메뉴 건너뛰기




Volumn 191, Issue 8, 2009, Pages 2485-2492

Novel trans-Acting Bacillus subtilis glnA mutations that DerepressglnRA expression

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE AMMONIA LIGASE; GLUTAMINE; GLYCINE DERIVATIVE; MUTANT PROTEIN; BACTERIAL DNA; BACTERIAL PROTEIN; GLUTAMINE SYNTHETASE I; REPRESSOR PROTEIN; SCGR PROTEIN, BACILLUS SUBTILIS; TRANSACTIVATOR PROTEIN;

EID: 65249139317     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01734-08     Document Type: Article
Times cited : (17)

References (57)
  • 1
    • 0026067217 scopus 로고
    • Identification of genes and gene products whose expression is activated during nitrogen-limited growth in Bacillus subtilis
    • Atkinson, M. R., and S. H. Fisher. 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
  • 2
    • 0024989791 scopus 로고
    • Regulation of histidine and proline degradation enzymes by amino acid availability in Bacillus subtilis
    • Atkinson, M. R., L. V. Wray, Jr., and S. H. Fisher. 1990. Regulation of histidine and proline degradation enzymes by amino acid availability in Bacillus subtilis. J. Bacteriol. 172:4758-4765.
    • (1990) J. Bacteriol , vol.172 , pp. 4758-4765
    • Atkinson, M.R.1    Wray Jr., L.V.2    Fisher, S.H.3
  • 3
    • 0036778131 scopus 로고    scopus 로고
    • Activation of the glnA, glnK, and nac promoters as Escherichia coli undergoes the transition from nitrogen excess growth to nitrogen starvation
    • Atkinson, M. R., T. A. Blauwkamp, V. Bondarenko, V. Studitsky, and A. J. Ninfa. 2002. Activation of the glnA, glnK, and nac promoters as Escherichia coli undergoes the transition from nitrogen excess growth to nitrogen starvation. J. Bacteriol. 184:5358-5363.
    • (2002) J. Bacteriol , vol.184 , pp. 5358-5363
    • Atkinson, M.R.1    Blauwkamp, T.A.2    Bondarenko, V.3    Studitsky, V.4    Ninfa, A.J.5
  • 4
    • 0036275506 scopus 로고    scopus 로고
    • Transcriptional analysis of the Bacillus subtilis PucR regulon and identification of a cis-acting site required for PucR-regulated expression of genes involved in purine catabolism
    • Beier, L., P. Nygaard, H. Jamer, and H. H. Saxild. 2002. Transcriptional analysis of the Bacillus subtilis PucR regulon and identification of a cis-acting site required for PucR-regulated expression of genes involved in purine catabolism. J. Bacteriol. 184:3232-3241.
    • (2002) J. Bacteriol , vol.184 , pp. 3232-3241
    • Beier, L.1    Nygaard, P.2    Jamer, H.3    Saxild, H.H.4
  • 5
    • 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
    • 0029882155 scopus 로고    scopus 로고
    • Autogenous regulation of the Bacillus subtilis glnRA operon
    • Brown, S. W., and A. L. Sonenshein. 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
  • 8
    • 0014410024 scopus 로고
    • Induction and repression of the histidine-degrading enzymes of Bacillus subtilis
    • Chasin, L. A., and B. Magasanik. 1968. Induction and repression of the histidine-degrading enzymes of Bacillus subtilis. J. Biol. Chem. 243:5165-5178.
    • (1968) J. Biol. Chem , vol.243 , pp. 5165-5178
    • Chasin, L.A.1    Magasanik, B.2
  • 9
    • 0002301028 scopus 로고
    • Genetic analysis
    • C. R. Harwood and S. M. Cutting ed, John Wiley & Sons, Inc, New York, NY
    • Cutting, S. M., and P. B. Vander Horn. 1990. Genetic analysis, p. 27-74. In C. R. Harwood and S. M. Cutting (ed.), Molecular biological methods for Bacillus. John Wiley & Sons, Inc., New York, NY.
    • (1990) Molecular biological methods for Bacillus , pp. 27-74
    • Cutting, S.M.1    Vander Horn, P.B.2
  • 10
    • 0017718533 scopus 로고
    • Alteration of the Bacillus subtilis glutamine synthetase results in overproduction of the enzyme
    • Dean, D. R., J. A. Hoch, and A. I. Aronson. 1977. Alteration of the Bacillus subtilis glutamine synthetase results in overproduction of the enzyme. J. Bacteriol. 131:981-987.
