메뉴 건너뛰기




Volumn 191, Issue 11, 2009, Pages 3726-3735

Characterization of the DraT/DraG system for posttranslational regulation of nitrogenase in the endophytic betaproteobacterium Azoarcus sp. strain BH72

Author keywords

[No Author keywords available]

Indexed keywords

DINITROGENASE REDUCTASE; DINITROGENASE REDUCTASE ACTIVATING GLYCOHYDROLASE 1; DINITROGENASE REDUCTASE ACTIVATING GLYCOHYDROLASE 2; DINITROGENASE REDUCTASE NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; GLYCOSIDASE; IRON; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NITROGEN; NITROGENASE; UNCLASSIFIED DRUG; AMMONIUM CHLORIDE; BACTERIAL PROTEIN;

EID: 66149098542     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01720-08     Document Type: Article
Times cited : (13)

References (57)
  • 1
    • 0004270170 scopus 로고
    • Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). John Wiley & Sons, New York, NY
    • Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). 1987. Current protocols in molecular biology. John Wiley & Sons, New York, NY.
    • (1987) Current Protocols in Molecular Biology
  • 2
    • 0002405741 scopus 로고
    • Biochemical genetics of nitrogenase
    • G. Stacey, R. H. Burris, and H. J. Evans (ed.), Chapman and Hall, New York, NY
    • Dean, D. R., and M. R. Jacobson. 1992. Biochemical genetics of nitrogenase, p. 763-835. In G. Stacey, R. H. Burris, and H. J. Evans (ed.), Biological nitrogen fixation. Chapman and Hall, New York, NY.
    • (1992) Biological Nitrogen Fixation , pp. 763-835
    • Dean, D.R.1    Jacobson, M.R.2
  • 3
    • 0028040342 scopus 로고
    • Posttranslational modification of nitrogenase. Differences between the purple bacterium Rhodospirillum rubrum and the cyanobacterium Anabaena variabilis
    • Durner, J., I. Böhm, H. Hilz, and P. Böger. 1994. Posttranslational modification of nitrogenase. Differences between the purple bacterium Rhodospirillum rubrum and the cyanobacterium Anabaena variabilis. Eur. J. Biochem. 220:125-130. (Pubitemid 24067561)
    • (1994) European Journal of Biochemistry , vol.220 , Issue.1 , pp. 125-130
    • Durner, J.1    Bohm, I.2    Hilz, H.3    Boger, P.4
  • 4
    • 17144366135 scopus 로고    scopus 로고
    • Electron transport to nitrogenase in Rhodospirillum rubrum: Identification of a new fdxN gene encoding the primary electron donor to nitrogenase
    • Edgren, T., and S. Nordlund. 2005. Electron transport to nitrogenase in Rhodospirillum rubrum: identification of a new fdxN gene encoding the primary electron donor to nitrogenase. FEMS Microbiol. Lett. 245:345-351.
    • (2005) FEMS Microbiol. Lett. , vol.245 , pp. 345-351
    • Edgren, T.1    Nordlund, S.2
  • 5
    • 0032798572 scopus 로고    scopus 로고
    • Endophytic expression of nif genes of Azoarcus sp. strain BH72 in rice roots
    • Egener, T., T. Hurek, and B. Reinhold-Hurek. 1999. Endophytic expression of nif genes of Azoarcus sp. strain BH72 in rice roots. Mol. Plant-Microbe Interact. 12:813-819.
    • (1999) Mol. Plant-Microbe Interact. , vol.12 , pp. 813-819
    • Egener, T.1    Hurek, T.2    Reinhold-Hurek, B.3
  • 8
    • 0024710884 scopus 로고
    • Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum
    • Fitzmaurice, W. P., L. L. Saari, R. G. Lowery, P. W. Ludden, and G. P. Roberts. 1989. Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum. Mol. Gen. Genet. 218:340-347.
