메뉴 건너뛰기




Volumn 152, Issue 4, 1999, Pages 1343-1351

Genetics of nitrogen regulation in Methanococcus maripaludis

Author keywords

[No Author keywords available]

Indexed keywords

NITROGEN;

EID: 0344289523     PISSN: 00166731     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (65)

References (55)
  • 1
    • 0029804967 scopus 로고    scopus 로고
    • Neomycin resistance as a selectable marker in Methanococcus maripaludis
    • ARGYLE, J. L., D. L. TUMBULA and J. A. LEIGH, 1996 Neomycin resistance as a selectable marker in Methanococcus maripaludis. Appl. Environ. Microbiol. 62: 4233-4237.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4233-4237
    • Argyle, J.L.1    Tumbula, D.L.2    Leigh, J.A.3
  • 2
    • 0029743218 scopus 로고    scopus 로고
    • Modulation of NifA activity by PII in Azospirillum brasilense: Evidence for a regulatory role of the NifA N-terminal domain
    • ARSENE, F., P. A. KAMINSKI and C. ELMERICH, 1996 Modulation of NifA activity by PII in Azospirillum brasilense: evidence for a regulatory role of the NifA N-terminal domain. J. Bacteriol. 178: 4830-4838.
    • (1996) J. Bacteriol. , vol.178 , pp. 4830-4838
    • Arsene, F.1    Kaminski, P.A.2    Elmerich, C.3
  • 3
    • 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
  • 4
    • 0021714067 scopus 로고
    • Dinitrogen fixation by a thermophilic methanogenic bacterium
    • BELAY, N., R. SPARLING and L. DANIELS, 1984 Dinitrogen fixation by a thermophilic methanogenic bacterium. Nature 312: 286-288.
    • (1984) Nature , vol.312 , pp. 286-288
    • Belay, N.1    Sparling, R.2    Daniels, L.3
  • 5
    • 0028785817 scopus 로고
    • Genetics in methanogens: Transposon insertion mutagenesis of a Methanococcus maripaludis nifH gene
    • BLANK, C. E., P. S. KESSLER and J. A. LEIGH, 1995 Genetics in methanogens: transposon insertion mutagenesis of a Methanococcus maripaludis nifH gene. J. Bacteriol. 177: 5773-5777.
    • (1995) J. Bacteriol. , vol.177 , pp. 5773-5777
    • Blank, C.E.1    Kessler, P.S.2    Leigh, J.A.3
  • 6
    • 85069257187 scopus 로고    scopus 로고
    • Nitrogen state regulation and osmolyte production in the methanogenic archaeon Methanosarcina barkeri 227
    • Abstracts, Atlanta
    • BRABBAN, A. D., and S. H. ZINDER, 1998 Nitrogen state regulation and osmolyte production in the methanogenic archaeon Methanosarcina barkeri 227, pp. 316 in Abstracts, 98th General Meeting of the American Society for Microbiology, Atlanta.
    • (1998) 98th General Meeting of the American Society for Microbiology , pp. 316
    • Brabban, A.D.1    Zinder, S.H.2
  • 7
    • 0028308478 scopus 로고
    • Evolutionary relationships of bacterial and archaeal glutamine synthetase genes
    • BROWN, J. R., Y. MASUCHI, F. T. ROBB and W. F. DOOLITTLE, 1994 Evolutionary relationships of bacterial and archaeal glutamine synthetase genes. J. Mol. Evol. 38: 566-576.
    • (1994) J. Mol. Evol. , vol.38 , pp. 566-576
    • Brown, J.R.1    Masuchi, Y.2    Robb, F.T.3    Doolittle, W.F.4
  • 8
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • BULT, C. J., O. WHITE, G. J. OLSEN, L. ZHOU, R. D. FLEISCHMANN et al., 1996 Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273: 1058-1073.
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1    White, O.2    Olsen, G.J.3    Zhou, L.4    Fleischmann, R.D.5
  • 9
    • 0030040863 scopus 로고    scopus 로고
    • X-ray structure of the signal transduction protein PII from Escherichia coli at 1.9Å
    • CARR, P. D., E. CHEAH, P. M. SUFFOLK, S. G. VASUDEVAN, N. E. DIXON et al., 1996 X-ray structure of the signal transduction protein PII from Escherichia coli at 1.9Å. Acta Crystallogr. Sect. D 52: 93-104.
