메뉴 건너뛰기




Volumn 178, Issue 10, 1996, Pages 2948-2953

Presence of a second mechanism for the posttranslational regulation of nitrogenase activity in Azospirillum brasilense in response to ammonium

Author keywords

[No Author keywords available]

Indexed keywords

DINITROGENASE REDUCTASE; NITROGENASE;

EID: 0029911652     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.10.2948-2953.1996     Document Type: Article
Times cited : (26)

References (44)
  • 1
    • 15844431024 scopus 로고
    • Biological nitrogen fixation associated with sugar cane
    • M. Polsinelli, R. Materassi, and M. Vincenzini (ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Boddey, R. M., S. Urquiaga, V. Reis, and J. Döbereiner. 1991. Biological nitrogen fixation associated with sugar cane, p. 105-125. In M. Polsinelli, R. Materassi, and M. Vincenzini (ed.), Nitrogen fixation. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1991) Nitrogen Fixation , pp. 105-125
    • Boddey, R.M.1    Urquiaga, S.2    Reis, V.3    Döbereiner, J.4
  • 2
    • 0015484759 scopus 로고
    • Nitrogen fixation - Assay methods and techniques
    • Burris, R. H. 1972. Nitrogen fixation - assay methods and techniques. Methods Enzymol. 24B:415-431.
    • (1972) Methods Enzymol. , vol.24 B , pp. 415-431
    • Burris, R.H.1
  • 3
    • 0242490169 scopus 로고
    • Control of nitrogenase in Azospirillum sp
    • Burris, R. H., A. Hartmann, Y. Zhang, and H. Fu. 1991. Control of nitrogenase in Azospirillum sp. Plant Soil 137:127-134.
    • (1991) Plant Soil , vol.137 , pp. 127-134
    • Burris, R.H.1    Hartmann, A.2    Zhang, Y.3    Fu, H.4
  • 4
    • 0024077486 scopus 로고
    • Characterization of nifH mutations in Klebsiella pneumoniae
    • Chang, C. L., L. C. Davis, M. Rider, and D. J. Takemoto. 1988. Characterization of nifH mutations in Klebsiella pneumoniae. J. Baeteriol. 170:4015-4022.
    • (1988) J. Baeteriol. , vol.170 , pp. 4015-4022
    • Chang, C.L.1    Davis, L.C.2    Rider, M.3    Takemoto, D.J.4
  • 6
    • 0002405741 scopus 로고
    • Biochemical genetics of nitrogenase
    • G. Stacey, R. H. Burris, and H. J. Evans (ed.), Chapman and Hall, Inc., London
    • Dean, D. R., and M. R. Jacobson. 1992. Biochemical genetics of nitrogenase, p. 763-834. In G. Stacey, R. H. Burris, and H. J. Evans (ed.), Biological nitrogen fixation. Chapman and Hall, Inc., London.
    • (1992) Biological Nitrogen Fixation , pp. 763-834
    • Dean, D.R.1    Jacobson, M.R.2
  • 7
    • 0026601458 scopus 로고
    • Site-directed mutagenesis of virtually any plasmid by eliminating a unique site
    • Deng, W. P., and J. A. Nickoloff. 1992. Site-directed mutagenesis of virtually any plasmid by eliminating a unique site. Anal. Biochem. 200:81-88.
    • (1992) Anal. Biochem. , vol.200 , pp. 81-88
    • Deng, W.P.1    Nickoloff, J.A.2
  • 8
    • 0022000283 scopus 로고
    • Plasmids related to the broad host range vector, pRK290, useful for gene cloning and for monitoring gene expression
    • Ditta, G., T. Schmidhauser, E. Yakobson, P. Lu, X.-W. Liang, D. R. Finlay, D. Guiney, and D. R. Helinski. 1985. Plasmids related to the broad host range vector, pRK290, useful for gene cloning and for monitoring gene expression. Plasmid 13:149-153.
    • (1985) Plasmid , vol.13 , pp. 149-153
    • Ditta, G.1    Schmidhauser, T.2    Yakobson, E.3    Lu, P.4    Liang, X.-W.5    Finlay, D.R.6    Guiney, D.7    Helinski, D.R.8
  • 9
    • 0028040342 scopus 로고
    • Posttranslational modification of nitrogenase: Difference between the purple bacterium Rhodospirillum rubrum and the cyanobacterium Anahaena variabilis
    • Durner, J., I. Bohm, H. Hilz, and P. Boger. 1994. Posttranslational modification of nitrogenase: difference between the purple bacterium Rhodospirillum rubrum and the cyanobacterium Anahaena variabilis. Eur. J. Biochem. 220:125-130.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 125-130
    • Durner, J.1    Bohm, I.2    Hilz, H.3    Boger, P.4
