메뉴 건너뛰기




Volumn 69, Issue 3, 2003, Pages 1527-1531

Fnr is involved in oxygen control of Herbaspirillum seropedicae N-truncated NifA protein activity in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

DEGRADATION; ESCHERICHIA COLI; MECHANISMS; OXYGEN;

EID: 0037337661     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.69.3.1527-1531.2003     Document Type: Article
Times cited : (7)

References (34)
  • 1
    • 2542509740 scopus 로고    scopus 로고
    • Studies on the roles of GlnK and GlnB in regulating Klebsiella pneumoniae NifL-dependent nitrogen control
    • Arcondeguy, T., W. C. van Heeswijk, and M. Merrick. 1999. Studies on the roles of GlnK and GlnB in regulating Klebsiella pneumoniae NifL-dependent nitrogen control. FEMS Microbiol Lett. 180:263-270.
    • (1999) FEMS Microbiol. Lett. , vol.180 , pp. 263-270
    • Arcondeguy, T.1    Van Heeswijk, W.C.2    Merrick, M.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
    • 0025058956 scopus 로고
    • Characterisation of the Klebsiella pneumoniae nitrogen-fixation regulatory proteins NIFA and NIFL in vitro
    • Austin, S., N. Henderson, and R. Dixon. 1990. Characterisation of the Klebsiella pneumoniae nitrogen-fixation regulatory proteins NIFA and NIFL in vitro. Eur. J. Biochem. 187:353-360.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 353-360
    • Austin, S.1    Henderson, N.2    Dixon, R.3
  • 4
    • 0022629490 scopus 로고
    • Characterization of Herbaspirillum seropedicae gen. nov., sp. nov., a root-associated nitrogen-fixing bacterium
    • Baldani, J. I., V. L. D. Baldani, L. Seldin, and J. Dobereiner. 1986. Characterization of Herbaspirillum seropedicae gen. nov., sp. nov., a root-associated nitrogen-fixing bacterium. Int. J. Syst. Bacteriol. 36:86-93.
    • (1986) Int. J. Syst. Bacteriol. , vol.36 , pp. 86-93
    • Baldani, J.I.1    Baldani, V.L.D.2    Seldin, L.3    Dobereiner, J.4
  • 5
    • 0030746346 scopus 로고    scopus 로고
    • Evidence for two possible glnB-type genes in Herbaspirillum seropedicae
    • Benelli, E. M., E. M. Souza, S. Funayama, L. U. Rigo, and F. O. Pedrosa. 1997. Evidence for two possible glnB-type genes in Herbaspirillum seropedicae. J. Bacteriol. 179:4623-4626.
    • (1997) J. Bacteriol. , vol.179 , pp. 4623-4626
    • Benelli, E.M.1    Souza, E.M.2    Funayama, S.3    Rigo, L.U.4    Pedrosa, F.O.5
  • 6
    • 0019551730 scopus 로고
    • "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette, W. N. 1981. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112:195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 7
    • 0017694882 scopus 로고
    • Complementation analysis of Klebsiella pneumoniae mutants defective in nitrogen fixation
    • Dixon, R., C. Kennedy, A. Kondorosi, V. Krishnapillai, and M. Merrick. 1977. Complementation analysis of Klebsiella pneumoniae mutants defective in nitrogen fixation. Mol. Gen. Genet. 157:189-198.
    • (1977) Mol. Gen. Genet. , vol.157 , pp. 189-198
    • Dixon, R.1    Kennedy, C.2    Kondorosi, A.3    Krishnapillai, V.4    Merrick, M.5
  • 8
    • 0028108941 scopus 로고
    • Genetic regulation of nitrogen fixation in rhizobia
    • Fischer, H. 1994. Genetic regulation of nitrogen fixation in rhizobia. Microbiol. Rev. 58:352-386.
    • (1994) Microbiol. Rev. , vol.58 , pp. 352-386
    • Fischer, H.1
  • 9
    • 0024296535 scopus 로고
    • Essential and non-essential domains in the Bradyrhizobium japonicum NifA protein: Identification of indispensable cysteine residues potentially involved in redox reactivity and/or metal binding
    • Fischer, H. M., T. Bruderer, and H. Hennecke. 1988. Essential and non-essential domains in the Bradyrhizobium japonicum NifA protein: identification of indispensable cysteine residues potentially involved in redox reactivity and/or metal binding. Nucleic Acids Res. 16:2207-2224.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 2207-2224
    • Fischer, H.M.1    Bruderer, T.2    Hennecke, H.3
  • 10
    • 0035140627 scopus 로고    scopus 로고
    • Fnr is required for NifL-dependent oxygen control of nif gene expression in Klebsiella pneumoniae
    • Grabbe, R., K. Klopprogge, and R. A. Schmitz. 2001. Fnr is required for NifL-dependent oxygen control of nif gene expression in Klebsiella pneumoniae. J. Bacteriol. 183:1385-1393.
    • (2001) J. Bacteriol. , vol.183 , pp. 1385-1393
    • Grabbe, R.1    Klopprogge, K.2    Schmitz, R.A.3
  • 11
    • 0029797082 scopus 로고    scopus 로고
