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Volumn 187, Issue 21, 2005, Pages 7481-7491

Biochemical and mutational analysis of glutamine synthetase type III from the rumen anaerobe Ruminococcus albus 8

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; GAMMA GLUTAMYLTRANSFERASE; GLUTAMATE AMMONIA LIGASE; GLUTAMATE AMMONIA LIGASE III; MESSENGER RNA; MONOMER; OLIGOMER; UNCLASSIFIED DRUG;

EID: 27144437574     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.21.7481-7491.2005     Document Type: Article
Times cited : (28)

References (35)
  • 1
    • 0033953222 scopus 로고    scopus 로고
    • Critical factors influencing the recovery and integrity of rRNA extracted from environmental samples: Use of an optimized protocol to measure depth-related biomass distribution in freshwater sediments
    • Alm, E. W., and D. A. Stahl. 2000. Critical factors influencing the recovery and integrity of rRNA extracted from environmental samples: use of an optimized protocol to measure depth-related biomass distribution in freshwater sediments. J. Microbiol. Methods 40:153-162.
    • (2000) J. Microbiol. Methods , vol.40 , pp. 153-162
    • Alm, E.W.1    Stahl, D.A.2
  • 2
    • 0022776515 scopus 로고
    • Novel subunit-subunit interaction in the structure of glutamine synthetase
    • Almassy, R. J., C. A. Janson, R. Hamlin, N.-H. Xuong, and D. Eisenberg. 1986. Novel subunit-subunit interaction in the structure of glutamine synthetase. Nature 323:304-309.
    • (1986) Nature , vol.323 , pp. 304-309
    • Almassy, R.J.1    Janson, C.A.2    Hamlin, R.3    Xuong, N.-H.4    Eisenberg, D.5
  • 3
    • 0037333775 scopus 로고    scopus 로고
    • Characterization of the gene encoding glutamate dehydrogenase (gdhA) from the ruminai bacterium Ruminococcus flavefaciens FD-1
    • Antonopoulos, D. A., R. I. Aminov, P. A. Duncan, B. A. White, and R. I. Mackie. 2003. Characterization of the gene encoding glutamate dehydrogenase (gdhA) from the ruminai bacterium Ruminococcus flavefaciens FD-1. Arch. Microbiol. 179:184-190.
    • (2003) Arch. Microbiol. , vol.179 , pp. 184-190
    • Antonopoulos, D.A.1    Aminov, R.I.2    Duncan, P.A.3    White, B.A.4    Mackie, R.I.5
  • 5
    • 0000386558 scopus 로고    scopus 로고
    • Analysis of RNA by Northern and slot blot hybridization
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). Wiley, New York, N.Y.
    • Brown, T., and K. Mackey. 1997. Analysis of RNA by Northern and slot blot hybridization, p.4.9.1-4.9.16. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, vol. 1. Wiley, New York, N.Y.
    • (1997) Current Protocols in Molecular Biology , vol.1
    • Brown, T.1    Mackey, K.2
  • 6
    • 0035093865 scopus 로고    scopus 로고
    • Biochemical analysis of replication factor C from the hyperthermophilic archaeon Pyrococcus furiosus
    • Cann, I. K. O., S. Ishino, M. Yuasa, H. Daiyasu, H. Tab, and Y. Ishino. 2001. Biochemical analysis of replication factor C from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 183:2614-2623.
    • (2001) J. Bacteriol. , vol.183 , pp. 2614-2623
    • Cann, I.K.O.1    Ishino, S.2    Yuasa, M.3    Daiyasu, H.4    Tab, H.5    Ishino, Y.6
  • 7
    • 0002030661 scopus 로고    scopus 로고
    • Polysaccharide degradation by rumen microorganisms
    • P. N. Hobson and C. S. Stewart (ed.). Blackie Academic & Professional, New York, N.Y.
    • Chesson, A., and C. W. Forsberg. 1997. Polysaccharide degradation by rumen microorganisms, p. 329-381. In P. N. Hobson and C. S. Stewart (ed.), The rumen microbial ecosystem, 2nd ed. Blackie Academic & Professional, New York, N.Y.