  • 10
    • 0023272340 scopus 로고
    • Interposon mutagenesis of soil and water bacteria: A family of DNA fragments designed for in vitro insertional mutagenesis of Gram-negative bacteria
    • Fellay, R., J. Frey, and H. Krisch. 1987. Interposon mutagenesis of soil and water bacteria: a family of DNA fragments designed for in vitro insertional mutagenesis of Gram-negative bacteria. Gene 52:147-154.
    • (1987) Gene , vol.52 , pp. 147-154
    • Fellay, R.1    Frey, J.2    Krisch, H.3
  • 11
    • 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
  • 12
    • 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. Baeteriol. 171:3168-3175.
    • (1989) J. Baeteriol. , vol.171 , pp. 3168-3175
    • Fu, H.1    Burris, R.H.2
  • 14
    • 0028938830 scopus 로고
    • Posttranslational regulation of nitrogenase in Rhodospirillum rubrum strains overexpressing the regulatory enzymes dinitrogcnase reductase ADP-ribosyltransferase and dinitrogenase reductase activating glycohydrolase
    • Grunwald, S. K., D. P. Lies, G. P. Roberts, and P. W. Ludden. 1995. Posttranslational regulation of nitrogenase in Rhodospirillum rubrum strains overexpressing the regulatory enzymes dinitrogcnase reductase ADP-ribosyltransferase and dinitrogenase reductase activating glycohydrolase. J. Bacteriol. 177:628-635.
    • (1995) J. Bacteriol. , vol.177 , pp. 628-635
    • Grunwald, S.K.1    Lies, D.P.2    Roberts, G.P.3    Ludden, P.W.4
  • 16
    • 0023131526 scopus 로고
    • Regulation of nitrogenase activity by oxygen in Azospirillum brasilense and Azospirillum lipoferum
    • Hartmann, A., and R. H. Burris. 1987. Regulation of nitrogenase activity by oxygen in Azospirillum brasilense and Azospirillum lipoferum. J. Bacteriol. 169:944-948.
    • (1987) J. Bacteriol. , vol.169 , pp. 944-948
    • Hartmann, A.1    Burris, R.H.2
  • 17
    • 0022456173 scopus 로고
    • Regulation of nitrogenase activity by ammonium chloride in Azospirillum spp
    • Hartmann, A., H.-A. 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.-A.2    Burris, R.H.3
  • 18
    • 0018676861 scopus 로고
    • Glutamine as a feedback inhibitor of the Rhodopseudomonas sphaeroides nitrogenase system
    • Jones, B. L., and K. J. Monty. 1979. Glutamine as a feedback inhibitor of the Rhodopseudomonas sphaeroides nitrogenase system. J. Bacteriol. 139:1007-1013.
    • (1979) J. Bacteriol. , vol.139 , pp. 1007-1013
    • Jones, B.L.1    Monty, K.J.2
  • 19
    • 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
  • 20
    • 0021353152 scopus 로고
    • Effect of ammonia, darkness, and phenazine methosulfate on whole-cell nitrogenase activity and Fe protein modification in Rhodospirillum rubrum
    • Kanemoto, R. H., and P. W. Ludden. 1984. Effect of ammonia, darkness, and phenazine methosulfate on whole-cell nitrogenase activity and Fe protein modification in Rhodospirillum rubrum. J. Bacteriol. 158:713-720.
    • (1984) J. Bacteriol. , vol.158 , pp. 713-720
    • Kanemoto, R.H.1    Ludden, P.W.2
  • 21
    • 0021366502 scopus 로고
    • Inhibition of nitrogenase activity by ammonium chloride in Azotobacter vinelandii
    • Klugkist, J., and H. Haaker. 1984. Inhibition of nitrogenase activity by ammonium chloride in Azotobacter vinelandii. J. Bacteriol. 157:148-151.
    • (1984) J. Bacteriol. , vol.157 , pp. 148-151
    • Klugkist, J.1    Haaker, H.2
  • 22
    • 0018854864 scopus 로고
    • Short-term effect of ammonium chloride on nitrogen fixation by Azotobacter vinelandii and by bacteroides of Rhizobium leguminosarum
    • Lanne, C., W. Krone, W. Konings, H. Haaker, and C. Veeger. 1980. Short-term effect of ammonium chloride on nitrogen fixation by Azotobacter vinelandii and by bacteroides of Rhizobium leguminosarum. Eur. J. Biochem. 103:39-46.
    • (1980) Eur. J. Biochem. , vol.103 , pp. 39-46
    • Lanne, C.1    Krone, W.2    Konings, W.3    Haaker, H.4    Veeger, C.5
  • 23
    • 0025198530 scopus 로고
