in Bacillus subtilis: gene expression and enzyme activities evolved to avoid futile cycles and to allow rapid responses to perturbations of the system. J Bacteriol 190: 3557-3564.
    • (2008) J Bacteriol , vol.190 , pp. 3557-3564
    • Commichau, F.M.1    Gunka, K.2    Landmann, J.J.3    Stülke, J.4
  • 26
    • 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
  • 27
    • 0027993191 scopus 로고
    • The accumulation of glutamate is necessary for optimal growth of Salmonella typhimurium in media of high osmolality but not induction of the proU operon
    • Csonka, L.N., Ikeda, T.P., Fletcher, S.A., and Kustu, S. (1994) The accumulation of glutamate is necessary for optimal growth of Salmonella typhimurium in media of high osmolality but not induction of the proU operon. J Bacteriol 176: 6324-6333.
    • (1994) J Bacteriol , vol.176 , pp. 6324-6333
    • Csonka, L.N.1    Ikeda, T.P.2    Fletcher, S.A.3    Kustu, S.4
  • 29
    • 0018873069 scopus 로고
    • Glutamate synthase from Bacillus subtilis: in vitro reconstitution of an active amidotransferase
    • Deshpande, K.L., and Kane, J.F. (1980) Glutamate synthase from Bacillus subtilis: in vitro reconstitution of an active amidotransferase. Biochem Biophys Res Commun 93: 308-314.
    • (1980) Biochem Biophys Res Commun , vol.93 , pp. 308-314
    • Deshpande, K.L.1    Kane, J.F.2
  • 30
    • 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 149: 3289-3297.
    • (2003) Microbiology , vol.149 , pp. 3289-3297
    • Detsch, C.1    Stülke, J.2
  • 31
    • 0015980222 scopus 로고
    • Regulation of glutamine synthetase from Bacillus subtilis by divalent cations, feedback inhibitors, and L-glutamine
    • Deuel, T.F., and Prusiner, S. (1974) Regulation of glutamine synthetase from Bacillus subtilis by divalent cations, feedback inhibitors, and L-glutamine. J Biol Chem 249: 257-264.
    • (1974) J Biol Chem , vol.249 , pp. 257-264
    • Deuel, T.F.1    Prusiner, S.2
  • 32
    • 0014962857 scopus 로고
    • Bacillus subtilis glutamine synthetase: purification and physical characterization
    • Deuel, T.F., Ginsberg, A., Yeh, J., Shelton, E., and Stadtman, E.R. (1970) Bacillus subtilis glutamine synthetase: purification and physical characterization. J Biol Chem 245: 195-205.
    • (1970) J Biol Chem , vol.245 , pp. 195-205
    • Deuel, T.F.1    Ginsberg, A.2    Yeh, J.3    Shelton, E.4    Stadtman, E.R.5
  • 33
    • 33749560851 scopus 로고    scopus 로고
    • In vitro analysis of the Escherichia coli AmtB-GlnK complex reveals a stoichiometric interaction and sensitivity to ATP and 2-oxoglutarate
    • Durand, A., and Merrick, M. (2006) In vitro analysis of the Escherichia coli AmtB-GlnK complex reveals a stoichiometric interaction and sensitivity to ATP and 2-oxoglutarate. J Biol Chem 281: 29558-29567.
    • (2006) J Biol Chem , vol.281 , pp. 29558-29567
    • Durand, A.1    Merrick, M.2
  • 35
    • 0036367250 scopus 로고    scopus 로고
    • Mutations in Bacillus subtilis glutamine synthetase that blocks its interaction with transcription factor TnrA
    • Fisher, S., Brandenburg, J.L., and Wray, L.V., Jr (2002) Mutations in Bacillus subtilis glutamine synthetase that blocks its interaction with transcription factor TnrA. Mol Microbiol 45: 627-635.
    • (2002) Mol Microbiol , vol.45 , pp. 627-635
    • Fisher, S.1    Brandenburg, J.L.2    Wray Jr., L.V.3
  • 36
    • 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
  • 37
    • 0021271153 scopus 로고
    • 2-ketoglutarate and the regulation of aconitase and histidase formation in Bacillus subtilis
    • Fisher, S.H., and Magasanik, B. (1984) 2-ketoglutarate and the regulation of aconitase and histidase formation in Bacillus subtilis. J Bacteriol 158: 379-382.
    • (1984) J Bacteriol , vol.158 , pp. 379-382
    • Fisher, S.H.1    Magasanik, B.2
  • 38
    • 0021343043 scopus 로고
    • Bacillus subtilis glutamine synthetase mutants pleiotropically altered in glucose catabolite repression
    • Fisher, S.H., and Sonenshein, A.L. (1984) Bacillus subtilis glutamine synthetase mutants pleiotropically altered in glucose catabolite repression. J Bacteriol 157: 612-621.
