메뉴 건너뛰기




Volumn 190, Issue 10, 2008, Pages 3557-3564

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

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; ARGININE; GLUTAMATE DEHYDROGENASE; GLUTAMATE SYNTHASE; GLUTAMIC ACID;

EID: 47049089928     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00099-08     Document Type: Article
Times cited : (80)

References (38)
  • 2
    • 0033968158 scopus 로고    scopus 로고
    • Regulation of the transport system for C4-dicarboxylic acids in Bacillus subtilis
    • Asai, K., S. H. Baik, Y. Kasahara, S. Moriya, and N. Ogasawara. 2000. Regulation of the transport system for C4-dicarboxylic acids in Bacillus subtilis. Microbiology 146:263-271.
    • (2000) Microbiology , vol.146 , pp. 263-271
    • Asai, K.1    Baik, S.H.2    Kasahara, Y.3    Moriya, S.4    Ogasawara, N.5
  • 3
    • 0005736451 scopus 로고    scopus 로고
    • Biosynthesis of amino acids of the glutamate and aspartate families, alanine, and polyamines
    • A. L. Sonenshein, J. A. Hoch, and R. Losick ed, American Society for Microbiology, Washington, DC
    • Belitsky, B. R. 2002. Biosynthesis of amino acids of the glutamate and aspartate families, alanine, and polyamines, p. 203-231. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and its closest relatives: from genes to cells. American Society for Microbiology, Washington, DC.
    • (2002) Bacillus subtilis and its closest relatives: From genes to cells , pp. 203-231
    • Belitsky, B.R.1
  • 4
    • 0031756184 scopus 로고    scopus 로고
    • Role and regulation of Bacillus subtilis glutamate dehydrogenase genes
    • Belitsky, B. R., and A. L. Sonenshein. 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
  • 5
    • 0033621091 scopus 로고    scopus 로고
    • An enhancer element located downstream of the major glutamate dehydrogenase gene of Bacillus subtilis
    • Belitsky, B. R., and A. L. Sonenshein. 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
  • 6
    • 0033758755 scopus 로고    scopus 로고
    • Role of TnrA in nitrogen source-dependent repression of Bacillus subtilis glutamate synthase gene expression
    • Belitsky, B. R., L. V. Wray, Jr., S. H. Fisher, D. E. Bohannon, and A. L. Sonenshein. 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.E.4    Sonenshein, A.L.5
  • 7
    • 2442649038 scopus 로고    scopus 로고
    • Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase
    • Belitsky, B. R., and A. L. Sonenshein. 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
  • 8
    • 2442669092 scopus 로고    scopus 로고
    • CcpA-dependent regulation of Bacillus subtilis glutamate dehydrogenase gene expression
    • Belitsky, B. R., H.-J. Kim, and A. L. Sonenshein. 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
  • 9
    • 0024730354 scopus 로고
    • Positive regulation of glutamate biosynthesis in Bacillus subtilis
    • Bohannon, D. E., and A. L. Sonenshein. 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
  • 11
    • 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., C. Herzberg, P. Tripal, O. Valerius, and J. Stülke. 2007. 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
  • 13
    • 38449095243 scopus 로고    scopus 로고
    • Trigger enzymes: Bifunctional proteins active in metabolism and in controlling gene expression
    • Commichau, F. M., and J. Stülke. 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
  • 14
    • 0344875060 scopus 로고    scopus 로고
    • Ammonium utilization in Bacillus subtilis: Transport and regulatory functions of NrgA and NrgB
    • Detsch, C., and J. Stülke. 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
  • 16
    • 0029590029 scopus 로고
    • Antibiotic resistance cassettes for Bacillus subtilis
