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Volumn 181, Issue 20, 1999, Pages 6524-6529

Purification of P(II) and P(II)-UMP and in vitro studies of regulation of glutamine synthetase in Rhodospirillum rubrum

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; BACTERIAL PROTEIN; GLUTAMATE AMMONIA LIGASE; GLUTAMINE; PHOSPHATE; URIDINE DERIVATIVE;

EID: 0032692960     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.20.6524-6529.1999     Document Type: Article
Times cited : (8)

References (32)
  • 1
    • 0031824606 scopus 로고    scopus 로고
    • Role of the GlnK signal transduction protein in the regulation of nitrogen assimilation in Escherichia coli
    • Atkinson, M. R., and A. J. Ninfa. 1998. Role of the GlnK signal transduction protein in the regulation of nitrogen assimilation in Escherichia coli. Mol. Microbiol. 29:431-447.
    • (1998) Mol. Microbiol. , vol.29 , pp. 431-447
    • Atkinson, M.R.1    Ninfa, A.J.2
  • 2
    • 0025738922 scopus 로고
    • Purification and partial characterization of glutamate synthase from Rhodospirillum rubrum grown under nitrogen-fixing conditions
    • Carlberg, I., and S. Nordlund. 1991. Purification and partial characterization of glutamate synthase from Rhodospirillum rubrum grown under nitrogen-fixing conditions. Biochem. J. 279:151-154.
    • (1991) Biochem. J. , vol.279 , pp. 151-154
    • Carlberg, I.1    Nordlund, S.2
  • 3
    • 0031824693 scopus 로고    scopus 로고
    • Z of Azospirillum brasilense provide intracellular signalling for selective regulation of various nitrogen-dependent functions
    • Z of Azospirillum brasilense provide intracellular signalling for selective regulation of various nitrogen-dependent functions. Mol. Microbiol. 29:449-463.
    • (1998) Mol. Microbiol. , vol.29 , pp. 449-463
    • De Zamaroczy, M.1
  • 5
    • 0020453896 scopus 로고
    • The role of glutamine synthetase in the regulation of nitrogenase activity (switch-off effect) in Rhodospirillum rubrum
    • Falk, G., B. C. Johansson, and S. Nordlund. 1982. The role of glutamine synthetase in the regulation of nitrogenase activity (switch-off effect) in Rhodospirillum rubrum. Arch. Microbiol. 132:251-253.
    • (1982) Arch. Microbiol. , vol.132 , pp. 251-253
    • Falk, G.1    Johansson, B.C.2    Nordlund, S.3
  • 6
    • 0026003025 scopus 로고
    • Low- and high-activity forms of glutamine synthetase from Rhodospirillum rubrum: Sensitivity to feed-back effectors and activation of the low-activity form
    • Hammarström, A., A. Soliman, and S. Nordlund. 1991. Low- and high-activity forms of glutamine synthetase from Rhodospirillum rubrum: sensitivity to feed-back effectors and activation of the low-activity form. Biochim. Biophys. Acta 1080:259-263.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 259-263
    • Hammarström, A.1    Soliman, A.2    Nordlund, S.3
  • 7
    • 0015077320 scopus 로고
    • ATP: Glutamine synthetase adenylyltransferase from Escherichia coli: Purification and properties of a low-molecular weight enzyme form
    • Henning, S. B., and A. Ginsburg. 1971. ATP: glutamine synthetase adenylyltransferase from Escherichia coli: purification and properties of a low-molecular weight enzyme form. Arch. Biochem. Biophys. 144:611-627.
    • (1971) Arch. Biochem. Biophys. , vol.144 , pp. 611-627
    • Henning, S.B.1    Ginsburg, A.2
  • 8
    • 0030880188 scopus 로고    scopus 로고
    • The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction
    • Jaggi, R., W. C. van Heeswijk, H. V. Westerhoff, D. L. Ollis, and S. G. Vasudevan. 1997. The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction. EMBO J. 16:5562-5571.
    • (1997) EMBO J. , vol.16 , pp. 5562-5571
    • Jaggi, R.1    Van Heeswijk, W.C.2    Westerhoff, H.V.3    Ollis, D.L.4    Vasudevan, S.G.5
  • 9
    • 0032994344 scopus 로고    scopus 로고
    • Regulation of autophosphorylation of Escherichia coli nitrogen regulator II by the PII signal transduction protein
    • Jiang, P., and A. J. Ninfa. 1999. Regulation of autophosphorylation of Escherichia coli nitrogen regulator II by the PII signal transduction protein. J. Bacteriol. 181:1906-1911.
    • (1999) J. Bacteriol. , vol.181 , pp. 1906-1911
    • Jiang, P.1    Ninfa, A.J.2
  • 10