    • (1996) Acta Crystallogr. Sect. D , vol.52 , pp. 93-104
    • Carr, P.D.1    Cheah, E.2    Suffolk, P.M.3    Vasudevan, S.G.4    Dixon, N.E.5
  • 10
    • 0030047955 scopus 로고    scopus 로고
    • Cloning, functional organization, transcript studies, and phylogenetic analysis of the complete nitrogenase structural genes (nifHDK2) and associated genes in the Archaeon Methanosarcina barkeri
    • CHIEN, Y., and S. H. ZINDER, 1996 Cloning, functional organization, transcript studies, and phylogenetic analysis of the complete nitrogenase structural genes (nifHDK2) and associated genes in the Archaeon Methanosarcina barkeri. J. Bacteriol. 178: 143-148.
    • (1996) J. Bacteriol. , vol.178 , pp. 143-148
    • Chien, Y.1    Zinder, S.H.2
  • 11
    • 0031948599 scopus 로고    scopus 로고
    • 2- and ammonium-grown cells of the archaeon Methanosarcina barkeri 227
    • 2- and ammonium-grown cells of the archaeon Methanosarcina barkeri 227. J. Bacteriol. 180: 2723-2728.
    • (1998) J. Bacteriol. , vol.180 , pp. 2723-2728
    • Chien, Y.1    Helmann, J.D.2    Zinder, S.H.3
  • 12
    • 0031019644 scopus 로고    scopus 로고
    • Transcriptional regulation in Archaea: In vivo demonstration of a repressor binding site in a methanogen
    • COHEN-KUPIEC, R., C. BLANK and J. A. LEIGH, 1997 Transcriptional regulation in Archaea: in vivo demonstration of a repressor binding site in a methanogen. Proc. Natl. Acad. Sci. USA 94: 1316-1320.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1316-1320
    • Cohen-Kupiec, R.1    Blank, C.2    Leigh, J.A.3
  • 13
    • 0032899732 scopus 로고    scopus 로고
    • Function and regulation of glnA in the methanogenic archaeon Methanococcus maripaludis
    • COHEN-KUPIEC, R., C. J. MARX and J. A. LEIGH, 1999 Function and regulation of glnA in the methanogenic archaeon Methanococcus maripaludis. J. Bacteriol. 181: 256-261.
    • (1999) J. Bacteriol. , vol.181 , pp. 256-261
    • Cohen-Kupiec, R.1    Marx, C.J.2    Leigh, J.A.3
  • 14
    • 0002405741 scopus 로고
    • Biochemical genetics of nitrogenase
    • edited by G. STACEY, R. H. BURRIS and H. J. EVANS. Chapman & Hall, New York
    • DEAN, D. R., and M. R. JACOBSON, 1992 Biochemical genetics of nitrogenase, pp. 763-834 in Biological Nitrogen Fixation, edited by G. STACEY, R. H. BURRIS and H. J. EVANS. Chapman & Hall, New York.
    • (1992) Biological Nitrogen Fixation , pp. 763-834
    • Dean, D.R.1    Jacobson, M.R.2
  • 15
    • 0027494834 scopus 로고
    • Nitrogenase metalloclusters: Structures, organization, and synthesis
    • DEAN, D. R., J. T. BOLIN and L. ZHENG, 1993 Nitrogenase metalloclusters: structures, organization, and synthesis. J. Bacteriol. 175: 6737-6744.
    • (1993) J. Bacteriol. , vol.175 , pp. 6737-6744
    • Dean, D.R.1    Bolin, J.T.2    Zheng, L.3
  • 16
    • 0013609540 scopus 로고    scopus 로고
    • Regulatory roles of the structural homologues PII and PZ proteins in Azospririllum brasilense
    • edited by C. ELMERICH, A. KONDOROSI and W. E. NEWTON. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • DE ZAMAROCZY, M., and C. ELMERICH, 1998 Regulatory roles of the structural homologues PII and PZ proteins in Azospririllum brasilense, pp. 111-114 in Biological Nitrogen Fixation for the 21st Century, edited by C. ELMERICH, A. KONDOROSI and W. E. NEWTON. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1998) Biological Nitrogen Fixation for the 21st Century , pp. 111-114
    • De Zamaroczy, M.1    Elmerich, C.2
  • 17
    • 0025305971 scopus 로고
    • Construction of an integration vector for use in the archaebacterium Methanococcus voltae and expression of a eubacterial resistance gene
    • GERNHARDT, P., O. POSSOT, M. FOGLINO, L. SIBOLD and A. KLEIN, 1990 Construction of an integration vector for use in the archaebacterium Methanococcus voltae and expression of a eubacterial resistance gene. Mol. Gen. Genet. 221: 273-279.
