메뉴 건너뛰기




Volumn 180, Issue 23, 1998, Pages 6392-6395

Short-term regulation of nitrogenase activity by NH4+ in Rhodobacter capsulatus: Multiple in vivo nitrogenase responses to NH4+ addition

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; NITROGENASE;

EID: 0031725646     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.23.6392-6395.1998     Document Type: Article
Times cited : (31)

References (27)
  • 1
    • 0019789593 scopus 로고
    • Nitrogenase switch-off by ammonia in Rhodopseudomonas palustris: Loss under nitrogen deficiency and independence from the adenylylation state of glutamine synthetase
    • Alef, K., D. J. Arp, and W. G. Zumft. 1981. Nitrogenase switch-off by ammonia in Rhodopseudomonas palustris: loss under nitrogen deficiency and independence from the adenylylation state of glutamine synthetase. Arch. Microbiol. 130:138-142.
    • (1981) Arch. Microbiol. , vol.130 , pp. 138-142
    • Alef, K.1    Arp, D.J.2    Zumft, W.G.3
  • 2
    • 0023216113 scopus 로고
    • Ammonium and methylammonium transport in Rhodobacter sphaeroides
    • Cordts, M. L., and J. Gibson. 1987. Ammonium and methylammonium transport in Rhodobacter sphaeroides. J. Bacteriol. 169:1632-1636.
    • (1987) J. Bacteriol. , vol.169 , pp. 1632-1636
    • Cordts, M.L.1    Gibson, J.2
  • 3
    • 0020072790 scopus 로고
    • Nitrogenase from the photosynthetic bacterium Rhodopseudomonas capsulata: Purification and molecular properties
    • Hallenbeck, P. C., C. M. Meyer, and P. M. Vignais. 1982. Nitrogenase from the photosynthetic bacterium Rhodopseudomonas capsulata: purification and molecular properties. J. Bacteriol. 149:708-717.
    • (1982) J. Bacteriol. , vol.149 , pp. 708-717
    • Hallenbeck, P.C.1    Meyer, C.M.2    Vignais, P.M.3
  • 4
    • 0026547250 scopus 로고
    • Mutations affecting nitrogenase switch-off in Rhodobacter capsulatus
    • Hallenbeck, P. C. 1992. Mutations affecting nitrogenase switch-off in Rhodobacter capsulatus. Biochim. Biophys. Acta 1118:161-168.
    • (1992) Biochim. Biophys. Acta , vol.1118 , pp. 161-168
    • Hallenbeck, P.C.1
  • 5
    • 0030596516 scopus 로고    scopus 로고
    • Salmonella typhimurium apparently perceives external nitrogen limitation as internal glutamine limitation
    • Ikeda, T. P., A. E. Schauger, and S. Kustu. 1996. Salmonella typhimurium apparently perceives external nitrogen limitation as internal glutamine limitation. J. Mol. Biol. 259:589-607.
    • (1996) J. Mol. Biol. , vol.259 , pp. 589-607
    • Ikeda, T.P.1    Schauger, A.E.2    Kustu, S.3
  • 6
    • 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
  • 7
    • 0018676861 scopus 로고
    • Glutamine as feedback inhibitor of the Rhodopseudomonas sphaeroides nitrogenase system
    • Jones, B. L., and K. J. Monty. 1979. Glutamine as 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
  • 8
    • 0000601106 scopus 로고
    • Regulation of nitrogenase activity through iron protein interconversion into an active and inactive form in Rhodopseudomonas capsulata
    • Jouanneau, Y., C. M. Meyer, and P. M. Vignais. 1983. Regulation of nitrogenase activity through iron protein interconversion into an active and inactive form in Rhodopseudomonas capsulata. Biochim. Biophys. Acta 749:318-328.
    • (1983) Biochim. Biophys. Acta , vol.749 , pp. 318-328
    • Jouanneau, Y.1    Meyer, C.M.2    Vignais, P.M.3
  • 9
    • 0005682214 scopus 로고
    • Ammonia and light effect on nitrogenase activity in nitrogen-limited continuous culture of Rhodopseudomonas capsulata. Role of glutamine synthetase
    • Jouanneau, Y., S. Lebecque, and P. M. Vignais. 1984. Ammonia and light effect on nitrogenase activity in nitrogen-limited continuous culture of Rhodopseudomonas capsulata. Role of glutamine synthetase. Arch. Microbiol. 139:326-331.
    • (1984) Arch. Microbiol. , vol.139 , pp. 326-331
    • Jouanneau, Y.1    Lebecque, S.2    Vignais, P.M.3
  • 10
    • 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
  • 11
    • 0021114552 scopus 로고
    • 2 fixing bacteria, and its effect on ammonium transport
    • 2 fixing bacteria, and its effect on ammonium transport. FEBS Lett. 164:121-123.
    • (1983) FEBS Lett. , vol.164 , pp. 121-123
    • Kleiner, D.1    Alef, K.2    Hartman, A.3
  • 12
    • 0021796811 scopus 로고
    • Bacterial ammonium transport
    • Kleiner, D. 1985. Bacterial ammonium transport. FEMS Microbiol. Rev. 32:87-100.
    • (1985) FEMS Microbiol. Rev. , vol.32 , pp. 87-100
    • Kleiner, D.1
  • 13
    • 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
  • 14
    • 0022596239 scopus 로고
    • Reversible regulation of the nitrogenase iron protein from Rhodospirillum rubrum by ADP-ribosylation in vitro