    • (1984) J Bacteriol , vol.157 , pp. 612-621
    • Fisher, S.H.1    Sonenshein, A.L.2
  • 39
    • 33748669619 scopus 로고    scopus 로고
    • Feedback-resistant mutants in Bacillus subtilis glutamine synthetase are clustered in the active site
    • Fisher, S.H., and Wray, L.V., Jr (2006) Feedback-resistant mutants in Bacillus subtilis glutamine synthetase are clustered in the active site. J Bacteriol 188: 5966-5974.
    • (2006) J Bacteriol , vol.188 , pp. 5966-5974
    • Fisher, S.H.1    Wray Jr., L.V.2
  • 40
    • 38949168207 scopus 로고    scopus 로고
    • Bacillus subtilis glutamine synthetase regulates its own synthesis by acting as a chaperone to stabilize GlnR-DNA complexes
    • Fisher, S.H., and Wray, L.V., Jr (2008) Bacillus subtilis glutamine synthetase regulates its own synthesis by acting as a chaperone to stabilize GlnR-DNA complexes. Proc Natl Acad Sci USA 105: 1014-1019.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1014-1019
    • Fisher, S.H.1    Wray Jr., L.V.2
  • 41
    • 65249139317 scopus 로고    scopus 로고
    • Novel trans-acting Bacillus subtilis glnA mutations that derepress glnRA expression
    • Fisher, S.H., and Wray, L.V., Jr (2009) Novel trans-acting Bacillus subtilis glnA mutations that derepress glnRA expression. J Bacteriol 191: 2485-2492.
    • (2009) J Bacteriol , vol.191 , pp. 2485-2492
    • Fisher, S.H.1    Wray Jr., L.V.2
  • 42
    • 78651060607 scopus 로고    scopus 로고
    • SPABBATS: a pathway-discovery method based on Boolean satisfiability that facilitates the characterization of suppressor mutants
    • Flórez, L.A., Gunka, K., Polanía, R., Tholen, S., and Stülke, J. (2011) SPABBATS: a pathway-discovery method based on Boolean satisfiability that facilitates the characterization of suppressor mutants. BMC Syst Biol 5: 5.
    • (2011) BMC Syst Biol , vol.5 , pp. 5
    • Flórez, L.A.1    Gunka, K.2    Polanía, R.3    Tholen, S.4    Stülke, J.5
  • 43
    • 39049106044 scopus 로고    scopus 로고
    • PII signal transducers: novel functional and structural insights
    • Forchhammer, K. (2008) PII signal transducers: novel functional and structural insights. Trends Microbiol 16: 65-72.
    • (2008) Trends Microbiol , vol.16 , pp. 65-72
    • Forchhammer, K.1
  • 45
    • 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
  • 46
    • 0030967333 scopus 로고    scopus 로고
    • Role of the transcriptional activator RocR in the arginine-degradation pathway of Bacillus subtilis
    • Gardan, R., Rapoport, G., and Débarbouillé, M. (1997) Role of the transcriptional activator RocR in the arginine-degradation pathway of Bacillus subtilis. Mol Microbiol 24: 825-837.
    • (1997) Mol Microbiol , vol.24 , pp. 825-837
    • Gardan, R.1    Rapoport, G.2    Débarbouillé, M.3
  • 47
    • 37549068524 scopus 로고    scopus 로고
    • Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis
    • Gerth, U., Kock, H., Kusters, I., Michalik, S., Switzer, R.L., and Hecker, M. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190: 321-331.
    • (2008) J Bacteriol , vol.190 , pp. 321-331
    • Gerth, U.1    Kock, H.2    Kusters, I.3    Michalik, S.4    Switzer, R.L.5    Hecker, M.6
  • 48
    • 33846106811 scopus 로고    scopus 로고
    • Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 Å
    • Gruswitz, F., O'Connell, J., III, and Stroud, R.M. (2006) Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 Å. Proc Natl Acad Sci USA 104: 42-47.
    • (2006) Proc Natl Acad Sci USA , vol.104 , pp. 42-47
    • Gruswitz, F.1    O'Connell III, J.2    Stroud, R.M.3
  • 49
    • 77954383542 scopus 로고    scopus 로고
    • Functional dissection of a trigger enzyme: mutations of the Bacillus subtilis glutamate dehydrogenase RocG that affect differentially its catalytic activity and regulatory properties
    • Gunka, K., Newman, J.A., Commichau, F.M., Herzberg, C., Rodrigues, C., Hewitt, L., etal. (2010) Functional dissection of a trigger enzyme: mutations of the Bacillus subtilis glutamate dehydrogenase RocG that affect differentially its catalytic activity and regulatory properties. J Mol Biol 400: 815-827.