    • Guérout-Fleury, A. M., K. Shazand, N. Frandsen, and P. Stragier. 1995. Antibiotic resistance cassettes for Bacillus subtilis. Gene 167:335-336.
    • (1995) Gene , vol.167 , pp. 335-336
    • Guérout-Fleury, A.M.1    Shazand, K.2    Frandsen, N.3    Stragier, P.4
  • 17
    • 0021004801 scopus 로고
    • Role of cryptic genes in microbial evolution
    • Hall, B. G., S. Yokoyama, and D. H. Calhoun. 1983. Role of cryptic genes in microbial evolution. Mol. Biol. Evol. 1:109-124.
    • (1983) Mol. Biol. Evol , vol.1 , pp. 109-124
    • Hall, B.G.1    Yokoyama, S.2    Calhoun, D.H.3
  • 18
    • 0032839004 scopus 로고    scopus 로고
    • Sensing of nitrogen limitation by Bacillus subtilis: Comparison to enteric bacteria
    • Hu, P., T. Leighton, G. Ishkhanova, and S. Kustu. 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
  • 19
    • 0034695574 scopus 로고    scopus 로고
    • The HPr kinase from Bacillus subtilis is a homooligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding
    • Jault, J. M., S. Fieulaine, S. Nessler, P. Gonzalo, A. Di Pietro, J. Deutscher, and A. Galinier. 2000. The HPr kinase from Bacillus subtilis is a homooligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding. J. Biol. Chem. 275:1773-1780.
    • (2000) J. Biol. Chem , vol.275 , pp. 1773-1780
    • Jault, J.M.1    Fieulaine, S.2    Nessler, S.3    Gonzalo, P.4    Di Pietro, A.5    Deutscher, J.6    Galinier, A.7
  • 20
    • 33745923792 scopus 로고    scopus 로고
    • Regulation of LiaRS-dependent gene expression in Bacillus subtilis: Identification of inhibitor proteins, regulator binding sites, and target genes of a conserved cell envelope stress-sensing two-component system
    • Jordan, S., A. Junker, J. D. Helmann, and T. Mascher. 2006. Regulation of LiaRS-dependent gene expression in Bacillus subtilis: identification of inhibitor proteins, regulator binding sites, and target genes of a conserved cell envelope stress-sensing two-component system. J. Bacteriol. 188:5153-5166.
    • (2006) J. Bacteriol , vol.188 , pp. 5153-5166
    • Jordan, S.1    Junker, A.2    Helmann, J.D.3    Mascher, T.4
  • 21
    • 27644547321 scopus 로고    scopus 로고
    • Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis
    • Khan, M. I., K. Ito, H. Kim, H. Ashida, T. Ishikawa, H. Shibata, and Y. Sawa. 2005. Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis. Biosci. Biotechnol. Biochem. 69:1861-1870.
    • (2005) Biosci. Biotechnol. Biochem , vol.69 , pp. 1861-1870
    • Khan, M.I.1    Ito, K.2    Kim, H.3    Ashida, H.4    Ishikawa, T.5    Shibata, H.6    Sawa, Y.7
  • 22
    • 0031780217 scopus 로고    scopus 로고
    • The Bacillus subtilis AraE protein displays a broad substrate specificity for several different sugars
    • Krispin, O., and R. Allmansberger. 1998. The Bacillus subtilis AraE protein displays a broad substrate specificity for several different sugars. J. Bacteriol. 180:3250-3252.
    • (1998) J. Bacteriol , vol.180 , pp. 3250-3252
    • Krispin, O.1    Allmansberger, R.2
  • 23
    • 0029006115 scopus 로고
    • Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis
    • Kunst, F., and G. Rapoport. 1995. Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis. J. Bacteriol. 177: 2403-2407.
    • (1995) J. Bacteriol , vol.177 , pp. 2403-2407
    • Kunst, F.1    Rapoport, G.2
  • 24
    • 0028038196 scopus 로고
    • Interaction of wild-type truncated LevR of Bacillus subtilis with the upstream activating sequence of the levanase operon
    • Martin-Verstraete, I., M. Débarbouillé, A. Klier, and G. Rapoport. 1994. Interaction of wild-type 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
  • 25
    • 1642480263 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae HPr kinase/phosphorylase: Assigning functional roles to the P-loop and the HPrK/P signature sequence motif