    • The cloning and functional characterization of the nifH gene of Rhodospirillum rubrum
    • Lehman, L. J., W. P. Fitzmaurice, and G. P. Roberts. 1990. The cloning and functional characterization of the nifH gene of Rhodospirillum rubrum. Gene 95:143-147.
    • (1990) Gene , vol.95 , pp. 143-147
    • Lehman, L.J.1    Fitzmaurice, W.P.2    Roberts, G.P.3
  • 24
    • 0025944930 scopus 로고
    • Identification of an alternative nitrogenase system in Rhodospirillum rubrum
    • Lehman, L. J., and G. P. Roberts. 1991. Identification of an alternative nitrogenase system in Rhodospirillum rubrum. J. Bacteriol. 173:5705-5711.
    • (1991) J. Bacteriol. , vol.173 , pp. 5705-5711
    • Lehman, L.J.1    Roberts, G.P.2
  • 25
    • 0026009164 scopus 로고
    • Glycine 100 in the dinitrogenase reductase of Rhodospirillum rubrum is required for nitrogen fixation but not for ADP-ribosylation
    • Lehman, L. J., and G. P. Roberts. 1991. Glycine 100 in the dinitrogenase reductase of Rhodospirillum rubrum is required for nitrogen fixation but not for ADP-ribosylation. J. Bacteriol. 173:6159-6161.
    • (1991) J. Bacteriol. , vol.173 , pp. 6159-6161
    • Lehman, L.J.1    Roberts, G.P.2
  • 26
    • 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, 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.-H.1    Nielsen, G.M.2    Lies, D.P.3    Burris, R.H.4    Roberts, G.P.5    Ludden, P.W.6
  • 27
    • 0024963556 scopus 로고
    • Substitution of histidine for arginine-101 of dinitrogenase reductase disrupts electron transfer to dinitrogenase
    • Lowery, R. G., C. L. Chang, L. C. Davis, M.-C. McKenna, P. J. Stephens, and P. W. Ludden. 1989. Substitution of histidine for arginine-101 of dinitrogenase reductase disrupts electron transfer to dinitrogenase. Biochemistry 28: 1206-1212.
    • (1989) Biochemistry , vol.28 , pp. 1206-1212
    • Lowery, R.G.1    Chang, C.L.2    Davis, L.C.3    McKenna, M.-C.4    Stephens, P.J.5    Ludden, P.W.6
  • 28
    • 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. 30:23-56.
    • (1989) Curr. Top. Cell. Regul. , vol.30 , pp. 23-56
    • Ludden, P.W.1    Roberts, G.P.2
  • 29
    • 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
  • 30
    • 0021251214 scopus 로고
    • Regulation of nitrogen fixation (nif) genes of Azospirillum brasilense by nifA and Mr (gln) type gene products
    • Pedrosa, F. O., and M. G. Yates. 1984. Regulation of nitrogen fixation (nif) genes of Azospirillum brasilense by nifA and Mr (gln) type gene products. FEMS Microbiol. Lett. 23:95-101.
    • (1984) FEMS Microbiol. Lett. , vol.23 , pp. 95-101
    • Pedrosa, F.O.1    Yates, M.G.2
  • 31
    • 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
  • 32
    • 0027326681 scopus 로고
    • Site-directed mutagenesis of the target arginine for ADP-ribosylation of nitrogenase component II in Rhodobacter capsulatus
    • Pierrard, J., J. C. Willison, P. M. Vignais, J. L. Gaspar, P. W. Ludden, and G. P. Roberts. 1993. Site-directed mutagenesis of the target arginine for ADP-ribosylation of nitrogenase component II in Rhodobacter capsulatus. Biochem. Biophys. Res. Commun. 192:1223-1229.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 1223-1229
    • Pierrard, J.1    Willison, J.C.2    Vignais, P.M.3    Gaspar, J.L.4    Ludden, P.W.5    Roberts, G.P.6
  • 33
    • 0021821712 scopus 로고
    • Covalent modification of the iron protein of nitrogenase from Rhodospirillum rubrum by adenosine diphosphoribosylation of a specific arginine residue
    • Pope, M. R., S. A. Murrell, and P. W. Ludden. 1985. Covalent modification of the iron protein of nitrogenase from Rhodospirillum rubrum by adenosine 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    Murrell, S.A.2    Ludden, P.W.3
  • 34
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 35
    • 0018068329 scopus 로고