    • 0030743733 scopus 로고    scopus 로고
    • Structure/function analysis of the PII signal transduction protein of Escherichia coli: Genetic separation of interactions with protein receptors
    • Jiang, P., P. Zucker, M. R. Atkinson, E. S. Kamberov, W. Tirasophon, P. Chandran, B. R. Schefke, and A. J. Ninfa. 1997. Structure/function analysis of the PII signal transduction protein of Escherichia coli: genetic separation of interactions with protein receptors. J. Bacteriol. 179:4342-4353.
    • (1997) J. Bacteriol. , vol.179 , pp. 4342-4353
    • Jiang, P.1    Zucker, P.2    Atkinson, M.R.3    Kamberov, E.S.4    Tirasophon, W.5    Chandran, P.6    Schefke, B.R.7    Ninfa, A.J.8
  • 11
    • 0017752245 scopus 로고
    • Adenylylation/deadenylylation control of the glutamine synthetase of Rhodopseudomonas capsulata
    • Johansson, B. C., and H. Gest. 1977. Adenylylation/deadenylylation control of the glutamine synthetase of Rhodopseudomonas capsulata. Eur. J. Biochem. 81:365-371.
    • (1977) Eur. J. Biochem. , vol.81 , pp. 365-371
    • Johansson, B.C.1    Gest, H.2
  • 12
    • 0029882745 scopus 로고    scopus 로고
    • Transcription of the glnB and glnA genes in the photosynthetic bacterium Rhodospirillum rubrum
    • Johansson, M., and S. Nordlund. 1996. Transcription of the glnB and glnA genes in the photosynthetic bacterium Rhodospirillum rubrum. Microbiology 142:1265-1272.
    • (1996) Microbiology , vol.142 , pp. 1265-1272
    • Johansson, M.1    Nordlund, S.2
  • 13
    • 0030860684 scopus 로고    scopus 로고
    • Uridylylation of the PII protein in the photosynthetic bacterium Rhodospirillum rubrum
    • Johansson, M., and S. Nordlund. 1997. Uridylylation of the PII protein in the photosynthetic bacterium Rhodospirillum rubrum. J. Bacteriol. 179:4190-4194.
    • (1997) J. Bacteriol. , vol.179 , pp. 4190-4194
    • Johansson, M.1    Nordlund, S.2
  • 14
    • 0029051027 scopus 로고
    • The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP
    • Kamberov, E. S., M. R. Atkinson, and A. J. Ninfa. 1995. The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP. J. Biol. Chem. 270:17797-17807.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17797-17807
    • Kamberov, E.S.1    Atkinson, M.R.2    Ninfa, A.J.3
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0018171365 scopus 로고
    • Purification and properties of nitrogenase from Rhodospirillum rubrum and evidence for phosphate, ribose and an adenine-like unit covalently bound to the iron protein
    • Ludden, P. W., and R. H. Burris. 1978. Purification and properties of nitrogenase from Rhodospirillum rubrum and evidence for phosphate, ribose and an adenine-like unit covalently bound to the iron protein. Biochem. J. 175: 251-259.
    • (1978) Biochem. J. , vol.175 , pp. 251-259
    • Ludden, P.W.1    Burris, R.H.2
  • 17
    • 0024832910 scopus 로고
    • Regulation of nitrogenase activity by reversible ADP-ribosylation
    • Ludden, P. W., and G. P. Roberts. 1989. Regulation of nitrogenase activity by reversible ADP-ribosylation. Curr. Top. Cell. Regul. 30:23-55.
    • (1989) Curr. Top. Cell. Regul. , vol.30 , pp. 23-55
    • Ludden, P.W.1    Roberts, G.P.2
  • 18
    • 0031779083 scopus 로고    scopus 로고
    • Characterization of the glnK-amtB operon of Azotobacter vinelandii
    • Meletzus, D., P. Rudnick, N. Doetsch, A. Green, and C. Kennedy. 1998. Characterization of the glnK-amtB operon of Azotobacter vinelandii. J. Bacteriol. 180:3260-3264.
    • (1998) J. Bacteriol. , vol.180 , pp. 3260-3264
    • Meletzus, D.1    Rudnick, P.2    Doetsch, N.3    Green, A.4    Kennedy, C.5
  • 19
    • 0031849423 scopus 로고    scopus 로고
    • Characterisation of the glnK-amtB operon and the involvement of AmtB in methylammonium uptake in Azorhizobium caulinodans
    • Michel-Reydellet, N., N. Desnoues, M. de Zamaroczy, C. Elmerich, and P. A. Kaminski. 1998. Characterisation of the glnK-amtB operon and the involvement of AmtB in methylammonium uptake in Azorhizobium caulinodans. Mol. Gen. Genet. 258:671-677.
    • (1998) Mol. Gen. Genet. , vol.258 , pp. 671-677
    • Michel-Reydellet, N.1    Desnoues, N.2    De Zamaroczy, M.3    Elmerich, C.4    Kaminski, P.A.5
  • 20
    • 0021929167 scopus 로고