    • (1990) Mol. Gen. Genet. , vol.221 , pp. 273-279
    • Gernhardt, P.1    Possot, O.2    Foglino, M.3    Sibold, L.4    Klein, A.5
  • 18
    • 0032428697 scopus 로고    scopus 로고
    • Physiological role for the GInK protein of enteric bacteria: Relief of NifL inhibition under nitrogen-limiting conditions
    • HE, L., E. SOUPENE, A. NINFA and S. KUSTU, 1998 Physiological role for the GInK protein of enteric bacteria: relief of NifL inhibition under nitrogen-limiting conditions. J. Bacteriol. 180: 6661-6667.
    • (1998) J. Bacteriol. , vol.180 , pp. 6661-6667
    • He, L.1    Soupene, E.2    Ninfa, A.3    Kustu, S.4
  • 19
    • 0033061058 scopus 로고    scopus 로고
    • The signal transduction protein GlnK is required for NifL-dependent nitrogen control of nifgene expression in Klebsiella pneumoniae
    • JACK, R., M. DE ZAMAROCZY and M. MERRICK, 1999 The signal transduction protein GlnK is required for NifL-dependent nitrogen control of nifgene expression in Klebsiella pneumoniae. J. Bacteriol. 181: 1156-1162.
    • (1999) J. Bacteriol. , vol.181 , pp. 1156-1162
    • Jack, R.1    De Zamaroczy, M.2    Merrick, M.3
  • 20
    • 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 et al., 1997a 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
  • 21
    • 0030808284 scopus 로고    scopus 로고
    • Probing interactions of the homotrimeric PII signal transduction protein with its receptors by use of PII heterotrimers formed in vitro from wild-type and mutant subunits
    • JIANG, P., P. ZUCKER and A. J. NINFA, 1997b Probing interactions of the homotrimeric PII signal transduction protein with its receptors by use of PII heterotrimers formed in vitro from wild-type and mutant subunits. J. Bacteriol. 179: 4354-4360.
    • (1997) J. Bacteriol. , vol.179 , pp. 4354-4360
    • Jiang, P.1    Zucker, P.2    Ninfa, A.J.3
  • 22
    • 0032530304 scopus 로고    scopus 로고
    • Enzymological characterization of the signal-transducing uridylyltransferase/uridylyl-removing enzyme (EC 2.7.7.59) of Ecscherichia coli and its interaction with the PII protein
    • JIANG, P., J. A. PELISKA and A.J. NINFA, 1998a Enzymological characterization of the signal-transducing uridylyltransferase/uridylyl-removing enzyme (EC 2.7.7.59) of Ecscherichia coli and its interaction with the PII protein. Biochemistry 37: 12782-12794.
    • (1998) Biochemistry , vol.37 , pp. 12782-12794
    • Jiang, P.1    Peliska, J.A.2    Ninfa, A.J.3
  • 23
    • 0032530305 scopus 로고    scopus 로고
    • Reconstitution of the signal-transduction bicyclic cascade responsible for the regulation of Ntr gene transcription in Escherichia coli
    • JIANG, P., J. A. PELISKA and A. J. NINFA, 1998b Reconstitution of the signal-transduction bicyclic cascade responsible for the regulation of Ntr gene transcription in Escherichia coli. Biochemistry 37: 12795-12801.
    • (1998) Biochemistry , vol.37 , pp. 12795-12801
    • Jiang, P.1    Peliska, J.A.2    Ninfa, A.J.3
  • 24
    • 0032530281 scopus 로고    scopus 로고
    • The regulation of Escherichia coli glutamine synthetase revisited: Role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state
    • JIANG, P., J. A. PELISKA and A. J. NINFA, 1998c The regulation of Escherichia coli glutamine synthetase revisited: role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state. Biochemistry 37: 12802-12810.