    • (2010) J Mol Biol , vol.400 , pp. 815-827
    • Gunka, K.1    Newman, J.A.2    Commichau, F.M.3    Herzberg, C.4    Rodrigues, C.5    Hewitt, L.6
  • 50
    • 84857887703 scopus 로고    scopus 로고
    • A high-frequency mutation in Bacillus subtilis: requirements for the decryptification of the gudB glutamate dehydrogenase gene
    • Gunka, K., Tholen, S., Gerwig, J., Herzberg, C., Stülke, J., and Commichau, F.M. (2012) A high-frequency mutation in Bacillus subtilis: requirements for the decryptification of the gudB glutamate dehydrogenase gene. J Bacteriol 1036: 1036-1044.
    • (2012) J Bacteriol , vol.1036 , pp. 1036-1044
    • Gunka, K.1    Tholen, S.2    Gerwig, J.3    Herzberg, C.4    Stülke, J.5    Commichau, F.M.6
  • 51
    • 33845942520 scopus 로고    scopus 로고
    • Interaction of the membrane-bound GlnK-AmtB complex with the master regulator of nitrogen metabolism TnrA in Bacillus subtilis
    • Heinrich, A., Woyda, K., Brauburger, K., Meiss, G., Detsch, C., Stülke, J., and Forchhammer, K. (2006) Interaction of the membrane-bound GlnK-AmtB complex with the master regulator of nitrogen metabolism TnrA in Bacillus subtilis. J Biol Chem 281: 34909-34917.
    • (2006) J Biol Chem , vol.281 , pp. 34909-34917
    • Heinrich, A.1    Woyda, K.2    Brauburger, K.3    Meiss, G.4    Detsch, C.5    Stülke, J.6    Forchhammer, K.7
  • 52
    • 0028129875 scopus 로고
    • Why does Escherichia coli have two primary pathways for synthesis of glutamate?
    • Helling, R.B. (1994) Why does Escherichia coli have two primary pathways for synthesis of glutamate? J Bacteriol 176: 4664-4668.
    • (1994) J Bacteriol , vol.176 , pp. 4664-4668
    • Helling, R.B.1
  • 53
    • 0032839004 scopus 로고    scopus 로고
    • Sensing of nitrogen limitation by Bacillus subtilis: comparison to enteric bacteria
    • Hu, P., Leighton, T., Ishkhanova, G., and Kustu, S. (1999) Sensing of nitrogen limitation by Bacillus subtilis: comparison to enteric bacteria. J Bacteriol 181: 5042-5050.
    • (1999) J Bacteriol , vol.181 , pp. 5042-5050
    • Hu, P.1    Leighton, T.2    Ishkhanova, G.3    Kustu, S.4
  • 54
    • 0030596516 scopus 로고    scopus 로고
    • Salmonella typhimurium apparently perceives external nitrogen limitation as internal glutamine limitation
    • Ikeda, T.P., Shauger, A.E., and Kustu, S. (1996) Salmonella typhimurium apparently perceives external nitrogen limitation as internal glutamine limitation. J Mol Biol 259: 589-607.
    • (1996) J Mol Biol , vol.259 , pp. 589-607
    • Ikeda, T.P.1    Shauger, A.E.2    Kustu, S.3
  • 55
    • 14644439901 scopus 로고    scopus 로고
    • Complex formation between AmtB and GlnK: an ancestral role of prokaryotic nitrogen control
    • Javelle, A., and Merrick, M. (2005) Complex formation between AmtB and GlnK: an ancestral role of prokaryotic nitrogen control. Biochem Soc Trans 33: 170-172.
    • (2005) Biochem Soc Trans , vol.33 , pp. 170-172
    • Javelle, A.1    Merrick, M.2
  • 56
    • 51149098510 scopus 로고    scopus 로고
    • Inactivation of the general transcription factor TnrA in Bacillus subtilis by proteolysis
    • Kayumov, A., Heinrich, A., Sharipova, M., Iljinskaya, O., and Forchhammer, K. (2008) Inactivation of the general transcription factor TnrA in Bacillus subtilis by proteolysis. Microbiology 154: 2348-2355.
    • (2008) Microbiology , vol.154 , pp. 2348-2355
    • Kayumov, A.1    Heinrich, A.2    Sharipova, M.3    Iljinskaya, O.4    Forchhammer, K.5
  • 57
    • 79955593865 scopus 로고    scopus 로고
    • Interaction of the general transcription factor TnrA with the PII-like protein GlnK and glutamine synthetase in Bacillus subtilis
    • Kayumov, A., Heinrich, A., Fedorova, K., Iljinskaya, O., and Forchhammer, K. (2011) Interaction of the general transcription factor TnrA with the PII-like protein GlnK and glutamine synthetase in Bacillus subtilis. FEBS J 278: 1778-1789.
    • (2011) FEBS J , vol.278 , pp. 1778-1789
    • Kayumov, A.1    Heinrich, A.2    Fedorova, K.3    Iljinskaya, O.4    Forchhammer, K.5
  • 58
    • 33845318547 scopus 로고    scopus 로고
    • The Amt/MEP/Rh family: structure of AmtB and the mechanism of ammonium gas conduction
    • Khademi, S., and Stroud, R.M. (2006) The Amt/MEP/Rh family: structure of AmtB and the mechanism of ammonium gas conduction. Physiology (Bethesda) 21: 419-429.