    • (1977) J. Bacteriol , vol.131 , pp. 981-987
    • Dean, D.R.1    Hoch, J.A.2    Aronson, A.I.3
  • 11
    • 0014962857 scopus 로고
    • Bacillus subtilis glutamine synthetase. Purification and physical characterization
    • Deuel, T. F., A. Ginsburg, J. Yeh, E. Shelton, and E. R. Stadtman. 1970. Bacillus subtilis glutamine synthetase. Purification and physical characterization. J. Biol. Chem. 245:5195-5205.
    • (1970) J. Biol. Chem , vol.245 , pp. 5195-5205
    • Deuel, T.F.1    Ginsburg, A.2    Yeh, J.3    Shelton, E.4    Stadtman, E.R.5
  • 12
    • 0015980222 scopus 로고
    • Regulationofglutamine synthetase from Bacillus subtilis by divalent cations, feedback inhibitors, and L-glutamine
    • Deuel, T. F., and S. Prusiner. 1974. Regulationofglutamine 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
  • 14
    • 0029805601 scopus 로고    scopus 로고
    • Expression of the Bacillus subtilis gabP gene is regulated independently in response to nitrogen and amino acid availability
    • Ferson, A. E., L. V. Wray, Jr., and S. H. Fisher. 1996. Expression of the Bacillus subtilis gabP gene is regulated independently in response to nitrogen and amino acid availability. Mol. Microbiol. 22:693-701.
    • (1996) Mol. Microbiol , vol.22 , pp. 693-701
    • Ferson, A.E.1    Wray Jr., L.V.2    Fisher, S.H.3
  • 15
    • 0032950276 scopus 로고    scopus 로고
    • Regulation of nitrogen metabolism in Bacillus subtilis: Vive la difference!
    • Fisher, S. H. 1999. Regulation of nitrogen metabolism in Bacillus subtilis: vive la difference! Mol. Microbiol. 32:223-232.
    • (1999) Mol. Microbiol , vol.32 , pp. 223-232
    • Fisher, S.H.1
  • 16
    • 0036367250 scopus 로고    scopus 로고
    • Fisher, S. H., J. L. Brandenburg, and L. V. Wray, Jr. 2002. Mutations in Bacillus subtilis glutamine synthetase that block its interaction with transcription factor TnrA. Mol. Microbiol. 45:627-635.
    • Fisher, S. H., J. L. Brandenburg, and L. V. Wray, Jr. 2002. Mutations in Bacillus subtilis glutamine synthetase that block its interaction with transcription factor TnrA. Mol. Microbiol. 45:627-635.
  • 17
    • 0021343043 scopus 로고
    • Bacillus subtilis glutamine syn- thetase mutants pleiotropically altered in glucose catabolite repression
    • Fisher, S. H., and A. L. Sonenshein. 1984. Bacillus subtilis glutamine syn- thetase 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
  • 18
    • 0036206506 scopus 로고    scopus 로고
    • Fisher, S. H., and L. V. Wray, Jr. 2002. Bacillus subtilis 168 contains two differentially regulated genes encoding L-asparaginase. J. Bacteriol. 184: 2148-2154.
    • Fisher, S. H., and L. V. Wray, Jr. 2002. Bacillus subtilis 168 contains two differentially regulated genes encoding L-asparaginase. J. Bacteriol. 184: 2148-2154.
  • 19
    • 33748669619 scopus 로고    scopus 로고
    • Fisher, S. H., and L. V. Wray, Jr. 2006. Feedback-resistant mutations in Bacillus subtilis glutamine synthetase are clustered in the active site. J. Bacteriol. 188:5966-5974.
    • Fisher, S. H., and L. V. Wray, Jr. 2006. Feedback-resistant mutations in Bacillus subtilis glutamine synthetase are clustered in the active site. J. Bacteriol. 188:5966-5974.
  • 20
    • 38949168207 scopus 로고    scopus 로고
    • Fisher, S. H., and L. V. Wray, 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.
    • Fisher, S. H., and L. V. Wray, 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.
  • 21
    • 0035916242 scopus 로고    scopus 로고
    • The crystal structure ofphosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition
    • Gill, H. S., and D. Eisenberg. 2001. The crystal structure ofphosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition. Biochemistry 40:1903-1912.
    • (2001) Biochemistry , vol.40 , pp. 1903-1912
    • Gill, H.S.1    Eisenberg, D.2
  • 22
    • 0026511476 scopus 로고
    • Interaction of the Bacillus subtilis glnRA repressor with operator and promoter regions in vivo
    • Gutowski, J. C., and H. J. Schreier. 1992. Interaction of the Bacillus subtilis glnRA repressor with operator and promoter regions in vivo. J. Bacteriol. 174:671-681.