    • (1989) Mol. Gen. Genet. , vol.218 , pp. 340-347
    • Fitzmaurice, W.P.1    Saari, L.L.2    Lowery, R.G.3    Ludden, P.W.4    Roberts, G.P.5
  • 9
    • 0024687641 scopus 로고
    • Ammonium inhibition of nitrogenase activity in Herbaspirillum seropedicae
    • Fu, H., and R. H. Burris. 1989. Ammonium inhibition of nitrogenase activity in Herbaspirillum seropedicae. J. Bacteriol. 171:3168-3175.
    • (1989) J. Bacteriol. , vol.171 , pp. 3168-3175
    • Fu, H.1    Burris, R.H.2
  • 11
    • 0034108232 scopus 로고    scopus 로고
    • Regulation of biological nitrogen fixation
    • Halbleib, C. M., and P. W. Ludden. 2000. Regulation of biological nitrogen fixation. J. Nutr. 130:1081-1084. (Pubitemid 30233250)
    • (2000) Journal of Nutrition , vol.130 , Issue.5 , pp. 1081-1084
    • Halbleib, C.M.1    Ludden, P.W.2
  • 12
    • 0034123366 scopus 로고    scopus 로고
    • Effects of perturbations of the nitrogenase electron transfer chain on reversible ADP-ribosylation of nitrogenase Fe protein in Klebsiella pneumoniae strains bearing the Rhodospirillum rubrum dra operon
    • DOI 10.1128/JB.182.13.3681-3687.2000
    • Halbleib, C. M., Y. Zhang, G. P. Roberts, and P. W. Ludden. 2000. Effects of perturbations of the nitrogenase electron transfer chain on reversible ADP-ribosylation of nitrogenase Fe protein in Klebsiella pneumoniae strains bearing the Rhodospirillum rubrum dra operon. J. Bacteriol. 182:3681-3687. (Pubitemid 30413018)
    • (2000) Journal of Bacteriology , vol.182 , Issue.13 , pp. 3681-3687
    • Halbleib, C.M.1    Zhang, Y.2    Roberts, G.P.3    Ludden, P.W.4
  • 13
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 14
    • 0022456173 scopus 로고
    • Regulation of nitrogenase activity by ammonium chloride in Azospirillum spp.
    • Hartmann, A., H. Fu, and R. H. Burris. 1986. Regulation of nitrogenase activity by ammonium chloride in Azospirillum spp. J. Bacteriol. 165:864-870.
    • (1986) J. Bacteriol. , vol.165 , pp. 864-870
    • Hartmann, A.1    Fu, H.2    Burris, R.H.3
  • 17
    • 33645089445 scopus 로고    scopus 로고
    • ADP-ribosylation of dinitrogenase reductase in Azospirillum brasilense is regulated by AmtB-dependent membrane sequestration of DraG
    • Huergo, L. F., E. M. Souza, M. S. Araujo, F. O. Pedrosa, L. S. Chubatsu, M. B. Steffens, and M. Merrick. 2006. ADP-ribosylation of dinitrogenase reductase in Azospirillum brasilense is regulated by AmtB-dependent membrane sequestration of DraG. Mol. Microbiol. 59:326-337.
    • (2006) Mol. Microbiol. , vol.59 , pp. 326-337
    • Huergo, L.F.1    Souza, E.M.2    Araujo, M.S.3    Pedrosa, F.O.4    Chubatsu, L.S.5    Steffens, M.B.6    Merrick, M.7
  • 18
    • 0027430312 scopus 로고
    • 16S rRNA-targeted polymerase chain reaction and oligonucleotide hybridization to screen for Azoarcus spp., grass-associated diazotrophs
    • Hurek, T., S. Burggraf, C. R. Woese, and B. Reinhold-Hurek. 1993. 16S rRNA-targeted polymerase chain reaction and oligonucleotide hybridization to screen for Azoarcus spp., grass-associated diazotrophs. Appl. Environ. Microbiol. 59:3816-3824.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3816-3824
    • Hurek, T.1    Burggraf, S.2    Woese, C.R.3    Reinhold-Hurek, B.4
  • 19
    • 0030814221 scopus 로고    scopus 로고
    • Divergence in nitrogenases of Azoarcus spp., Proteobacteria of the β-subclass
    • Hurek, T., T. Egener, and B. Reinhold-Hurek. 1997. Divergence in nitrogenases of Azoarcus spp., Proteobacteria of the β-subclass. J. Bacteriol. 179:4172-4178.