    • (2006) Physiology (Bethesda) , vol.21 , pp. 419-429
    • Khademi, S.1    Stroud, R.M.2
  • 59
    • 0036049588 scopus 로고    scopus 로고
    • Direct and indirect roles of CcpA in regulation of Bacillus subtilis Krebs cycle genes
    • Kim, H.J., Roux, A., and Sonenshein, A.L. (2002) Direct and indirect roles of CcpA in regulation of Bacillus subtilis Krebs cycle genes. Mol Microbiol 45: 179-190.
    • (2002) Mol Microbiol , vol.45 , pp. 179-190
    • Kim, H.J.1    Roux, A.2    Sonenshein, A.L.3
  • 60
    • 0021796811 scopus 로고
    • Bacterial ammonium transport
    • Kleiner, D. (1985) Bacterial ammonium transport. FEMS Microbiol Rev 32: 87-100.
    • (1985) FEMS Microbiol Rev , vol.32 , pp. 87-100
    • Kleiner, D.1
  • 61
  • 62
    • 77649218943 scopus 로고    scopus 로고
    • Is evolution Darwinian or/and Lamarckian?
    • Koonin, E.V., and Wolf, Y.I. (2009) Is evolution Darwinian or/and Lamarckian? Biol Direct 4: 33.
    • (2009) Biol Direct , vol.4 , pp. 33
    • Koonin, E.V.1    Wolf, Y.I.2
  • 63
    • 33745470323 scopus 로고    scopus 로고
    • GlnR-mediated regulation of nitrogen metabolism in Lactococcus lactis
    • Larsen, R., Kloostermann, T.G., Kok, J., and Kuipers, O.P. (2006) GlnR-mediated regulation of nitrogen metabolism in Lactococcus lactis. J Bacteriol 188: 4978-4982.
    • (2006) J Bacteriol , vol.188 , pp. 4978-4982
    • Larsen, R.1    Kloostermann, T.G.2    Kok, J.3    Kuipers, O.P.4
  • 64
    • 84863230621 scopus 로고    scopus 로고
    • Glutamate dehydrogenase affects resistance to cell wall antibiotics in Bacillus subtilis
    • Lee, Y.H., Kingston, A.W., and Helmann, J.D. (2012) Glutamate dehydrogenase affects resistance to cell wall antibiotics in Bacillus subtilis. J Bacteriol 194: 993-1001.
    • (2012) J Bacteriol , vol.194 , pp. 993-1001
    • Lee, Y.H.1    Kingston, A.W.2    Helmann, J.D.3
  • 65
    • 35448984675 scopus 로고    scopus 로고
    • Nitrogen regulation in bacteria and archaea
    • Leigh, J.A., and Dodsworth, J.A. (2007) Nitrogen regulation in bacteria and archaea. Annu Rev Microbiol 61: 349-377.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 349-377
    • Leigh, J.A.1    Dodsworth, J.A.2
  • 66
    • 77956292192 scopus 로고    scopus 로고
    • Functional microdomains in bacterial membranes
    • López, D., and Kolter, R. (2010) Functional microdomains in bacterial membranes. Genes Dev 24: 1893-1902.
    • (2010) Genes Dev , vol.24 , pp. 1893-1902
    • López, D.1    Kolter, R.2
  • 67
    • 0028154018 scopus 로고
    • Interdependence of K+ and glutamate accumulation during osmotic adaptation of Escherichia coli
    • McLaggan, D., Naprstek, J., Buurman, E.T., and Epstein, W. (1994) Interdependence of K+ and glutamate accumulation during osmotic adaptation of Escherichia coli. J Biol Chem 269: 1911-1917.
    • (1994) J Biol Chem , vol.269 , pp. 1911-1917
    • McLaggan, D.1    Naprstek, J.2    Buurman, E.T.3    Epstein, W.4
  • 68
    • 0142153893 scopus 로고    scopus 로고
    • Ammonia assimilation by Saccharomyces cerevisiae
    • Magasanik, B. (2003) Ammonia assimilation by Saccharomyces cerevisiae. Eukaryot Cell 2: 827-829.
    • (2003) Eukaryot Cell , vol.2 , pp. 827-829
    • Magasanik, B.1
  • 70
    • 0016723556 scopus 로고
    • Role of amino acids in osmoregulation of non-halophilic bacteria
    • Measures, J.C. (1975) Role of amino acids in osmoregulation of non-halophilic bacteria. Nature 257: 398-400.