    • (1992) J. Bacteriol , vol.174 , pp. 671-681
    • Gutowski, J.C.1    Schreier, H.J.2
  • 23
    • 0032839004 scopus 로고    scopus 로고
    • Sensing of nitrogen limitation by Bacillus subtilis: Comparison to enteric bacteria
    • Hu, P., T. Leighton, G. Iskhanova, 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    Iskhanova, G.3    Kustu, S.4
  • 24
    • 5444225208 scopus 로고    scopus 로고
    • Multiple active site conformations revealed by distant site mutation in ornithine decarboxylase
    • Jackson, L. K., J. Baldwin, R. Akella, E. J. Goldsmith, and M. A. Phillips. 2004. Multiple active site conformations revealed by distant site mutation in ornithine decarboxylase. Biochemistry 43:12990-12999.
    • (2004) Biochemistry , vol.43 , pp. 12990-12999
    • Jackson, L.K.1    Baldwin, J.2    Akella, R.3    Goldsmith, E.J.4    Phillips, M.A.5
  • 25
    • 0037184065 scopus 로고    scopus 로고
    • Distribution of mutations in human thymidylate synthase yielding resistance to 5-fluorodeoxyuridine
    • Kawate, H., D. M. Landis, and L. A. Loeb. 2002. Distribution of mutations in human thymidylate synthase yielding resistance to 5-fluorodeoxyuridine. J. Biol. Chem. 277:36304-36311.
    • (2002) J. Biol. Chem , vol.277 , pp. 36304-36311
    • Kawate, H.1    Landis, D.M.2    Loeb, L.A.3
  • 26
    • 23044445202 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights
    • Krajewski, W. W., T. A. Jones, and S. L. Mowbray. 2005. Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights. Proc. Natl. Acad. Sci. USA 102:10499-10504.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10499-10504
    • Krajewski, W.W.1    Jones, T.A.2    Mowbray, S.L.3
  • 27
    • 0028082017 scopus 로고
    • Structural model for the reaction mechanism of glutamine synthetase, based on five crystal structures of enzyme-substrate complexes
    • Liaw, S.-H., and D. Eisenberg. 1994. Structural model for the reaction mechanism of glutamine synthetase, based on five crystal structures of enzyme-substrate complexes. Biochemistry 33:675-681.
    • (1994) Biochemistry , vol.33 , pp. 675-681
    • Liaw, S.-H.1    Eisenberg, D.2
  • 28
    • 0037469148 scopus 로고    scopus 로고
    • A major role for a set of non-active site mutations in the development of HIV-1 protease drug resistance
    • Muzammil, S., P. Ross, and E. Freire. 2003. A major role for a set of non-active site mutations in the development of HIV-1 protease drug resistance. Biochemistry 42:631-638.
    • (2003) Biochemistry , vol.42 , pp. 631-638
    • Muzammil, S.1    Ross, P.2    Freire, E.3
  • 29
    • 0028932022 scopus 로고
    • Nitrogenregulation of nasA and the nasB operon, which encode genes required for nitrate assimilation in Bacillus subtilis
    • Nakano, M. M., F. Yang, P. Hardin, and P. Zuber. 1995. Nitrogenregulation of nasA and the nasB operon, which encode genes required for nitrate assimilation in Bacillus subtilis. J. Bacteriol. 177:573-579.
    • (1995) J. Bacteriol , vol.177 , pp. 573-579
    • Nakano, M.M.1    Yang, F.2    Hardin, P.3    Zuber, P.4
  • 31
    • 0023665129 scopus 로고
    • Initiation of transcription at the bacterial glnAp2 promoter by purified E. coli components is facilitated by enhancers
    • Ninfa, A. J., L. J. Reitzer, and B. Magasanik. 1987. Initiation of transcription at the bacterial glnAp2 promoter by purified E. coli components is facilitated by enhancers. Cell 50:1039-1046.
    • (1987) Cell , vol.50 , pp. 1039-1046
    • Ninfa, A.J.1    Reitzer, L.J.2    Magasanik, B.3
  • 32
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., F. Vajdos, L. Fee, G. Grimsley, and T. Gray. 1995. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4:2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 34
    • 0020030827 scopus 로고
    • Complex glnA-glnL-glnG operon of Escherichia coli
    • Pahel, G., D. M. Rothstein, and B. Magasanik. 1982. Complex glnA-glnL-glnG operon of Escherichia coli. J. Bacteriol. 150:202-213.