    • (1997) J. Bacteriol. , vol.179 , pp. 4172-4178
    • Hurek, T.1    Egener, T.2    Reinhold-Hurek, B.3
  • 21
    • 0028265651 scopus 로고
    • Root colonization and systemic spreading of Azoarcus sp. strain BH72 in grasses
    • Hurek, T., B. Reinhold-Hurek, M. Van Montagu, and E. Kellenberger. 1994. Root colonization and systemic spreading of Azoarcus sp. strain BH72 in grasses. J. Bacteriol. 176:1913-1923.
    • (1994) J. Bacteriol. , vol.176 , pp. 1913-1923
    • Hurek, T.1    Reinhold-Hurek, B.2    Van Montagu, M.3    Kellenberger, E.4
  • 22
    • 0028840504 scopus 로고
    • Induction of complex intracytoplasmic membranes related to nitrogen fixation in Azoarcus sp. BH72
    • Hurek, T., M. Van Montagu, E. Kellenberger, and B. Reinhold-Hurek. 1995. Induction of complex intracytoplasmic membranes related to nitrogen fixation in Azoarcus sp. BH72. Mol. Microbiol. 18:225-236.
    • (1995) Mol. Microbiol. , vol.18 , pp. 225-236
    • Hurek, T.1    Van Montagu, M.2    Kellenberger, E.3    Reinhold-Hurek, B.4
  • 23
    • 0029877819 scopus 로고    scopus 로고
    • Cloning, sequencing and transcriptional regulation of the draT and draG genes of Azospirillum lipoferum FS
    • Inoue, A., T. Shigematsu, M. Hidaka, H. Masaki, and T. Uozumi. 1996. Cloning, sequencing and transcriptional regulation of the draT and draG genes of Azospirillum lipoferum FS. Gene 170:101-106.
    • (1996) Gene , vol.170 , pp. 101-106
    • Inoue, A.1    Shigematsu, T.2    Hidaka, M.3    Masaki, H.4    Uozumi, T.5
  • 24
    • 0342444416 scopus 로고
    • GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson, R. A., T. A. Kavanagh, and M. W. Bevan. 1987. GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 6:3901-3908.
    • (1987) EMBO J. , vol.6 , pp. 3901-3908
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 25
    • 0001515028 scopus 로고
    • ADP-ribosylation of dinitrogenase reductase in Rhodobacter capsulatus
    • Jouanneau, Y., C. Roby, C. M. Meyer, and P. M. Vignais. 1989. ADP-ribosylation of dinitrogenase reductase in Rhodobacter capsulatus. Biochemistry 28:6524-6530.
    • (1989) Biochemistry , vol.28 , pp. 6524-6530
    • Jouanneau, Y.1    Roby, C.2    Meyer, C.M.3    Vignais, P.M.4
  • 26
    • 0021353152 scopus 로고
    • Effect of ammonia, darkness, and phenazine methosulfate on whole-cell nitrogenase acivity and Fe protein modification in Rhodospirillum rubrum
    • Kanemoto, R. H., and P. W. Ludden. 1984. Effect of ammonia, darkness, and phenazine methosultate on whole-cell nitrogenase activity and Fe protein modification in Rhodospirillum rubrum. J. Bacteriol. 158:713-720. (Pubitemid 14145676)
    • (1984) Journal of Bacteriology , vol.158 , Issue.2 , pp. 713-720
    • Kanemoto, R.H.1    Ludden, P.W.2
  • 27
    • 0029797930 scopus 로고    scopus 로고
    • 2-fixing Azoarcus sp. strain BH72 upon diazosome formation
    • 2-fixing Azoarcus sp. strain BH72 upon diazosome formation. J. Bacteriol. 178:5748-5754.