    • (1975) Nature , vol.257 , pp. 398-400
    • Measures, J.C.1
  • 71
    • 33845421546 scopus 로고    scopus 로고
    • Iron starvation triggers the stringent response and induces amino acid biosynthesis for bacillibactin production in Bacillus subtilis
    • Miethke, M., Westers, H., Blom, E.-J., Kuipers, O.P., and Marahiel, M.A. (2006) Iron starvation triggers the stringent response and induces amino acid biosynthesis for bacillibactin production in Bacillus subtilis. J Bacteriol 188: 8655-8657.
    • (2006) J Bacteriol , vol.188 , pp. 8655-8657
    • Miethke, M.1    Westers, H.2    Blom, E.-J.3    Kuipers, O.P.4    Marahiel, M.A.5
  • 72
    • 0030763298 scopus 로고    scopus 로고
    • Operator interactions by the Bacillus subtilis arginine repressor/activator, AhrC: novel positioning and DNA-mediated assembly of a transcriptional activator at catabolic sites
    • Miller, C.M., Baumberg, S., and Stockley, P.G. (1997) Operator interactions by the Bacillus subtilis arginine repressor/activator, AhrC: novel positioning and DNA-mediated assembly of a transcriptional activator at catabolic sites. Mol Microbiol 26: 37-46.
    • (1997) Mol Microbiol , vol.26 , pp. 37-46
    • Miller, C.M.1    Baumberg, S.2    Stockley, P.G.3
  • 73
    • 0031691173 scopus 로고    scopus 로고
    • Nitrogen and oxygen regulation of Bacillus subtilis nasDEF encoding NADH-dependent nitrite reductase by TnrA and ResDE
    • Nakano, M.M., Hoffmann, T., Zhu, Y., and Jahn, D. (1998) Nitrogen and oxygen regulation of Bacillus subtilis nasDEF encoding NADH-dependent nitrite reductase by TnrA and ResDE. J Bacteriol 180: 5344-5350.
    • (1998) J Bacteriol , vol.180 , pp. 5344-5350
    • Nakano, M.M.1    Hoffmann, T.2    Zhu, Y.3    Jahn, D.4
  • 74
    • 0026059616 scopus 로고
    • Purification and characterization of a repressor for the Bacillus cereus glnRA operon
    • Nakano, Y., and Kimura, Y. (1991) Purification and characterization of a repressor for the Bacillus cereus glnRA operon. J Biochem 109: 223-228.
    • (1991) J Biochem , vol.109 , pp. 223-228
    • Nakano, Y.1    Kimura, Y.2
  • 75
    • 15744405123 scopus 로고    scopus 로고
    • II signal transduction proteins: sensors of alpha-ketoglutarate that regulate nitrogen metabolism
    • II signal transduction proteins: sensors of alpha-ketoglutarate that regulate nitrogen metabolism. Curr Opin Microbiol 8: 168-173.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 168-173
    • Ninfa, A.J.1    Jiang, P.2
  • 76
    • 35348934254 scopus 로고    scopus 로고
    • Genome-scale reconstruction of metabolic network in Bacillus subtilis based on high-throughput phenotyping and gene essentiality data
    • Oh, Y.-K., Palsson, B., Park, S.M., Schilling, C.H., and Mahadevan, R. (2007) Genome-scale reconstruction of metabolic network in Bacillus subtilis based on high-throughput phenotyping and gene essentiality data. J Biol Chem 282: 28791-28799.
    • (2007) J Biol Chem , vol.282 , pp. 28791-28799
    • Oh, Y.-K.1    Palsson, B.2    Park, S.M.3    Schilling, C.H.4    Mahadevan, R.5
  • 77
    • 33845970515 scopus 로고    scopus 로고
    • Molecular mechanism of the regulation Bacillus subtilis gltAB expression by GltC
    • Picossi, S., Belitsky, B.R., and Sonenshein, A.L. (2007) Molecular mechanism of the regulation Bacillus subtilis gltAB expression by GltC. J Mol Biol 365: 1298-1313.
    • (2007) J Mol Biol , vol.365 , pp. 1298-1313
    • Picossi, S.1    Belitsky, B.R.2    Sonenshein, A.L.3
  • 78
    • 78651061152 scopus 로고    scopus 로고
    • Engineering of nitrogen metabolism and its regulation in Corynebacterium glutamicum: influence on amino acid pools and production
    • Rehm, N., and Burkovski, A. (2010) Engineering of nitrogen metabolism and its regulation in Corynebacterium glutamicum: influence on amino acid pools and production. Appl Microbiol Biotechnol 89: 239-248.