    • (1982) J. Bacteriol , vol.150 , pp. 202-213
    • Pahel, G.1    Rothstein, D.M.2    Magasanik, B.3
  • 35
    • 1942503297 scopus 로고    scopus 로고
    • Controlling the enantioselectivity of enzymes by directed evolution: Practical and theoretical ramifications
    • Reetz, M. T. 2004. Controlling the enantioselectivity of enzymes by directed evolution: practical and theoretical ramifications. Proc. Natl. Acad. Sci. USA 101:5716-5722.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5716-5722
    • Reetz, M.T.1
  • 36
    • 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
  • 38
    • 0033965778 scopus 로고    scopus 로고
    • Expression of a new operon from Bacillus subtilis ykzB-ykoL under the control of the TnrA and PhoO-PhoR global regulators
    • Robichon, D., M. Arnaud, R. Gardan, Z. Pragai, M. O'Reilly, G. Rapoport, and M. Débarbouille. 2000. Expression of a new operon from Bacillus subtilis ykzB-ykoL under the control of the TnrA and PhoO-PhoR global regulators. J. Bacteriol. 182:1226-1231.
    • (2000) J. Bacteriol , vol.182 , pp. 1226-1231
    • Robichon, D.1    Arnaud, M.2    Gardan, R.3    Pragai, Z.4    O'Reilly, M.5    Rapoport, G.6    Débarbouille, M.7
  • 39
    • 0038810233 scopus 로고    scopus 로고
    • Correlated motion and the effect of distal mutations in dihydrofolate reductase
    • Rod, T. H., J. L. Radkiewicz, and C. L. Brooks. 2003. Correlated motion and the effect of distal mutations in dihydrofolate reductase. Proc. Natl. Acad. Sci. USA 100:6980-6985.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6980-6985
    • Rod, T.H.1    Radkiewicz, J.L.2    Brooks, C.L.3
  • 40
    • 1642489708 scopus 로고
    • Regulation of expression from the glnA promoter of Escherichia coli in the absence of glutamine synthetase
    • Rothstein, D. M., G. Pahel, B. Tyler, and B. Maganasik. 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    Maganasik, B.4
  • 41
    • 0024461721 scopus 로고
    • Regulation of Bacillus subtilis glutamine synthetase gene expression by the product of the glnR gene
    • Schreier, H. J., S. W. Brown, K. D. Hirschi, J. F. Nomellini, and A. L. Sonenshein. 1989. Regulation of Bacillus subtilis glutamine synthetase gene expression by the product of the glnR gene. J. Mol. Biol. 210:51-63.
    • (1989) J. Mol. Biol , vol.210 , pp. 51-63
    • Schreier, H.J.1    Brown, S.W.2    Hirschi, K.D.3    Nomellini, J.F.4    Sonenshein, A.L.5
  • 42
    • 0021814004 scopus 로고
    • Regulation of expression from the glnA promoter of Bacillus subtilis requires the glnA gene product
    • Schreier, H. J., S. H. Fisher, and A. L. Sonenshein. 1985. Regulation of expression from the glnA promoter of Bacillus subtilis requires the glnA gene product. Proc. Natl. Acad. Sci. USA 82:3375-3379.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3375-3379
    • Schreier, H.J.1    Fisher, S.H.2    Sonenshein, A.L.3
  • 43
    • 0027478177 scopus 로고
    • Altered regulation of the glnRA operon in a Bacillus subtilis mutant that produces methionine sulfoximine-tolerant glutamine synthetase
    • Schreier, H. J., C. A. Rostkowski, and E. M. Kellner. 1993. Altered regulation of the glnRA operon in a Bacillus subtilis mutant that produces methionine sulfoximine-tolerant glutamine synthetase. J. Bacteriol. 175:892-897.
    • (1993) J. Bacteriol , vol.175 , pp. 892-897
    • Schreier, H.J.1    Rostkowski, C.A.2    Kellner, E.M.3
  • 44
    • 0022486523 scopus 로고
    • Altered regulation of the glnA gene in glutamine synthetase mutants of Bacillus subtilis
    • Schreier, H. J., and A. L. Sonenshein. 1986. Altered regulation of the glnA gene in glutamine synthetase mutants of Bacillus subtilis. J. Bacteriol. 167: 35-43.