    • (1996) J. Bacteriol. , vol.178 , pp. 5748-5754
    • Karg, T.1    Reinhold-Hurek, B.2
  • 28
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: Improvement in accuracy of multiple sequence alignment
    • DOI 10.1093/nar/gki198
    • Katoh, K., K. Kuma, H. Toh, and T. Miyata. 2005. MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucleic Acids Res. 33:511-518. (Pubitemid 40360980)
    • (2005) Nucleic Acids Research , vol.33 , Issue.2 , pp. 511-518
    • Katoh, K.1    Kuma, K.-I.2    Toh, H.3    Miyata, T.4
  • 29
    • 33847310423 scopus 로고    scopus 로고
    • PartTree: An algorithm to build an approximate tree from a large number of unaligned sequences
    • DOI 10.1093/bioinformatics/btl592
    • Katoh, K., and H. Toh. 2007. PartTree: an algorithm to build an approximate tree from a large number of unaligned sequences. Bioinformatics 23:372-374. (Pubitemid 46323161)
    • (2007) Bioinformatics , vol.23 , Issue.3 , pp. 372-374
    • Katoh, K.1    Toh, H.2
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 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., G. M. Nielsen, D. P. Lies, R. H. Burris, G. P. Roberts, and P. W. Ludden. 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.1    Nielsen, G.M.2    Lies, D.P.3    Burris, R.H.4    Roberts, G.P.5    Ludden, P.W.6
  • 33
    • 0024289173 scopus 로고
    • Purification and properties of dinitrogenase reductase ADP-ribosyltransferase from the photosynthetic bacterium Rhodospirillum rubrum
    • Lowery, R. G., and P. W. Ludden. 1988. Purification and properties of dinitrogenase reductase ADP-ribosyltransferase from the photosynthetic bacterium Rhodospirillum rubrum. J. Biol. Chem. 263:16714-16719.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16714-16719
    • Lowery, R.G.1    Ludden, P.W.2
  • 34
    • 0036209809 scopus 로고    scopus 로고
    • II-like signal transmitter protein and amtB in regulation of nif gene expression, nitrogenase activity, and posttranslational modification of NifH in Azoarcus sp. strain BH72
    • II-like signal transmitter protein and amtB in regulation of nif gene expression, nitrogenase activity, and posttranslational modification of NifH in Azoarcus sp. strain BH72. J. Bacteriol. 184:2251-2259.
    • (2002) J. Bacteriol. , vol.184 , pp. 2251-2259
    • Martin, D.E.1    Reinhold-Hurek, B.2
  • 35
    • 0027332197 scopus 로고
    • The draTG gene region of Rhodobacter capsulatus is required for post-translational regulation of both the molybdenum and the alternative nitrogenase
    • Masepohl, B., R. Krey, and W. Klipp. 1993. The draTG gene region of Rhodobacter capsulatus is required for post-translational regulation of both the molybdenum and the alternative nitrogenase. J. Gen. Microbiol. 139:2667-2675.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2667-2675
    • Masepohl, B.1    Krey, R.2    Klipp, W.3
  • 36
    • 0028865193 scopus 로고
    • Nitrogen control in bacteria
    • Merrick, M., and R. Edwards. 1995. Nitrogen control in bacteria. Microbiol. Rev. 59:604-622.