    • (1997) The Rumen Microbial Ecosystem, 2nd Ed. , pp. 329-381
    • Chesson, A.1    Forsberg, C.W.2
  • 8
    • 0037083882 scopus 로고    scopus 로고
    • Membrane sequestration of the signal transduction protein GlnK by the ammonium transporter AmtB
    • Coutts, G., G. Thomas, D. Blakey, and M. Merrick. 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
  • 9
    • 0031770178 scopus 로고    scopus 로고
    • Nitrogen control of the glnN gene that codes for GS type III, the only glutamine synthetase in the cyanobacterium Pseudanabaena sp. PCC 6903
    • Crespo, J. L., M. Garcia-Dominguez, and F. J. Florencio. 1998. Nitrogen control of the glnN gene that codes for GS type III, the only glutamine synthetase in the cyanobacterium Pseudanabaena sp. PCC 6903. Mol. Microbiol. 30:1101-1112.
    • (1998) Mol. Microbiol. , vol.30 , pp. 1101-1112
    • Crespo, J.L.1    Garcia-Dominguez, M.2    Florencio, F.J.3
  • 10
    • 0017660968 scopus 로고
    • Two forms of glutamine synthetase in free-living root-nodule bacteria
    • Darrow, R. A., and R. R. Knotts. 1977. Two forms of glutamine synthetase in free-living root-nodule bacteria. Biochem. Biophys. Res. Commun. 78:554-559.
    • (1977) Biochem. Biophys. Res. Commun. , vol.78 , pp. 554-559
    • Darrow, R.A.1    Knotts, R.R.2
  • 11
    • 8744262953 scopus 로고    scopus 로고
    • Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein
    • Das, A., L. Rajagopalan, V. S. Mathura, S. J. Rigby, S. Mitra, and T. K. Hazra. 2004. Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein. J. Biol. Chem. 279:47132-47138.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47132-47138
    • Das, A.1    Rajagopalan, L.2    Mathura, V.S.3    Rigby, S.J.4    Mitra, S.5    Hazra, T.K.6
  • 12
    • 0026462830 scopus 로고
    • Purification and properties of NADP-dependent glutamate dehydrogenase from Ruminococcus flavefaciens FD-1
    • Duncan, P. A., B. A. White, and R. I. Mackie. 1992. Purification and properties of NADP-dependent glutamate dehydrogenase from Ruminococcus flavefaciens FD-1. Appl. Environ. Microbiol. 58:4032-4037.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 4032-4037
    • Duncan, P.A.1    White, B.A.2    Mackie, R.I.3
  • 13
    • 0344521379 scopus 로고
    • Ph.D. dissertation. Department of Animal Sciences, University of Illinois, Urbana-Champaign
    • Duncan, P. A. 1993. Ammonia assimilation by Ruminococcus flavefaciens FD-1. Ph.D. dissertation. Department of Animal Sciences, University of Illinois, Urbana-Champaign.
    • (1993) Ammonia Assimilation by Ruminococcus Flavefaciens FD-1
    • Duncan, P.A.1
  • 14
    • 0001190087 scopus 로고    scopus 로고
    • Polysaccharide degradation in the rumen and large intestine
    • R. I. Mackie and B. A. White (ed.). Chapman and Hall, New York, N.Y.
    • Forsberg, C. W., K.-J. Cheng, and B. A. White. 1997. Polysaccharide degradation in the rumen and large intestine, p. 319-379. In R. I. Mackie and B. A. White (ed.), Gastrointestinal microbiology, vol. 1. Chapman and Hall, New York, N.Y.