    • (1986) J. Bacteriol , vol.167 , pp. 35-43
    • Schreier, H.J.1    Sonenshein, A.L.2
  • 45
  • 46
    • 0015919826 scopus 로고
    • Studies onglutamine synthetase from Escherichia coli. Formation of pyrrolidone carboxylate and inhibition by methionine sulfoximine
    • Weisbrod, R. E., and A. Meister. 1973. Studies onglutamine synthetase from Escherichia coli. Formation of pyrrolidone carboxylate and inhibition by methionine sulfoximine. J. Biol. Chem. 248:3997-4002.
    • (1973) J. Biol. Chem , vol.248 , pp. 3997-4002
    • Weisbrod, R.E.1    Meister, A.2
  • 47
    • 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., M. R. Atkinson, and S. H. Fisher. 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
  • 48
    • 1842335131 scopus 로고    scopus 로고
    • Wray, L. V., Jr., A. E. Ferson, and S. H. Fisher. 1997. Expression of the Bacillus subtilis ureABC operon is controlled by multiple regulatory factors including CodY, GlnR, TnrA, and Spo0H. J. Bacteriol. 179:5494-5501.
    • Wray, L. V., Jr., A. E. Ferson, and S. H. Fisher. 1997. Expression of the Bacillus subtilis ureABC operon is controlled by multiple regulatory factors including CodY, GlnR, TnrA, and Spo0H. J. Bacteriol. 179:5494-5501.
  • 49
    • 9444233868 scopus 로고    scopus 로고
    • TnrA, a transcriptional factor required for global nitrogen regulation in Bacillus subtilis
    • Wray, L. V., Jr., A. E. Ferson, K. Rohrer, and S. H. Fisher. 1996. TnrA, a transcriptional 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
  • 50
    • 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 S. H. Fisher. 2005. A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in nitrogen- regulated gene expression. J. Biol. Chem. 280:33298-33304.
    • (2005) J. Biol. Chem , vol.280 , pp. 33298-33304
    • Wray Jr., L.V.1    Fisher, S.H.2
  • 51
    • 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 S. H. Fisher. 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
  • 52
    • 0028205413 scopus 로고
    • Catabolite repression of the Bacillus subtilis hut operon requires a cis -acting site located downstream of the transcription start site
    • Wray, L. V., Jr., F. K. Pettengill, and S. H. Fisher. 1994. Catabolite repression of the Bacillus subtilis hut operon requires a cis -acting site located downstream of the transcription start site. J. Bacteriol. 176:1894-1902.
    • (1994) J. Bacteriol , vol.176 , pp. 1894-1902
    • Wray Jr., L.V.1    Pettengill, F.K.2    Fisher, S.H.3
  • 53
    • 0032464364 scopus 로고    scopus 로고
    • Mutational analysis of the TnrA-binding sites in the Bacillus subtilis nrgAB and gabP promoter regions
    • Wray, L. V., Jr., J. M. Zalieckas, A. E. Ferson, and S. H. Fisher. 1998. Mutational analysis of the TnrA-binding sites in the Bacillus subtilis nrgAB and gabP promoter regions. J. Bacteriol. 180:2943-2949.
    • (1998) J. Bacteriol , vol.180 , pp. 2943-2949
    • Wray Jr., L.V.1    Zalieckas, J.M.2    Ferson, A.E.3    Fisher, S.H.4
  • 54
    • 0034733384 scopus 로고    scopus 로고
    • Purification and in vitro activities of the Bacillus subtilis TnrA transcription factor
    • Wray, L. V., Jr., J. M. Zalieckas, and S. H. Fisher. 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
  • 55
    • 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
  • 56
    • 0037709014 scopus 로고    scopus 로고
    • Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box
    • Yoshida, K., H. Yamaguchi, M. Kinehara, Y. Ohki, Y. Nakaura, and Y. Fujita. 2003. Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box. Mol. Microbiol. 49:157-165.
    • (2003) Mol. Microbiol , vol.49 , pp. 157-165
    • Yoshida, K.1    Yamaguchi, H.2    Kinehara, M.3    Ohki, Y.4    Nakaura, Y.5    Fujita, Y.6
  • 57
    • 33645215815 scopus 로고    scopus 로고
    • Cross-regulation of the Bacillus subtilis glnRA and tnrA genes provides evidence for DNA binding site discrimination by GlnR and TnrA
    • Zalieckas, J. M., L. V. Wray, Jr., and S. H. Fisher. 2006. Cross-regulation of the Bacillus subtilis glnRA and tnrA genes provides evidence for DNA binding site discrimination by GlnR and TnrA. 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.