    • (2010) Appl Microbiol Biotechnol , vol.89 , pp. 239-248
    • Rehm, N.1    Burkovski, A.2
  • 79
    • 0242276682 scopus 로고    scopus 로고
    • Nitrogen assimilation and global regulation in Escherichia coli
    • Reitzer, L.J. (2003) Nitrogen assimilation and global regulation in Escherichia coli. Annu Rev Microbiol 57: 155-176.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 155-176
    • Reitzer, L.J.1
  • 80
    • 1642489708 scopus 로고
    • Regulation of expression from the glnA promoter of Escherichia coli in the absence of glutamine synthetase
    • Rothstein, D.M., Pahel, G., Tyler, B., and Magasanik, B. (1980) Regulation of expression from the glnA promoter of Escherichia coli in the absence of glutamine synthetase. Proc Natl Acad Sci USA 77: 7372-7376.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 7372-7376
    • Rothstein, D.M.1    Pahel, G.2    Tyler, B.3    Magasanik, B.4
  • 81
    • 33749315818 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of the biosynthesis of glutamine and glutamate, two major compatible solutes in the moderately halophilic bacterium Halobacillus halophilus
    • Saum, S.H., Sydow, J.F., Palm, P., Pfeiffer, F., Oesterhelt, D., and Müller, V. (2006) Biochemical and molecular characterization of the biosynthesis of glutamine and glutamate, two major compatible solutes in the moderately halophilic bacterium Halobacillus halophilus. J Bacteriol 188: 6808-6815.
    • (2006) J Bacteriol , vol.188 , pp. 6808-6815
    • Saum, S.H.1    Sydow, J.F.2    Palm, P.3    Pfeiffer, F.4    Oesterhelt, D.5    Müller, V.6
  • 82
    • 0027446708 scopus 로고
    • Molecular biology of the LysR-type transcriptional regulator (LTTR) family proteins
    • Schell, M.A. (1993) Molecular biology of the LysR-type transcriptional regulator (LTTR) family proteins. Annu Rev Microbiol 47: 597-626.
    • (1993) Annu Rev Microbiol , vol.47 , pp. 597-626
    • Schell, M.A.1
  • 83
    • 0024461721 scopus 로고
    • Regulation of Bacillus subtilis glutamine synthetase gene expression by the product of the glnR gene
    • Schreier, H.J., Brown, S.W., Hirschi, K.D., Nomellini, J.F., and Sonenshein, A.L. (1989) Regulation of Bacillus subtilis glutamine synthetase gene expression by the product of the glnR gene. J Mol Biol 201: 51-63.
    • (1989) J Mol Biol , vol.201 , pp. 51-63
    • Schreier, H.J.1    Brown, S.W.2    Hirschi, K.D.3    Nomellini, J.F.4    Sonenshein, A.L.5
  • 84
    • 41049099764 scopus 로고    scopus 로고
    • Apparative negative co-operativity and substrate inhibition in overexpressed glutamate dehydrogenase from Escherichia coli
    • Sharkey, M.A., and Engel, P.C. (2008) Apparative negative co-operativity and substrate inhibition in overexpressed glutamate dehydrogenase from Escherichia coli. FEMS Microbiol Lett 281: 132-139.
    • (2008) FEMS Microbiol Lett , vol.281 , pp. 132-139
    • Sharkey, M.A.1    Engel, P.C.2
  • 85
    • 0033899859 scopus 로고    scopus 로고
    • Analysis of tnrA alleles which result in a glucose-resistant sporulation phenotype in Bacillus subtilis
    • Shin, B.-S., Choi, S.-K., Smith, I., and Park, S.-H. (2000) Analysis of tnrA alleles which result in a glucose-resistant sporulation phenotype in Bacillus subtilis. J Bacteriol 182: 5009-5012.
    • (2000) J Bacteriol , vol.182 , pp. 5009-5012
    • Shin, B.-S.1    Choi, S.-K.2    Smith, I.3    Park, S.-H.4
  • 86
    • 84861412664 scopus 로고    scopus 로고
    • A global investigation of the Bacillus subtilis iron-sparing response identifies major changes in metabolism
    • Smaldone, G.T., Revelles, O., Gaballa, A., Sauer, U., Antelmann, H., and Helmann, J.D. (2012) A global investigation of the Bacillus subtilis iron-sparing response identifies major changes in metabolism. J Bacteriol 194: 2594-2605.
    • (2012) J Bacteriol , vol.194 , pp. 2594-2605
    • Smaldone, G.T.1    Revelles, O.2    Gaballa, A.3    Sauer, U.4    Antelmann, H.5    Helmann, J.D.6
  • 87
    • 36248971737 scopus 로고    scopus 로고
    • Control of key metabolic intersections in Bacillus subtilis
    • Sonenshein, A.L. (2007) Control of key metabolic intersections in Bacillus subtilis. Nat Rev Microbiol 5: 917-927.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 917-927
    • Sonenshein, A.L.1
  • 88
    • 0016433823 scopus 로고
    • Genetic control of glutamine synthetase in Klebsiella aerogenes
    • Streicher, S.L., Bender, R.A., and Magasanik, B. (1975) Genetic control of glutamine synthetase in Klebsiella aerogenes. J Bacteriol 121: 320-331.