    • (1995) Microbiol. Rev. , vol.59 , pp. 604-622
    • Merrick, M.1    Edwards, R.2
  • 37
    • 0042130559 scopus 로고    scopus 로고
    • Yeast two-hybrid studies on interaction of proteins involved in regulation of nitrogen fixation in the phototrophic bacterium Rhodobacter capsulatus
    • DOI 10.1128/JB.185.17.5240-5247.2003
    • Pawlowski, A., K. U. Riedel, W. Klipp, P. Dreiskemper, S. Gross, H. Bierhoff, T. Drepper, and B. Masepohl. 2003. Yeast two-hybrid studies on interaction of proteins involved in regulation of nitrogen fixation in the phototrophic bacterium Rhodobacter capsulatus. J. Bacteriol. 185:5240-5247. (Pubitemid 37021985)
    • (2003) Journal of Bacteriology , vol.185 , Issue.17 , pp. 5240-5247
    • Pawlowski, A.1    Riedel, K.-U.2    Klipp, W.3    Dreiskemper, P.4    Gross, S.5    Bierhoff, H.6    Drepper, T.7    Masepohl, B.8
  • 38
    • 0027418844 scopus 로고
    • Posttranslational regulation of nitrogenase in Rhodobacter capsulatus: Existence of two independent regulatory effects of ammonium
    • Pierrard, J., P. W. Ludden, and G. P. Roberts. 1993. Posttranslational regulation of nitrogenase in Rhodobacter capsulatus: existence of two independent regulatory effects of ammonium. J. Bacteriol. 175:1358-1366.
    • (1993) J. Bacteriol. , vol.175 , pp. 1358-1366
    • Pierrard, J.1    Ludden, P.W.2    Roberts, G.P.3
  • 39
    • 0021821712 scopus 로고
    • Covalent modification of the iron protein of nitrogenase from Rhodospirillum rubrum by adenine diphosphoribosylation of a specific arginine residue
    • Pope, M. R., S. A. Murell, and P. W. Ludden. 1985. Covalent modification of the iron protein of nitrogenase from Rhodospirillum rubrum by adenine diphosphoribosylation of a specific arginine residue. Proc. Natl. Acad. Sci. USA 82:3173-3177.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3173-3177
    • Pope, M.R.1    Murell, S.A.2    Ludden, P.W.3
  • 40
    • 0001316539 scopus 로고
    • Close association of Azospirillum and diazotrophic rods with different root zones of Kallar grass
    • Reinhold, B., T. Hurek, E.-G. Niemann, and I. Fendrik. 1986. Close association of Azospirillum and diazotrophic rods with different root zones of Kallar grass. Appl. Environ. Microbiol. 52:520-526.
    • (1986) Appl. Environ. Microbiol. , vol.52 , pp. 520-526
    • Reinhold, B.1    Hurek, T.2    Niemann, E.-G.3    Fendrik, I.4
  • 41
    • 0027428008 scopus 로고
    • Cloning, expression in Escherichia coli, and characterization of cellulolytic enzymes of Azoarcus sp., a root-invading diazotroph
    • Reinhold-Hurek, B., T. Hurek, M. Claeyssens, and M. Van Montagu. 1993. Cloning, expression in Escherichia coli, and characterization of cellulolytic enzymes of Azoarcus sp., a root-invading diazotroph. J. Bacteriol. 175:7056-7065.