    • (1998) Biochemistry , vol.37 , pp. 12802-12810
    • Jiang, P.1    Peliska, J.A.2    Ninfa, A.J.3
  • 25
    • 0032579989 scopus 로고    scopus 로고
    • Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3
    • KAWARABAYASI, Y., M. SAWADA, H. HORIKAWA, Y. HAIKAWA, Y. HINO et al., 1998 Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3. DNA Res. 5: 55-76.
    • (1998) DNA Res. , vol.5 , pp. 55-76
    • Kawarabayasi, Y.1    Sawada, M.2    Horikawa, H.3    Haikawa, Y.4    Hino, Y.5
  • 26
    • 0031895257 scopus 로고    scopus 로고
    • The nif gene operon of the methanogenic archaeon Methanococcus maripaludis
    • KESSLER, P. S., C. BLANK and J. A. LEIGH, 1998 The nif gene operon of the methanogenic archaeon Methanococcus maripaludis. J. Bacteriol. 180: 1504-1511.
    • (1998) J. Bacteriol. , vol.180 , pp. 1504-1511
    • Kessler, P.S.1    Blank, C.2    Leigh, J.A.3
  • 27
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
    • KLENK, H. P., R. A. CLAYTON, J. F. TOMB, O. WHITE, K. E. NELSON et al., 1997 The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390: 364-370.
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.P.1    Clayton, R.A.2    Tomb, J.F.3    White, O.4    Nelson, K.E.5
  • 28
    • 0033119587 scopus 로고    scopus 로고
    • Transcriptional regulation in Archaea
    • LEIGH, J. A., 1999 Transcriptional regulation in Archaea. Curr. Opin. Microbiol. 2: 131-134.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 131-134
    • Leigh, J.A.1
  • 29
    • 0025718763 scopus 로고
    • Mutations in the draT and draG genes of Rhodospirillum rubrum result in loss of regulation of nitrogenase by reversible ADP-ribosylation
    • LIANG, J. H., G. M. NIELSEN, D. P. LIES, R. H. BURRIS, G. P. ROBERTS et al., 1991 Mutations in the draT and draG genes of Rhodospirillum rubrum result in loss of regulation of nitrogenase by reversible ADP-ribosylation. J. Bacteriol. 173: 6903-6909.
    • (1991) J. Bacteriol. , vol.173 , pp. 6903-6909
    • Liang, J.H.1    Nielsen, G.M.2    Lies, D.P.3    Burris, R.H.4    Roberts, G.P.5
  • 30
    • 0000217771 scopus 로고
    • Diazotrophy and nitrogenase activity in the archaebacterium Methanosarcina barkeri 227
    • LOBO, A. L., and S. H. ZINDER, 1988 Diazotrophy and nitrogenase activity in the archaebacterium Methanosarcina barkeri 227. Appl. Environ. Microbiol. 54: 1656-1661.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 1656-1661
    • Lobo, A.L.1    Zinder, S.H.2
  • 31
    • 0025630680 scopus 로고
    • Nitrogenase in the archaebacterium Methanosarcina barkeri 227
    • LOBO, A. L., and S. H. ZINDER, 1990 Nitrogenase in the archaebacterium Methanosarcina barkeri 227. J. Bacteriol. 172: 6789-6796.
    • (1990) J. Bacteriol. , vol.172 , pp. 6789-6796
    • Lobo, A.L.1    Zinder, S.H.2
  • 32
    • 0003237822 scopus 로고
    • Nitrogen fixation by methanogenic bacteria
    • edited by G. STACEY, R. H. BURRIS and H. J. EVANS. Chapman and Hall, New York
    • LOBO, A. L., and S. H. ZINDER, 1992 Nitrogen fixation by methanogenic bacteria, pp. 191-211 in Biological Nitrogen Fixation, edited by G. STACEY, R. H. BURRIS and H. J. EVANS. Chapman and Hall, New York.