    • (1975) J Bacteriol , vol.121 , pp. 320-331
    • Streicher, S.L.1    Bender, R.A.2    Magasanik, B.3
  • 89
    • 0027204864 scopus 로고
    • Cloning and nucleotide sequence of the Bacillus subtilis ansR gene, which encodes a repressor for the ans operon coding for L-asparaginase and L-aspartase
    • Sun, D., and Setlow, P. (1993) Cloning and nucleotide sequence of the Bacillus subtilis ansR gene, which encodes a repressor for the ans operon coding for L-asparaginase and L-aspartase. J Bacteriol 175: 2501-2506.
    • (1993) J Bacteriol , vol.175 , pp. 2501-2506
    • Sun, D.1    Setlow, P.2
  • 90
    • 0025816503 scopus 로고
    • Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans operon, which encodes for L-asparaginase and L-aspartase
    • Sun, D.X., and Setlow, P. (1991) Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans operon, which encodes for L-asparaginase and L-aspartase. J Bacteriol 173: 3831-3845.
    • (1991) J Bacteriol , vol.173 , pp. 3831-3845
    • Sun, D.X.1    Setlow, P.2
  • 91
    • 0014909673 scopus 로고
    • Influence of environment on the content and composition of microbial free amino acid pools
    • Tempest, D.W., and Meers, J.L. (1970) Influence of environment on the content and composition of microbial free amino acid pools. J Gen Microbiol 64: 171-185.
    • (1970) J Gen Microbiol , vol.64 , pp. 171-185
    • Tempest, D.W.1    Meers, J.L.2
  • 93
    • 0033968928 scopus 로고    scopus 로고
    • The glnKamtB operon: a conserved gene pair in prokaryotes
    • Thomas, G., Coutts, G., and Merrick, M. (2001) The glnKamtB operon: a conserved gene pair in prokaryotes. Trends Genet 16: 11-14.
    • (2001) Trends Genet , vol.16 , pp. 11-14
    • Thomas, G.1    Coutts, G.2    Merrick, M.3
  • 94
    • 0142106372 scopus 로고    scopus 로고
    • The regulatory link between carbon and nitrogen metabolism in Bacillus subtilis: regulation of the gltAB operon by the catabolite control protein CcpA
    • Wacker, I., Ludwig, H., Reif, I., Blencke, H.-M., Detsch, C., and Stülke, J. (2003) The regulatory link between carbon and nitrogen metabolism in Bacillus subtilis: regulation of the gltAB operon by the catabolite control protein CcpA. Microbiology 149: 3001-3009.
    • (2003) Microbiology , vol.149 , pp. 3001-3009
    • Wacker, I.1    Ludwig, H.2    Reif, I.3    Blencke, H.-M.4    Detsch, C.5    Stülke, J.6
  • 95
    • 0025674148 scopus 로고
    • The effects of osmotic upshock on the intracellular solute pools of Bacillus subtilis
    • Whatmore, A.M., Chudek, J.A., and Reed, R.H. (1990) The effects of osmotic upshock on the intracellular solute pools of Bacillus subtilis. J Bacteriol 136: 2527-2535.
    • (1990) J Bacteriol , vol.136 , pp. 2527-2535
    • Whatmore, A.M.1    Chudek, J.A.2    Reed, R.H.3
  • 96
    • 0002715287 scopus 로고
    • Regulation of glutamine synthesis in vivo in E. coli
    • Prusiner, S.B., and Stadtmann, E.R. (eds). New York: Academic Press.
    • Wohlheuter, R.M., Schutt, H., and Holzer, H. (1973) Regulation of glutamine synthesis in vivo in E. coli. In The Enzymes of Glutamine Metabolism. Prusiner, S.B., and Stadtmann, E.R. (eds). New York: Academic Press, pp. 45-64.
    • (1973) The Enzymes of Glutamine Metabolism , pp. 45-64
    • Wohlheuter, R.M.1    Schutt, H.2    Holzer, H.3
  • 97
    • 25844488139 scopus 로고    scopus 로고
    • A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in nitrogen-regulated gene expression
    • Wray, L.V., Jr, and Fisher, S.H. (2005) A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in nitrogen-regulated gene expression. J Biol Chem 280: 33299-33304.
    • (2005) J Biol Chem , vol.280 , pp. 33299-33304
    • Wray Jr., L.V.1    Fisher, S.H.2
  • 98
    • 33845928570 scopus 로고    scopus 로고
    • Functional analysis of the carboxy-terminal region of Bacillus subtilis TnrA, a MerR family protein
    • Wray, L.V., Jr, and Fisher, S.H. (2007) Functional analysis of the carboxy-terminal region of Bacillus subtilis TnrA, a MerR family protein. J Bacteriol 189: 20-27.
    • (2007) J Bacteriol , vol.189 , pp. 20-27
    • Wray Jr., L.V.1    Fisher, S.H.2
  • 99
    • 41049106965 scopus 로고    scopus 로고
    • Bacillus subtilis GlnR contains an autoinhibitory C-terminal domain required for the interaction with glutamine synthetase
    • Wray, L.V., Jr, and Fisher, S.H. (2008) Bacillus subtilis GlnR contains an autoinhibitory C-terminal domain required for the interaction with glutamine synthetase. Mol Microbiol 68: 277-285.