    • Properties and regulation of glutamine synthetase from Rhodospirillum rubrum
    • Nordlund, S., R. H. Kanemoto, S. A. Murrell, and P. W. Ludden. 1985. Properties and regulation of glutamine synthetase from Rhodospirillum rubrum. J. Bacteriol. 161:13-17.
    • (1985) J. Bacteriol. , vol.161 , pp. 13-17
    • Nordlund, S.1    Kanemoto, R.H.2    Murrell, S.A.3    Ludden, P.W.4
  • 21
    • 0031721765 scopus 로고    scopus 로고
    • Expression of glnB and a glnB-like gene (glnK) in a ribulose bisphosphate carboxylase/oxygenase-deficient mutant of Rhodobacter sphaeroides
    • Qian, Y., and F. R. Tabita. 1998. Expression of glnB and a glnB-like gene (glnK) in a ribulose bisphosphate carboxylase/oxygenase-deficient mutant of Rhodobacter sphaeroides. J. Bacteriol. 180:4644-4649.
    • (1998) J. Bacteriol. , vol.180 , pp. 4644-4649
    • Qian, Y.1    Tabita, F.R.2
  • 22
    • 0024569342 scopus 로고
    • Regulation of Escherichia coli glutamine synthetase
    • Rhee, S. G., P. B. Chock, and E. R. Stadtman. 1989. Regulation of Escherichia coli glutamine synthetase. Adv. Enzymol. 62:37-92.
    • (1989) Adv. Enzymol. , vol.62 , pp. 37-92
    • Rhee, S.G.1    Chock, P.B.2    Stadtman, E.R.3
  • 23
    • 0018236966 scopus 로고
    • IID regulatory protein, uridylyltransferase, and uridylyl-removing enzyme in glutamine synthetase cascade
    • IID regulatory protein, uridylyltransferase, and uridylyl-removing enzyme in glutamine synthetase cascade. Anal. Biochem. 90:752-766.
    • (1978) Anal. Biochem. , vol.90 , pp. 752-766
    • Rhee, S.G.1    Huang, G.Y.2    Chock, P.B.3    Stadtman, E.R.4
  • 25
    • 0024959491 scopus 로고
    • Purification and partial characterization of glutamine synthetase from the photosynthetic bacterium Rhodospirillum rubrum
    • Soliman, A., and S. Nordlund. 1989. Purification and partial characterization of glutamine synthetase from the photosynthetic bacterium Rhodospirillum rubrum. Biochim. Biophys. Acta 994:138-141.
    • (1989) Biochim. Biophys. Acta , vol.994 , pp. 138-141
    • Soliman, A.1    Nordlund, S.2
  • 26
    • 0023664544 scopus 로고
    • Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII protein and nucleotide sequence of its structural gene
    • Son, H. S., and S. G. Rhee. 1987. Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII protein and nucleotide sequence of its structural gene. J. Biol. Chem. 262:8690-8695.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8690-8695
    • Son, H.S.1    Rhee, S.G.2
  • 27
    • 0018406441 scopus 로고
    • Enzymic procedures for determining the average state of adenylylation of Escherichia coli glutamine synthetase
    • Stadtman, E. R., P. Z. Smyrniotis, J. N. Davis, and M. E. Wittenberger. 1979. Enzymic procedures for determining the average state of adenylylation of Escherichia coli glutamine synthetase. Anal. Biochem. 95:275-285.
    • (1979) Anal. Biochem. , vol.95 , pp. 275-285
    • Stadtman, E.R.1    Smyrniotis, P.Z.2    Davis, J.N.3    Wittenberger, M.E.4
  • 28
    • 0009482260 scopus 로고
    • Electrophoretic transfer from polyacrylamide gels to nitrocellulose sheet: Procedure and some applications
    • Towbin, H. T., T. Staehlin, and J. Gordon. 1979. Electrophoretic transfer from polyacrylamide gels to nitrocellulose sheet: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.T.1    Staehlin, T.2    Gordon, J.3
  • 30
    • 0027281747 scopus 로고
    • The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli
    • van Heeswijk, W. C., M. Rabenberg, H. V. Westernoff, and D. Kahn. 1993. The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli. Mol. Microbiol. 9:443-457.
    • (1993) Mol. Microbiol. , vol.9 , pp. 443-457
    • Van Heeswijk, W.C.1    Rabenberg, M.2    Westernoff, H.V.3    Kahn, D.4
  • 32
    • 0025045391 scopus 로고
    • ATP-dependent and NAD-dependent modification of glutamine synthetase from Rhodospirillum rubrum in vitro
    • Woehle, D. L., B. A. Lueddecke, and P. W. Ludden. 1990. ATP-dependent and NAD-dependent modification of glutamine synthetase from Rhodospirillum rubrum in vitro. J. Biol. Chem. 265:13741-13749.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13741-13749
    • Woehle, D.L.1    Lueddecke, B.A.2    Ludden, P.W.3


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