    • (1992) Biological Nitrogen Fixation , pp. 191-211
    • Lobo, A.L.1    Zinder, S.H.2
  • 33
    • 0001391185 scopus 로고    scopus 로고
    • Regulation of nitrogen utilization
    • edited by F. C. NEIDHARDT. ASM Press, Washington, DC
    • MAGASANIK, B., 1996 Regulation of nitrogen utilization, pp. 1344-1356 in Escherichia coli and Salmonella: Cellular and Molecular Biology, edited by F. C. NEIDHARDT. ASM Press, Washington, DC.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 1344-1356
    • Magasanik, B.1
  • 34
    • 0028865193 scopus 로고
    • Nitrogen control in bacteria
    • MERRICK, M. J., and R. A. EDWARDS, 1995 Nitrogen control in bacteria. Microbiol. Rev. 59: 604-622.
    • (1995) Microbiol. Rev. , vol.59 , pp. 604-622
    • Merrick, M.J.1    Edwards, R.A.2
  • 35
    • 0021686170 scopus 로고
    • Nitrogen fixation by a methanogenic archaebacterium
    • MURRAY, P. A., and S. H. ZINDER, 1984 Nitrogen fixation by a methanogenic archaebacterium. Nature 312: 284-286.
    • (1984) Nature , vol.312 , pp. 284-286
    • Murray, P.A.1    Zinder, S.H.2
  • 36
    • 0024461260 scopus 로고
    • Nucleotide sequence and expression of the glutamine synthetase gene, glnA, of the archaebacterium Methanococcus voltae
    • POSSOT, O., L. SIBOLD and J. P. AUBERT, 1989 Nucleotide sequence and expression of the glutamine synthetase gene, glnA, of the archaebacterium Methanococcus voltae. Res. Microbiol. 140: 355-371.
    • (1989) Res. Microbiol. , vol.140 , pp. 355-371
    • Possot, O.1    Sibold, L.2    Aubert, J.P.3
  • 37
    • 0000060736 scopus 로고    scopus 로고
    • Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine, L-alanine and D-alanine
    • edited by F. C. NEIDHARDT. ASM Press, Washington, DC
    • REITZER, L. J., 1996 Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine, L-alanine and D-alanine, pp. 391-407 in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, edited by F. C. NEIDHARDT. ASM Press, Washington, DC.
    • (1996) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 391-407
    • Reitzer, L.J.1
  • 38
    • 0025856535 scopus 로고
    • Recovery of an integration shuttle vector from tandem repeats in Methanococcus maripaludis
    • SANDBECK, K. A., and J. A. LEIGH, 1991 Recovery of an integration shuttle vector from tandem repeats in Methanococcus maripaludis. Appl. Environ. Microbiol. 57: 2762-2763.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 2762-2763
    • Sandbeck, K.A.1    Leigh, J.A.2
  • 39
    • 0031721044 scopus 로고    scopus 로고
    • Salmonella typhimurium nit is nadE: Defective nitrogen utilization and ammonia-dependent NAD synthetase
    • SCHNEIDER, B. L., and L. J. REITZER, 1998 Salmonella typhimurium nit is nadE: defective nitrogen utilization and ammonia-dependent NAD synthetase. J. Bacteriol. 180: 4739-4741.
    • (1998) J. Bacteriol. , vol.180 , pp. 4739-4741
    • Schneider, B.L.1    Reitzer, L.J.2
  • 40
    • 0032947995 scopus 로고    scopus 로고
    • Requirement of NifX and other nif proteins for in vitro biosynthesis of the iron-molybdenum cofactor of nitrogenase
    • SHAH, V. K., P. RANGARAJ, R. CHATTERJEE, R. M. ALLEN, J. T. ROLL et al., 1999 Requirement of NifX and other nif proteins for in vitro biosynthesis of the iron-molybdenum cofactor of nitrogenase. J. Bacteriol. 181: 2797-2801.
    • (1999) J. Bacteriol. , vol.181 , pp. 2797-2801
    • Shah, V.K.1    Rangaraj, P.2    Chatterjee, R.3    Allen, R.M.4    Roll, J.T.5
  • 41
    • 0025776672 scopus 로고
    • Nucleotide sequence of nifH regions from Methanobacterium ivanovii and Methanosarcina barkeri 227 and characterization of glnB-like genes
    • SIBOLD, L., M. HENRIQUET, O. POSSOT and J. P. AUBERT, 1991 Nucleotide sequence of nifH regions from Methanobacterium ivanovii and Methanosarcina barkeri 227 and characterization of glnB-like genes. Res. Microbiol. 142: 5-12.