    • (2008) Mol Microbiol , vol.68 , pp. 277-285
    • Wray Jr., L.V.1    Fisher, S.H.2
  • 100
    • 77957372313 scopus 로고    scopus 로고
    • Functional roles of the conserved Glu304 loop of Bacillus subtilis glutamine synthetase
    • Wray, L.V., Jr, and Fisher, S.H. (2010) Functional roles of the conserved Glu304 loop of Bacillus subtilis glutamine synthetase. J Bacteriol 192: 5018-5045.
    • (2010) J Bacteriol , vol.192 , pp. 5018-5045
    • Wray Jr., L.V.1    Fisher, S.H.2
  • 101
    • 0028069556 scopus 로고
    • The nitrogen-regulated Bacillus subtilis nrgAB operon encodes a membrane protein and a protein highly similar to the Escherichia coli glnB-encoded PII protein
    • Wray, L.V., Jr, Atkinson, M.R., and Fisher, S.H. (1994) The nitrogen-regulated Bacillus subtilis nrgAB operon encodes a membrane protein and a protein highly similar to the Escherichia coli glnB-encoded PII protein. J Bacteriol 176: 108-114.
    • (1994) J Bacteriol , vol.176 , pp. 108-114
    • Wray Jr., L.V.1    Atkinson, M.R.2    Fisher, S.H.3
  • 102
    • 9444233868 scopus 로고    scopus 로고
    • TnrA, a transcription factor required for global nitrogen regulation in Bacillus subtilis
    • Wray, L.V., Jr, Ferson, A.E., Rohrer, K., and Fisher, S.H. (1996) TnrA, a transcription factor required for global nitrogen regulation in Bacillus subtilis. Proc Natl Acad Sci USA 93: 8841-8845.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8841-8845
    • Wray Jr., L.V.1    Ferson, A.E.2    Rohrer, K.3    Fisher, S.H.4
  • 103
    • 0034733384 scopus 로고    scopus 로고
    • Purification and in vitro activities of the Bacillus subtilis TnrA transcription factor
    • Wray, L.V., Jr, Zalieckas, J.M., and Fisher, S.H. (2000) Purification and in vitro activities of the Bacillus subtilis TnrA transcription factor. J Mol Biol 300: 29-40.
    • (2000) J Mol Biol , vol.300 , pp. 29-40
    • Wray Jr., L.V.1    Zalieckas, J.M.2    Fisher, S.H.3
  • 104
    • 0035900641 scopus 로고    scopus 로고
    • Bacillus subtilis glutamine synthetase controls gene expression through a protein-protein interaction with transcription factor TnrA
    • Wray, L.V., Jr, Zalieckas, J.M., and Fisher, S.H. (2001) Bacillus subtilis glutamine synthetase controls gene expression through a protein-protein interaction with transcription factor TnrA. Cell 107: 427-435.
    • (2001) Cell , vol.107 , pp. 427-435
    • Wray Jr., L.V.1    Zalieckas, J.M.2    Fisher, S.H.3
  • 105
    • 34547148485 scopus 로고    scopus 로고
    • Protection of the glutamate pool concentration in enteric bacteria
    • Yan, D. (2007) Protection of the glutamate pool concentration in enteric bacteria. Proc Natl Acad Sci USA 104: 9475-9480.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 9475-9480
    • Yan, D.1
  • 106
    • 0037709014 scopus 로고    scopus 로고
    • Identification of additional TnrA-regulated genes of Bacillus subtilis associated with TnrA box
    • Yoshida, K.I., Yamaguchi, H., Kinehara, M., Ohki, Y.H., Nakaura, Y., and Fujita, Y. (2003) Identification of additional TnrA-regulated genes of Bacillus subtilis associated with TnrA box. Mol Microbiol 49: 157-165.
    • (2003) Mol Microbiol , vol.49 , pp. 157-165
    • Yoshida, K.I.1    Yamaguchi, H.2    Kinehara, M.3    Ohki, Y.H.4    Nakaura, Y.5    Fujita, Y.6
  • 107
    • 33645215815 scopus 로고    scopus 로고
    • Cross-regulation of the Bacillus subtilis glnRA and tnrA genes provides evidence for DNA binding site discrimination
    • Zalieckas, J.M., Wray, L.V., Jr, and Fisher, S.H. (2006) Cross-regulation of the Bacillus subtilis glnRA and tnrA genes provides evidence for DNA binding site discrimination. J Bacteriol 188: 2578-2585.
    • (2006) J Bacteriol , vol.188 , pp. 2578-2585
    • Zalieckas, J.M.1    Wray Jr., L.V.2    Fisher, S.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.