    • Reconstitution of the [4Fe-4S] cluster in FNR and demonstration of the aerobic-anaerobic transcription switch in vitro
    • Green, J., B. Bennett, P. Jordan, E. T. Ralph, A. J. Thomson, and J. R. Guest. 1996. Reconstitution of the [4Fe-4S] cluster in FNR and demonstration of the aerobic-anaerobic transcription switch in vitro. Biochem. J. 316:887-892.
    • (1996) Biochem. J. , vol.316 , pp. 887-892
    • Green, J.1    Bennett, B.2    Jordan, P.3    Ralph, E.T.4    Thomson, A.J.5    Guest, J.R.6
  • 12
    • 0032428697 scopus 로고    scopus 로고
    • Physiological role for the GlnK protein of enteric bacteria: Relief of NifL inhibition under nitrogenlimiting conditions
    • He, L., E. Soupene, A. Ninfa, and S. Kustu. 1998. Physiological role for the GlnK protein of enteric bacteria: relief of NifL inhibition under nitrogenlimiting 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
  • 13
    • 0029875231 scopus 로고    scopus 로고
    • Azotobacter vinelandii NIFL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via a redox-sensitive switch
    • Hill, S., S. Austin, T. Eydmann, T. Jones, and R. Dixon. 1996. Azotobacter vinelandii NIFL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via a redox-sensitive switch. Proc. Natl. Acad. Sci. USA 93:2143-2148.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2143-2148
    • Hill, S.1    Austin, S.2    Eydmann, T.3    Jones, T.4    Dixon, R.5
  • 14
    • 0026074114 scopus 로고
    • Aerobic inactivation of Rhizobium meliloti NifA in Escherichia coli is mediated by lon and two newly identified genes, snoB and snoC
    • Huala, E., A. L. Moon, and F. M. Ausubel. 1991. Aerobic inactivation of Rhizobium meliloti NifA in Escherichia coli is mediated by lon and two newly identified genes, snoB and snoC. J. Bacteriol. 173:382-390.
    • (1991) J. Bacteriol. , vol.173 , pp. 382-390
    • Huala, E.1    Moon, A.L.2    Ausubel, F.M.3
  • 15
    • 0033061058 scopus 로고    scopus 로고
    • The signal transduction protein GnlK is required for NifL-dependent nitrogen control of nif gene expression in Klebsiella pneumoniae
    • Jack, R., M. de Zamaroczy, and M. Merrick. 1999. The signal transduction protein GnlK is required for NifL-dependent nitrogen control of nif gene 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
  • 17
    • 0023785910 scopus 로고
    • Construction of multicopy expression vectors for regulated over-production of proteins in Klebsiella pneumoniae and other enteric bacteria
    • Kleiner, D., W. Paul, and M. J. Merrick. 1988. Construction of multicopy expression vectors for regulated over-production of proteins in Klebsiella pneumoniae and other enteric bacteria. J. Gen. Microbiol. 134:1779-1784.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1779-1784
    • Kleiner, D.1    Paul, W.2    Merrick, M.J.3
  • 18
    • 0032898919 scopus 로고    scopus 로고
    • NifL of Klebsiella pneumoniae: Redox characterization in relation to the nitrogen source
    • Klopprogge, K., and R. A. Schmitz. 1999. NifL of Klebsiella pneumoniae: redox characterization in relation to the nitrogen source. Biochim. Biophys. Acta 1431:462-470.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 462-470
    • Klopprogge, K.1    Schmitz, R.A.2
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T7
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T7. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0034669188 scopus 로고    scopus 로고
    • Signal transduction to the Azotobacter vinelandii NIFL-NIFA regulatory system is influenced directly by interaction with 2-oxoglutarate and the PII regulatory protein
    • Little, R., F. Reyes-Ramirez, Y. Zhang, W. C. van Heeswijk, and R. Dixon. 2000. Signal transduction to the Azotobacter vinelandii NIFL-NIFA regulatory system is influenced directly by interaction with 2-oxoglutarate and the PII regulatory protein. EMBO J. 19:6041-6050.
    • (2000) EMBO J. , vol.19 , pp. 6041-6050
    • Little, R.1    Reyes-Ramirez, F.2    Zhang, Y.3    Van Heeswijk, W.C.4    Dixon, R.5
  • 21
    • 0037013219 scopus 로고    scopus 로고
    • Direct interaction of the NIFL regulatory protein with the GLNK signal transducer enables the Azotobacter vinelandii NIFL-NIFA regulatory system to respond to conditions replete for nitrogen