    • (1997) Gastrointestinal Microbiology , vol.1 , pp. 319-379
    • Forsberg, C.W.1    Cheng, K.-J.2    White, B.A.3
  • 15
    • 0031051869 scopus 로고    scopus 로고
    • Purification and characterization of a new type of glutamine synthetase from cyanobacteria
    • Garcia-Dominguez, M., J. C. Reyes, and F. J. Florencio. 1997. Purification and characterization of a new type of glutamine synthetase from cyanobacteria. Eur. J. Biochem. 244:258-264.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 258-264
    • Garcia-Dominguez, M.1    Reyes, J.C.2    Florencio, F.J.3
  • 16
    • 0024851296 scopus 로고
    • Molecular analysis of a novel glutamine synthetase of the anaerobe Bacteroides fragilis
    • Hill, R. T., J. R. Parker, H. J. Goodman, D. T. Jones, and D. R. Woods. 1989. Molecular analysis of a novel glutamine synthetase of the anaerobe Bacteroides fragilis. J. Gen. Microbiol. 135:3271-3279.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 3271-3279
    • Hill, R.T.1    Parker, J.R.2    Goodman, H.J.3    Jones, D.T.4    Woods, D.R.5
  • 18
    • 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
  • 19
    • 77956944529 scopus 로고
    • Glutamine synthetase of mammals
    • P. D. Boyer (ed.). Academic Press, Inc., New York, N.Y.
    • Meister, A. 1974. Glutamine synthetase of mammals, p. 699-754. In P. D. Boyer (ed.), The enzymes, vol. 10. Academic Press, Inc., New York, N.Y.
    • (1974) The Enzymes , vol.10 , pp. 699-754
    • Meister, A.1
  • 20
    • 0025361926 scopus 로고
    • Purification and properties of glutamine synthetases from the cyanobacteria Synechocystis sp. strain PCC 6803 and Calothrix sp. strain PCC 7601
    • Mérida, A., L. Leurentop, P. Candau, and F. J. Florencio. 1990. Purification and properties of glutamine synthetases from the cyanobacteria Synechocystis sp. strain PCC 6803 and Calothrix sp. strain PCC 7601. J. Bacteriol. 172:4732-4735.
    • (1990) J. Bacteriol. , vol.172 , pp. 4732-4735
    • Mérida, A.1    Leurentop, L.2    Candau, P.3    Florencio, F.J.4
  • 22
    • 0013604747 scopus 로고    scopus 로고
    • Preparation of bacterial RNA
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). Wiley, New York, N.Y.
    • Reddy, K. J., and M. Gilman. 1997. Preparation of bacterial RNA, p. 4.4.1-4.4.7. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, vol. 1. Wiley, New York, N.Y.
    • (1997) Current Protocols in Molecular Biology , vol.1
    • Reddy, K.J.1    Gilman, M.2
  • 23
    • 0014301095 scopus 로고
    • Effects of specific divalent cations on some physical and chemical properties of glutamine synthetase from Escherichia coli: Taut and relaxed enzyme forms
    • Shapiro, B. M., and A. Ginsburg. 1968. Effects of specific divalent cations on some physical and chemical properties of glutamine synthetase from Escherichia coli: taut and relaxed enzyme forms. Biochemistry 7:2153-2167.
    • (1968) Biochemistry , vol.7 , pp. 2153-2167
    • Shapiro, B.M.1    Ginsburg, A.2
  • 24
    • 0003185856 scopus 로고    scopus 로고
    • The rumen bacteria
    • P. N. Hobson and C. S. Stewart (ed.). Blackie Academic & Professional, London, England
    • Stewart, C. S., H. J. Flint, and M. P. Bryant. 1997. The rumen bacteria, p. 10-72. In P. N. Hobson and C. S. Stewart (ed.), The rumen microbial ecosystem, 2nd ed. Blackie Academic & Professional, London, England.
    • (1997) The Rumen Microbial Ecosystem, 2nd Ed. , pp. 10-72
    • Stewart, C.S.1    Flint, H.J.2    Bryant, M.P.3
  • 25
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 26
    • 0014301425 scopus 로고
    • Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli
    • Valentine, R. C., B. M. Shapiro, and E. R. Stadtman. 1968. Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli Biochemistry 7:2143-2152.
    • (1968) Biochemistry , vol.7 , pp. 2143-2152
    • Valentine, R.C.1    Shapiro, B.M.2    Stadtman, E.R.3
  • 27
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., M. Saraste, M. J. Runswick, and N. J. Gay. 1982. Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 28
    • 0002634307 scopus 로고    scopus 로고
    • Metabolism of nitrogen-containing compounds
    • P. N. Hobson and C. S. Stewart (ed.). Blackie Academic & Professional, New York, N. Y.