    • (1991) Res. Microbiol. , vol.142 , pp. 5-12
    • Sibold, L.1    Henriquet, M.2    Possot, O.3    Aubert, J.P.4
  • 42
    • 15644383855 scopus 로고    scopus 로고
    • Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: Functional analysis and comparative genomics
    • SMITH, D. R., L. A. DOUCETTE-STAMM, C. DELOUGHERY, H. LEE, J. DUBOIS et al., 1997 Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics. J. Bacteriol. 179: 7135-7155.
    • (1997) J. Bacteriol. , vol.179 , pp. 7135-7155
    • Smith, D.R.1    Doucette-Stamm, L.A.2    Deloughery, C.3    H, L.E.E.4    Dubois, J.5
  • 43
    • 0024644241 scopus 로고
    • Primary structure, functional organization and expression of nitrogenase structural genes of the thermophilic archaebacterium Methanococcus thermolithotrophicus
    • SOUILLLARD, N., and L. SIBOLD, 1989 Primary structure, functional organization and expression of nitrogenase structural genes of the thermophilic archaebacterium Methanococcus thermolithotrophicus. Mol. Microbiol. 3: 541-551.
    • (1989) Mol. Microbiol. , vol.3 , pp. 541-551
    • Souilllard, N.1    Sibold, L.2
  • 44
    • 0023683589 scopus 로고
    • Nucleotide sequence of regions homologous to nifH (nitrogenase fe protein) from the nitrogen fixing archaebacteria Methanococcus thermolithotrophicus and Methanobacterium ivanovii: Evolutionary implications
    • SOUILLARD, N., M. MAGOT, O. POSSOT and L. SIBOLD, 1988 Nucleotide sequence of regions homologous to nifH (nitrogenase Fe protein) from the nitrogen fixing archaebacteria Methanococcus thermolithotrophicus and Methanobacterium ivanovii: evolutionary implications. J. Mol. Evol. 27: 65-76.
    • (1988) J. Mol. Evol. , vol.27 , pp. 65-76
    • Souillard, N.1    Magot, M.2    Possot, O.3    Sibold, L.4
  • 45
    • 0032499682 scopus 로고    scopus 로고
    • Ammonia acquisition in enteric bacteria: Physiological role of the ammonium/methylammonium transport B (AmtB) protein
    • SOUPENE, E., L. HE, D. YAN and S. KUSTU, 1998 Ammonia acquisition in enteric bacteria: physiological role of the ammonium/methylammonium transport B (AmtB) protein. Proc. Natl. Acad. Sci. USA 95: 7030-7034.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7030-7034
    • Soupene, E.1    He, L.2    Yan, D.3    Kustu, S.4
  • 46
    • 0027263638 scopus 로고
    • Cloning and sequencing of the gene encoding glutamine synthetase I from the archaeum Pyrococcus woesei: Anomalous phylogenies inferred from analysis of archaeal and bacterial glutamine synthetase I sequences
    • TIBONI, O., P. CAMMARANO and A. M. SANANGELANTONI, 1993 Cloning and sequencing of the gene encoding glutamine synthetase I from the archaeum Pyrococcus woesei: anomalous phylogenies inferred from analysis of archaeal and bacterial glutamine synthetase I sequences. J. Bacteriol. 175: 2961-2969.
    • (1993) J. Bacteriol. , vol.175 , pp. 2961-2969
    • Tiboni, O.1    Cammarano, P.2    Sanangelantoni, A.M.3
  • 47
    • 0028168940 scopus 로고
    • Transformation of Methanococcus maripaludis and identification of a PstI-like restriction system
    • TUMBULA, D. L., R. A. MAKULA and W. B. WHITMAN, 1994 Transformation of Methanococcus maripaludis and identification of a PstI-like restriction system. FEMS Microbiol. Lett. 121: 309-314.