    • Little, R., V. Colombo, A. Leech, and R. Dixon. 2002. Direct interaction of the NIFL regulatory protein with the GLNK signal transducer enables the Azotobacter vinelandii NIFL-NIFA regulatory system to respond to conditions replete for nitrogen. J. Biol. Chem. 277:15472-15481.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15472-15481
    • Little, R.1    Colombo, V.2    Leech, A.3    Dixon, R.4
  • 22
    • 0242560412 scopus 로고    scopus 로고
    • Ph.D. thesis. Universidade Federal do Paraná, Curitiba, Brazil
    • Machado, I. M. P. 1999. Ph.D. thesis. Universidade Federal do Paraná, Curitiba, Brazil.
    • (1999)
    • Machado, I.M.P.1
  • 24
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1990. Experiments in molecular genetics, p. 325-355. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1990) Experiments in Molecular Genetics , pp. 325-355
    • Miller, J.H.1
  • 25
    • 0033046312 scopus 로고    scopus 로고
    • Expression and functional analysis of an N-truncated NifA protein of Herbaspirillum seropedicae
    • Monteiro, R. A., E. M. Souza, S. Funayama, M. G. Yates, F. O. Pedrosa, and L. S. Chubatsu. 1999. Expression and functional analysis of an N-truncated NifA protein of Herbaspirillum seropedicae. FEBS Lett. 447:283-286.
    • (1999) FEBS Lett. , vol.447 , pp. 283-286
    • Monteiro, R.A.1    Souza, E.M.2    Funayama, S.3    Yates, M.G.4    Pedrosa, F.O.5    Chubatsu, L.S.6
  • 26
    • 0032733250 scopus 로고    scopus 로고
    • In-trans regulation of the N-truncated-NifA protein of Herbaspirillum seropedicae by the N-terminal domain
    • Monteiro, R. A., E. M. Souza, M. G. Yates, F. O. Pedrosa, and L. S. Chubatsu. 1999. In-trans regulation of the N-truncated-NifA protein of Herbaspirillum seropedicae by the N-terminal domain. FEMS Microbiol Lett. 180:157-161.
    • (1999) FEMS Microbiol. Lett. , vol.180 , pp. 157-161
    • Monteiro, R.A.1    Souza, E.M.2    Yates, M.G.3    Pedrosa, F.O.4    Chubatsu, L.S.5
  • 27
    • 0025909998 scopus 로고
    • Influence of oxygen on DNA binding, positive control, and stability of the Bradyrhizobium japonicum NifA regulatory protein
    • Morret, E., H. M. Fischer, and H. Hennecke. 1991. Influence of oxygen on DNA binding, positive control, and stability of the Bradyrhizobium japonicum NifA regulatory protein. J. Bacteriol. 173:3478-3487.
    • (1991) J. Bacteriol. , vol.173 , pp. 3478-3487
    • Morret, E.1    Fischer, H.M.2    Hennecke, H.3
  • 30
    • 0036174645 scopus 로고    scopus 로고
    • Role of GlnK in NifL-mediated regulation of NifA activity in Azotobacter vinelandii
    • Rudnik, P., C. Kunz, M. K. Gunattilaka, E. R. Hines, and C. Kennedy. 2002. Role of GlnK in NifL-mediated regulation of NifA activity in Azotobacter vinelandii. J. Bacteriol. 184:812-820.
    • (2002) J. Bacteriol. , vol.184 , pp. 812-820
    • Rudnik, P.1    Kunz, C.2    Gunattilaka, M.K.3    Hines, E.R.4    Kennedy, C.5
  • 31
    • 0020398202 scopus 로고
    • Amplification and product identification of the fnr gene of Escherichia coli
    • Shaw, D. J., and J. R. Guest. 1982. Amplification and product identification of the fnr gene of Escherichia coli. J. Gen. Microbiol. 128:2221-2228.
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 2221-2228
    • Shaw, D.J.1    Guest, J.R.2
  • 32
    • 0032956540 scopus 로고    scopus 로고
    • Control of Herbaspirillum seropedicae NifA activity by ammonium ions and oxygen
    • Souza, E. M., F. O. Pedrosa, M. Drummond, L. U. Rigo, and M. G. Yates. 1999. Control of Herbaspirillum seropedicae NifA activity by ammonium ions and oxygen. J. Bacteriol. 181:681-684.
    • (1999) J. Bacteriol. , vol.181 , pp. 681-684
    • Souza, E.M.1    Pedrosa, F.O.2    Drummond, M.3    Rigo, L.U.4    Yates, M.G.5
  • 33
    • 0024117670 scopus 로고
    • Inactivation of the FNR protein of Escherichia coli by targeted mutagenesis in the N-terminal region
    • Spiro, S., and J. R. Guest. 1988. Inactivation of the FNR protein of Escherichia coli by targeted mutagenesis in the N-terminal region. Mol. Microbiol. 2:701-707.
    • (1988) Mol. Microbiol. , vol.2 , pp. 701-707
    • Spiro, S.1    Guest, J.R.2
  • 34
    • 0030756106 scopus 로고    scopus 로고
    • The oxygen-responsive transcriptional regulator FNR of Escherichia coli: The search for signals and reactions
    • Unden, G., and J. Schirawski. 1997. The oxygen-responsive transcriptional regulator FNR of Escherichia coli: the search for signals and reactions. Mol. Microbiol. 25:205-210.
    • (1997) Mol. Microbiol. , vol.25 , pp. 205-210
    • Unden, G.1    Schirawski, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.