    • (1993) J. Bacteriol. , vol.175 , pp. 7056-7065
    • Reinhold-Hurek, B.1    Hurek, T.2    Claeyssens, M.3    Van Montagu, M.4
  • 42
    • 0027169610 scopus 로고
    • Azoarcus gen. nov., nitrogen-fixing Proteobacteria associated with roots of Kallar grass (Leptochloa fusca (L.) Kunth), and description of two species, Azoarcus indigens sp. nov. and Azoarcus communis sp. nov
    • Reinhold-Hurek, B., T. Hurek, M. Gillis, B. Hoste, M. Vancanneyt, K. Kersters, and J. De Ley. 1993. Azoarcus gen. nov., nitrogen-fixing proteobacteria associated with roots of Kallar grass (Leptochloa fusca (L.) Kunth) and description of two species, Azoarcus indigens sp. nov. and Azoarcus communis sp. nov. Int. J. Syst. Bacteriol. 43:574-584. (Pubitemid 23210440)
    • (1993) International Journal of Systematic Bacteriology , vol.43 , Issue.3 , pp. 574-584
    • Reinhold-Hurek, B.1    Hurek, T.2    Gillis, M.3    Hoste, B.4    Vancanneyt, M.5    Kersters, K.6    De Ley, J.7
  • 43
    • 0023019608 scopus 로고
    • Studies on the activating enzyme for iron protein of nitrogenase from Rhodospirillum rubrum
    • Saari, L. L., M. R. Pope, S. A. Murrell, and P. W. Ludden. 1986. Studies on the activating enzyme for iron protein of nitrogenase from Rhodospirillum rubrum. J. Biol. Chem. 261:4973-4977.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4973-4977
    • Saari, L.L.1    Pope, M.R.2    Murrell, S.A.3    Ludden, P.W.4
  • 44
    • 0021707085 scopus 로고
    • Purification and properties of the activating enzyme for iron protein of nitrogenase from the photosynthetic bacterium Rhodospirillum rubrum
    • Saari, L. L., E. W. Triplett, and P. W. Ludden. 1984. Purification and properties of the activating enzyme for iron protein of nitrogenase from the photosynthetic bacterium Rhodospirillum rubrum. J. Biol. Chem. 259:15502-15508. (Pubitemid 15193780)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.24 , pp. 15502-15508
    • Saari, L.L.1    Triplett, E.W.2    Ludden, P.W.3
  • 45
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • DOI 10.1016/0378-1119(94)90324-7
    • Schäfer, A., A. Tauch, W. Jager, J. Kalinowski, G. Thierbach, and A. Puhler. 1994. Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145:69-73. (Pubitemid 24224965)
    • (1994) Gene , vol.145 , Issue.1 , pp. 69-73
    • Schafer, A.1    Tauch, A.2    Jager, W.3    Kalinowski, J.4    Thierbach, G.5    Puhler, A.6
  • 46
    • 0022353127 scopus 로고
    • Purification and properties of the nitrogenase of Azospirillum amazonense
    • Song, S. D., A. Hartmann, and R. H. Burris. 1985. Purification and properties of the nitrogenase of Azospirillum amazonense. J. Bacteriol. 164:1271-1277.
    • (1985) J. Bacteriol. , vol.164 , pp. 1271-1277
    • Song, S.D.1    Hartmann, A.2    Burris, R.H.3
  • 47
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura, K., J. Dudley, M. Nei, and S. Kumar. 2007. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24:1596-1599.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 48
    • 34547799020 scopus 로고    scopus 로고
    • II proteins and nitrogenase regulation in the photosynthetic bacterium Rhodobacter capsulatus
    • II proteins and nitrogenase regulation in the photosynthetic bacterium Rhodobacter capsulatus. J. Bacteriol. 189:5850-5859.
    • (2007) J. Bacteriol. , vol.189 , pp. 5850-5859
    • Tremblay, P.L.1    Drepper, T.2    Masepohl, B.3    Hallenbeck, P.C.4
  • 49
    • 39749184089 scopus 로고    scopus 로고
    • Ammonia-induced formation of an AmtB-GlnK complex is not sufficient for nitrogenase regulation in the photosynthetic bacterium Rhodobacter capsulatus
    • Tremblay, P. L., and P. C. Hallenbeck. 2008. Ammonia-induced formation of an AmtB-GlnK complex is not sufficient for nitrogenase regulation in the photosynthetic bacterium Rhodobacter capsulatus. J. Bacteriol. 190:1588-1594.
    • (2008) J. Bacteriol. , vol.190 , pp. 1588-1594
    • Tremblay, P.L.1    Hallenbeck, P.C.2
  • 50
    • 0020362434 scopus 로고
    • Expression of the activating enzyme and Fe protein of nitrogenase from Rhodospirillum rubrum
    • Triplett, E. W., J. D. Wall, and P. W. Ludden. 1982. Expression of the activating enzyme and Fe protein of nitrogenase from Rhodospirillum rubrum. J. Bacteriol. 152:786-791.