    • (1994) FEMS Microbiol. Lett. , vol.121 , pp. 309-314
    • Tumbula, D.L.1    Makula, R.A.2    Whitman, W.B.3
  • 48
    • 0030903165 scopus 로고    scopus 로고
    • Characterization of pURB500 from the archaeon Methanococcus maripaludis and construction of a shuttle vector
    • TUMBUKA, D. L., T. L. BOWEN and W. B. WHITMAN, 1997 Characterization of pURB500 from the archaeon Methanococcus maripaludis and construction of a shuttle vector. J. Bacteriol. 179: 2976-2986.
    • (1997) J. Bacteriol. , vol.179 , pp. 2976-2986
    • Tumbuka, D.L.1    Bowen, T.L.2    Whitman, W.B.3
  • 49
    • 0031896588 scopus 로고    scopus 로고
    • (Methyl)ammonium transport in the nitrogen-fixing bacterium Azospirillum brasilense
    • VAN DOMMELEN, A., V. KEIJERS, J. VANDERLEYDEN and M. DE ZAMAROCZY, 1998 (Methyl)ammonium transport in the nitrogen-fixing bacterium Azospirillum brasilense. J. Bacteriol. 180: 2652-2659.
    • (1998) J. Bacteriol. , vol.180 , pp. 2652-2659
    • Van Dommelen, A.1    Keijers, V.2    Vanderleyden, J.3    De Zamaroczy, M.4
  • 50
    • 0029657995 scopus 로고    scopus 로고
    • An alternative PII protein in the regulation of glutamine synthetase in Escherichia coli
    • VAN HEESWIJK, W. C., S. HOVING, D. MOLENAAR, B. STEGEMAN, D. KAHN et al., 1996 An alternative PII protein in the regulation of glutamine synthetase in Escherichia coli. Mol. Microbiol. 21: 133-146.
    • (1996) Mol. Microbiol. , vol.21 , pp. 133-146
    • Van Heeswijk, W.C.1    Hoving, S.2    Molenaar, D.3    Stegeman, B.4    Kahn, D.5
  • 52
    • 0030800138 scopus 로고    scopus 로고
    • Development of genetic approaches for the methane-producing archaebacterium Methanococcus maripaludis
    • WHITMAN, W. B., D. L. TUMBULA, J. P. YU and W. KIM, 1997 Development of genetic approaches for the methane-producing archaebacterium Methanococcus maripaludis. Biofactors 6: 37-46.
    • (1997) Biofactors , vol.6 , pp. 37-46
    • Whitman, W.B.1    Tumbula, D.L.2    Yu, J.P.3    Kim, W.4
  • 53
    • 0032508415 scopus 로고    scopus 로고
    • GlnK, a PII-homologue: Structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition
    • XU, Y., E. CHEAH, P. D. CARR, W. C. VAN HEESWIJK, H. V. WESTERHOFF et al., 1998 GlnK, a PII-homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition. J. Mol. Biol. 282: 149-165.
    • (1998) J. Mol. Biol. , vol.282 , pp. 149-165
    • Xu, Y.1    Cheah, E.2    Carr, P.D.3    Van Heeswijk, W.C.4    Westerhoff, H.V.5
  • 54
    • 0026624782 scopus 로고
    • Cloning, sequencing, mutagenesis, and functional characterization of draT and drag genes from Azospirillum brasilense
    • ZHANO, Y., R. H. BURRIS and G. P. ROBERTS, 1992 Cloning, sequencing, mutagenesis, and functional characterization of draT and draG genes from Azospirillum brasilense. J. Bacteriol. 174: 3364-3369.
    • (1992) J. Bacteriol. , vol.174 , pp. 3364-3369
    • Zhano, Y.1    Burris, R.H.2    Roberts, G.P.3
  • 55
    • 0027485991 scopus 로고
    • Posttranslational regulation of nitrogenase activity by anaerobiosisand ammonium in Azospirillum brasilense
    • ZHANG, Y., R. H. BURRIS, P. W. LUDDEN and G. P. ROBERTS, 1993 Posttranslational regulation of nitrogenase activity by anaerobiosisand ammonium in Azospirillum brasilense. J. Bacteriol 175:6781-6788.
    • (1993) J. Bacteriol , vol.175 , pp. 6781-6788
    • Zhang, Y.1    Burris, R.H.2    Ludden, P.W.3    Roberts, G.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.