    • Wallace, R. J., R. Onodera, and M. A. Cotta. 1997. Metabolism of nitrogen-containing compounds, p. 283-328. In P. N. Hobson and C. S. Stewart (ed.), The rumen microbial ecosystem, 2nd ed. Blackie Academic & Professional, New York, N. Y.
    • (1997) The Rumen Microbial Ecosystem, 2nd Ed. , pp. 283-328
    • Wallace, R.J.1    Onodera, R.2    Cotta, M.A.3
  • 29
    • 0344740009 scopus 로고    scopus 로고
    • 14 is a family III enzyme (GlnN) and glutamine supports growth of mutants lacking glutamate dehydrogenase activity
    • 14 is a family III enzyme (GlnN) and glutamine supports growth of mutants lacking glutamate dehydrogenase activity. FEMS Microbiol. Lett. 229:15-21.
    • (2003) FEMS Microbiol. Lett. , vol.229 , pp. 15-21
    • Wen, Z.T.1    Peng, L.2    Morrison, M.3
  • 30
    • 0001279038 scopus 로고    scopus 로고
    • Preparation of genomic DNA from bacteria
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). Wiley, New York, N.Y.
    • Wilson, K. 1997. Preparation of genomic DNA from bacteria, p.2.4.1-2.4.5. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, vol. 1. Wiley, New York, N.Y.
    • (1997) Current Protocols in Molecular Biology , vol.1
    • Wilson, K.1
  • 31
    • 0001768395 scopus 로고    scopus 로고
    • Microbe-microbe interactions
    • P. N. Hobson and C. S. Stewart (ed.). Blackie Academic & Professional, New York, N.Y.
    • Wolin, M. J., and T. L. Miller. 1997. Microbe-microbe interactions, p. 467-491. In P. N. Hobson and C. S. Stewart (ed.), The rumen microbial ecosystem, 2nd ed. Blackie Academic & Professional, New York, N.Y.
    • (1997) The Rumen Microbial Ecosystem, 2nd Ed. , pp. 467-491
    • Wolin, M.J.1    Miller, T.L.2
  • 32
    • 0014028924 scopus 로고
    • Regulation of glutamine synthetase. I. Purification and properties of glutamine synthetase from Escherichia coli
    • Woolfolk, C. A., B. Shapiro, and E. R. Stadtman. 1966. Regulation of glutamine synthetase. I. Purification and properties of glutamine synthetase from Escherichia coli. Arch. Biochem. Biophys. 116:177-192.
    • (1966) Arch. Biochem. Biophys. , vol.116 , pp. 177-192
    • Woolfolk, C.A.1    Shapiro, B.2    Stadtman, E.R.3
  • 33
    • 0014143855 scopus 로고
    • Regulation of glutamine synthetase. IV. Reversible dissociation and inactivation of glutamine synthetase from Escherichia coli by the concerted action of EDTA and urea
    • Woolfolk, C. A., and E. R. Stadtman. 1967. Regulation of glutamine synthetase. IV. Reversible dissociation and inactivation of glutamine synthetase from Escherichia coli by the concerted action of EDTA and urea. Arch. Biochem. Biophys. 122:174-189.
    • (1967) Arch. Biochem. Biophys. , vol.122 , pp. 174-189
    • Woolfolk, C.A.1    Stadtman, E.R.2
  • 35
    • 0035142543 scopus 로고    scopus 로고
    • Purification and characterization of glutamine synthetase from the unicellular cyanobacterium Synechococcus RF-1
    • Yuan, H., C. Wang, and H. Kung. 2001. Purification and characterization of glutamine synthetase from the unicellular cyanobacterium Synechococcus RF-1. Bot. Bull. Acad. Sin. 42:23-33.
    • (2001) Bot. Bull. Acad. Sin. , vol.42 , pp. 23-33
    • Yuan, H.1    Wang, C.2    Kung, H.3


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