    • Lowery, R. G., L. L. Saari, and P. W. Ludden. 1986. Reversible regulation of the nitrogenase iron protein from Rhodospirillum rubrum by ADP-ribosylation in vitro. J. Bacteriol. 166:513-518.
    • (1986) J. Bacteriol. , vol.166 , pp. 513-518
    • Lowery, R.G.1    Saari, L.L.2    Ludden, P.W.3
  • 15
    • 0002886141 scopus 로고
    • The biochemistry and genetics of nitrogen fixation by photosynthetic bacteria
    • R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.) Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Ludden, P. W., and G. P. Roberts. 1995. The biochemistry and genetics of nitrogen fixation by photosynthetic bacteria, p. 929-947. In R. E. Blankenship, M. T. Madigan, and C. E. Bauer (ed.), Anoxygenic photosynthetic bacteria. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 929-947
    • Ludden, P.W.1    Roberts, G.P.2
  • 16
    • 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
  • 17
    • 0020560286 scopus 로고
    • 14C-labelling of glutamine synthetase and Fe-protein of nitrogenase in toluene-treated cells of Rhodopseudomonas capsulata
    • 14C-labelling of glutamine synthetase and Fe-protein of nitrogenase in toluene-treated cells of Rhodopseudomonas capsulata. Biochim. Biophys. Acta 743:136-148.
    • (1983) Biochim. Biophys. Acta , vol.743 , pp. 136-148
    • Michalski, W.P.1    Nicholas, D.J.D.2    Vignais, P.M.3
  • 18
    • 1542285610 scopus 로고
    • The rapid switch-off of nitrogenase activity in obligate methane-oxidizing bacteria
    • Murrell, J. C. 1988. The rapid switch-off of nitrogenase activity in obligate methane-oxidizing bacteria. Arch. Microbiol. 150:489-495.
    • (1988) Arch. Microbiol. , vol.150 , pp. 489-495
    • Murrell, J.C.1
  • 19
    • 0027418844 scopus 로고
    • Posttranslational regulation of nitrogenase in Rhodobacler capsulatus: Existence of two independent regulatory effects of ammonium
    • Pierrard, J., P. W. Ludden, and G. P. Roberts. 1993. Posttranslational regulation of nitrogenase in Rhodobacler 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
  • 20
    • 0022904669 scopus 로고
    • Methylammonium uptake by Rhodobacter capsulatus
    • Rapp, B. J., D. C. Landrum, and J. D. Wall. 1986. Methylammonium uptake by Rhodobacter capsulatus. Arch. Microbiol. 146:134-141.
    • (1986) Arch. Microbiol. , vol.146 , pp. 134-141
    • Rapp, B.J.1    Landrum, D.C.2    Wall, J.D.3
  • 21
    • 0022598142 scopus 로고
    • Short-term effect of ammonia on nitrogenase activity of Anabaena variabilis (ATCC 29413)
    • Reich, S., H. Almon, and P. Böger. 1986. Short-term effect of ammonia on nitrogenase activity of Anabaena variabilis (ATCC 29413). FEMS Microbiol. Lett. 34:53-62.
    • (1986) FEMS Microbiol. Lett. , vol.34 , pp. 53-62
    • Reich, S.1    Almon, H.2    Böger, P.3
  • 22
    • 77956999268 scopus 로고
    • Glutamine synthetase (Escherichia coli)
    • Shapiro, B. M., and E. R. Stadtman. 1970. Glutamine synthetase (Escherichia coli). Methods Enzymol. 17A:910-922.
    • (1970) Methods Enzymol. , vol.17 A , pp. 910-922
    • Shapiro, B.M.1    Stadtman, E.R.2
  • 23
    • 84944813042 scopus 로고
    • Determination of ammonia in natural sea water by the phenolhypochlorite method
    • Solorzano, L. 1969. Determination of ammonia in natural sea water by the phenolhypochlorite method. Limnol. Oceanogr. 14:799-801.
    • (1969) Limnol. Oceanogr. , vol.14 , pp. 799-801
    • Solorzano, L.1
  • 25
    • 15644381708 scopus 로고
    • Effect of ammonium on nitrogenase activity in the heterocystous cyanobacterium Anabaena variabilis
    • Yakunin, A. F., O. Y. Troshina, M. Jha, and I. N. Gogotov. 1992. Effect of ammonium on nitrogenase activity in the heterocystous cyanobacterium Anabaena variabilis. Mikrobiologiya 61:256-260.
    • (1992) Mikrobiologiya , vol.61 , pp. 256-260
    • Yakunin, A.F.1    Troshina, O.Y.2    Jha, M.3    Gogotov, I.N.4
  • 26
    • 0032502814 scopus 로고    scopus 로고
    • A luminol/iodophenol chemiluminescent detection system for Western immunoblots
    • Yakunin, A. F., and P. C. Hallenbeck. 1998. A luminol/iodophenol chemiluminescent detection system for Western immunoblots. Anal. Biochem. 258:146-149.
    • (1998) Anal. Biochem. , vol.258 , pp. 146-149
    • Yakunin, A.F.1    Hallenbeck, P.C.2
  • 27
    • 0017806548 scopus 로고
    • Regulatory properties of the nitrogenase from Rhodopseudomonas palustris
    • Zumft, W. G., and F. Castillo. 1978. Regulatory properties of the nitrogenase from Rhodopseudomonas palustris. Arch. Microbiol. 117:53-60.
    • (1978) Arch. Microbiol. , vol.117 , pp. 53-60
    • Zumft, W.G.1    Castillo, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.