    • Merzbacher, M., C. Detsch, W. Hillen, and J. Stülke. 2004. Mycoplasma pneumoniae HPr kinase/phosphorylase: assigning functional roles to the P-loop and the HPrK/P signature sequence motif. Eur. J. Biochem. 271:367-374.
    • (2004) Eur. J. Biochem , vol.271 , pp. 367-374
    • Merzbacher, M.1    Detsch, C.2    Hillen, W.3    Stülke, J.4
  • 26
    • 33845970515 scopus 로고    scopus 로고
    • Molecular mechanism of the regulation of Bacillus subtilis gltAB expression by GltC
    • Picossi, S., B. R. Belitsky, and A. L. Sonenshein. 2007. Molecular mechanism of the regulation of 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
  • 27
    • 0242276682 scopus 로고    scopus 로고
    • Nitrogen assimilation and global regulation in Escherichia coli
    • Reitzer, L. 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.1
  • 28
    • 0016697801 scopus 로고
    • Glutamate dehydrogenase from Escherichia coli: Purification and properties
    • Sakamoto, N., A. M. Kotre, and M. A. Savageau. 1975. Glutamate dehydrogenase from Escherichia coli: purification and properties. J. Bacteriol. 124: 775-783.
    • (1975) J. Bacteriol , vol.124 , pp. 775-783
    • Sakamoto, N.1    Kotre, A.M.2    Savageau, M.A.3
  • 30
    • 0032189445 scopus 로고    scopus 로고
    • Menaquinone-dependent succinate dehydrogenase of bacteria catalyzes reversed electron transport driven by the proton potential
    • Schirawski, J., and G. Unden. 1998. Menaquinone-dependent succinate dehydrogenase of bacteria catalyzes reversed electron transport driven by the proton potential. Eur. J. Biochem. 257:210-215.
    • (1998) Eur. J. Biochem , vol.257 , pp. 210-215
    • Schirawski, J.1    Unden, G.2
  • 31
    • 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
  • 32
    • 0034114864 scopus 로고    scopus 로고
    • Do bacterial cryptic genes really exist?
    • Tamburini, E., and G. Mastromei. 2000. Do bacterial cryptic genes really exist? Res. Microbiol. 151:179-182.
    • (2000) Res. Microbiol , vol.151 , pp. 179-182
    • Tamburini, E.1    Mastromei, G.2
  • 33
    • 0141591734 scopus 로고    scopus 로고
    • The Bacillus subtilis YufLM two-component system regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium
    • Tanaka, K., K. Kobayashi, and N. Ogasawara. 2003. The Bacillus subtilis YufLM two-component system regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Microbiology 149:2317-2329.
    • (2003) Microbiology , vol.149 , pp. 2317-2329
    • Tanaka, K.1    Kobayashi, K.2    Ogasawara, N.3
  • 34
    • 0029871347 scopus 로고    scopus 로고
    • PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in Saccharomyces cerevisiae
    • Wach, A. 1996. PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in Saccharomyces cerevisiae. Yeast 12:259-265.
    • (1996) Yeast , vol.12 , pp. 259-265
    • Wach, A.1
  • 35
    • 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., H. Ludwig, I. Reif, H.-M. Blencke, C. Detsch, and J. Stülke. 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
  • 36
    • 0025674148 scopus 로고
    • The effects of osmotic upshock on the intracellular solute pools of Bacillus subtilis
    • Whatmore, A. M., J. A. Chudek, and R. H. Reed. 1990. The effects of osmotic upshock on the intracellular solute pools of Bacillus subtilis. J. Gen. Microbiol. 136:2527-2535.
    • (1990) J. Gen. Microbiol , vol.136 , pp. 2527-2535
    • Whatmore, A.M.1    Chudek, J.A.2    Reed, R.H.3
  • 37
    • 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., J. M. Zalieckas, and S. H. Fisher. 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
  • 38
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.