    • (1982) J. Bacteriol. , vol.152 , pp. 786-791
    • Triplett, E.W.1    Wall, J.D.2    Ludden, P.W.3
  • 51
    • 27944489552 scopus 로고    scopus 로고
    • Reversible membrane association of dinitrogenase reductase activating glycohydrolase in the regulation of nitrogenase activity in Rhodospirillum rubrum; dependence on GlnJ and AmtB1
    • Wang, H., C. C. Franke, S. Nordlund, and A. Noren. 2005. Reversible membrane association of dinitrogenase reductase activating glycohydrolase in the regulation of nitrogenase activity in Rhodospirillum rubrum; dependence on GlnJ and AmtB1. FEMS Microbiol. Lett. 253:273-279.
    • (2005) FEMS Microbiol. Lett. , vol.253 , pp. 273-279
    • Wang, H.1    Franke, C.C.2    Nordlund, S.3    Noren, A.4
  • 52
    • 34248666415 scopus 로고    scopus 로고
    • Phylogenetic analysis, genome evolution and the rate of gene gain in the Herpesviridae
    • DOI 10.1016/j.ympev.2006.11.019, PII S1055790306004763
    • Wang, N., P. F. Baldi, and B. S. Gaut. 2007. Phylogenetic analysis, genome evolution and the rate of gene gain in the Herpesviridae. Mol. Phylogenet. Evol. 43:1066-1075. (Pubitemid 46777391)
    • (2007) Molecular Phylogenetics and Evolution , vol.43 , Issue.3 , pp. 1066-1075
    • Wang, N.1    Baldi, P.F.2    Gaut, B.S.3
  • 53
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • DOI 10.1016/0378-1119(85)90120-9
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119. (Pubitemid 15122816)
    • (1985) Gene , vol.33 , Issue.1 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 54
    • 0027485991 scopus 로고
    • Posttranslational regulation of nitrogenase activity by anaerobiosis and ammonium in Azospirillum brasilense
    • Zhang, Y., R. H. Burris, P. W. Ludden, and G. P. Roberts. 1993. Posttranslational regulation of nitrogenase activity by anaerobiosis and 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
  • 55
    • 0029911652 scopus 로고    scopus 로고
    • Presence of a second mechanism for the posttranslational regulation of nitrogenase activity in Azospirillum brasilense in response to ammonium
    • Zhang, Y., R. H. Burris, P. W. Ludden, and G. P. Roberts. 1996. Presence of a second mechanism for the posttranslational regulation of nitrogenase activity in Azospirillum brasilense in response to ammonium. J. Bacteriol. 178:2948-2953.
    • (1996) J. Bacteriol. , vol.178 , pp. 2948-2953
    • Zhang, Y.1    Burris, R.H.2    Ludden, P.W.3    Roberts, G.P.4
  • 56
    • 0026624782 scopus 로고
    • Cloning, sequencing, mutagenesis, and functional characterization of draT and draG genes from Azospirillum brasilense
    • Zhang, 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
    • Zhang, Y.1    Burris, R.H.2    Roberts, G.P.3
  • 57
    • 33644779117 scopus 로고    scopus 로고
    • Identification of Rhodospirillum rubrum GlnB variants that are altered in their ability to interact with different targets in response to nitrogen status signals
    • Zhu, Y., M. C. Conrad, Y. Zhang, and G. P. Roberts. 2006. Identification of Rhodospirillum rubrum GlnB variants that are altered in their ability to interact with different targets in response to nitrogen status signals. J. Bacteriol. 188:1866-1874.
    • (2006) J. Bacteriol. , vol.188 , pp. 1866-1874
    • Zhu, Y.1    Conrad, M.C.2    Zhang, Y.3    Roberts, G.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.