    • A taxonomic study of the Spirillum lipoferum group, with descriptions of a new genus, Azospirillum gen. nov. and two species, Azospirillum lipoferum (Beijerinck) comb. nov. and Azospirillum brasilense sp. nov
    • Tarrand, J. J., N. R. Krieg, and J. Döbereiner. 1978. A taxonomic study of the Spirillum lipoferum group, with descriptions of a new genus, Azospirillum gen. nov. and two species, Azospirillum lipoferum (Beijerinck) comb. nov. and Azospirillum brasilense sp. nov. Can. J. Microbiol. 24:967-980.
    • (1978) Can. J. Microbiol. , vol.24 , pp. 967-980
    • Tarrand, J.J.1    Krieg, N.R.2    Döbereiner, J.3
  • 36
    • 0021298879 scopus 로고
    • Analysis of copy number control elements in the region of the vegetative replication origin of broad host range plasmid PR2
    • Thomas, C. M., M. A. Cross, A. A. K. Hussain, and C. A. Smith. 1984. Analysis of copy number control elements in the region of the vegetative replication origin of broad host range plasmid PR2. EMBO J. 3:57-63.
    • (1984) EMBO J. , vol.3 , pp. 57-63
    • Thomas, C.M.1    Cross, M.A.2    Hussain, A.A.K.3    Smith, C.A.4
  • 37
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: 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.1    Staehelin, T.2    Gordon, J.3
  • 38
    • 0020442864 scopus 로고
    • The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • Vieira, J., and J. Messing. 1982. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19:259-268.
    • (1982) Gene , vol.19 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 39
    • 0026709637 scopus 로고
    • Ionic interactions in the nitrogenase complex: Properties of Fc-protein containing substitutions for Arg-100
    • Wolle, D., C. Kim, D. Dean, and J. B. Howard. 1992. Ionic interactions in the nitrogenase complex: properties of Fc-protein containing substitutions for Arg-100. J. Biol. Chem. 267:3667-3673.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3667-3673
    • Wolle, D.1    Kim, C.2    Dean, D.3    Howard, J.B.4
  • 40
    • 0024004559 scopus 로고
    • Ammonia switch-off of nitrogenase from Rhodobacter sphaeroides and Methylosinus trichosporium: No evidence for Fe protein modification
    • Yoch, D. C., J. Li, C.-Z. Hu, and C. Scholin. 1988. Ammonia switch-off of nitrogenase from Rhodobacter sphaeroides and Methylosinus trichosporium: no evidence for Fe protein modification. Arch. Microbiol. 150:1-5.
    • (1988) Arch. Microbiol. , vol.150 , pp. 1-5
    • Yoch, D.C.1    Li, J.2    Hu, C.-Z.3    Scholin, C.4
  • 41
    • 0023359283 scopus 로고
    • DNA mismatch-repair in Escherichia coli counteracting the hydrolytic deamination of 5-methyl-cytosine residue
    • Zell, R., and H.-J. Fritz. 1987. DNA mismatch-repair in Escherichia coli counteracting the hydrolytic deamination of 5-methyl-cytosine residue. EMBO J. 6:1809-1815.
    • (1987) EMBO J. , vol.6 , pp. 1809-1815
    • Zell, R.1    Fritz, H.-J.2
  • 42
    • 0027485991 scopus 로고
    • Posttranslational regulation of nitrogenase activity by anaerobiosis and ammonium in Azospirillum brasilenst
    • Zhang, Y., R. H. Burris, P. W. Ludden, and G. P. Roberts. 1993. Posttranslational regulation of nitrogenase activity by anaerobiosis and ammonium in Azospirillum brasilenst. 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
  • 43
    • 0029041228 scopus 로고
    • Comparison studies of dinitrogenase reductase ADP-ribosyl transferase/dinitrogenase reductase activating glycohydrolase regulatory systems in Rhodospirillum rubrum and Azospirillum brasilense
    • Zhang, Y., R. H. Burris, P. W. Ludden, and G. P. Roberts. 1995. Comparison studies of dinitrogenase reductase ADP-ribosyl transferase/dinitrogenase reductase activating glycohydrolase regulatory systems in Rhodospirillum rubrum and Azospirillum brasilense. J. Bacteriol. 177:2354-2359.
    • (1995) J. Bacteriol. , vol.177 , pp. 2354-2359
    • Zhang, Y.1    Burris, R.H.2    Ludden, P.W.3    Roberts, G.P.4
  • 44
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.