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Volumn 270, Issue 7, 2003, Pages 1555-1566

Oxygen control of nif gene expression in Klebsiella pneumoniae depends on NifL reduction at the cytoplasmic membrane by electrons derived from the reduced quinone pool

Author keywords

FNR; Klebsiella pneumoniae; NifL; Nitrogen fixation; Quinol quinone ratio

Indexed keywords

DIMETHYL NAPHTHOQUINOL; FLAVOPROTEIN; FORMATE DEHYDROGENASE; GLYCEROL; MENADIOL; NITRATE; NITROGEN; OXYGEN; PROTEIN NIFL; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UNCLASSIFIED DRUG;

EID: 0037392283     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03520.x     Document Type: Article
Times cited : (24)

References (64)
  • 1
    • 0031924101 scopus 로고    scopus 로고
    • The oxygen-responsive NIFL-NIFA complex: A novel two-component regulatory system controlling nitrogenase synthesis in gamma-proteobacteria
    • Dixon, R. (1998) The oxygen-responsive NIFL-NIFA complex: a novel two-component regulatory system controlling nitrogenase synthesis in gamma-proteobacteria. Arch. Microbiol. 169, 371-380.
    • (1998) Arch. Microbiol. , vol.169 , pp. 371-380
    • Dixon, R.1
  • 2
    • 0036198623 scopus 로고    scopus 로고
    • Regulation of nitrogen fixation in Klebsiella pneumoniae and Azotobacter vinelandii: NifL, transducing two environmental signals to the nif transcriptional activator NifA
    • Schmitz, R.A., Klopprogge, K. & Grabbe, R. (2002) Regulation of nitrogen fixation in Klebsiella pneumoniae and Azotobacter vinelandii: NifL, transducing two environmental signals to the nif transcriptional activator NifA. J. Mol. Microbiol. Biotechnol. 4, 235-242.
    • (2002) J. Mol. Microbiol. Biotechnol. , vol.4 , pp. 235-242
    • Schmitz, R.A.1    Klopprogge, K.2    Grabbe, R.3
  • 3
    • 2642677678 scopus 로고    scopus 로고
    • Mechanism of translational coupling in the nifLA operon of Klebsiella pneumoniae
    • Govantes, F., Andujar, E. & Santero, E. (1998) Mechanism of translational coupling in the nifLA operon of Klebsiella pneumoniae. EMBO J. 17, 2368-2377.
    • (1998) EMBO J. , vol.17 , pp. 2368-2377
    • Govantes, F.1    Andujar, E.2    Santero, E.3
  • 4
    • 0001645845 scopus 로고
    • Role of metal ions in negative regulation of nitrogen fixation by the nifL gene product from Klebsiella pneumoniae
    • Henderson, N., Austin, S. & Dixon, R.A. (1989) Role of metal ions in negative regulation of nitrogen fixation by the nifL gene product from Klebsiella pneumoniae. Mol. General Genet. 216, 484-491.
    • (1989) Mol. General Genet , vol.216 , pp. 484-491
    • Henderson, N.1    Austin, S.2    Dixon, R.A.3
  • 5
    • 0032765524 scopus 로고    scopus 로고
    • Isolation and properties of the complex between the enhancer binding protein NifA and the sensor NifL
    • Money T., Jones, T., Dixon, R. & Austin, S. (1999) Isolation and properties of the complex between the enhancer binding protein NifA and the sensor NifL. J. Bacteriol. 181, 4461-4468.
    • (1999) J. Bacteriol. , vol.181 , pp. 4461-4468
    • Money, T.1    Jones, T.2    Dixon, R.3    Austin, S.4
  • 6
    • 0032719343 scopus 로고    scopus 로고
    • Genetic analysis of nif regulatory genes by utilizing the yeast two-hybrid system detected formation of a NifL-NifA complex that is implicated in regulated expression of nif genes
    • Lei, S., Pulakat, L. & Gavini, N. (1999) Genetic analysis of nif regulatory genes by utilizing the yeast two-hybrid system detected formation of a NifL-NifA complex that is implicated in regulated expression of nif genes. J. Bacteriol. 181, 6535-6539.
    • (1999) J. Bacteriol. , vol.181 , pp. 6535-6539
    • Lei, S.1    Pulakat, L.2    Gavini, N.3
  • 7
    • 0035143627 scopus 로고    scopus 로고
    • Protein-protein interactions in the complex between the enhancer binding protein NifA and the sensor NifL from Azotobacter vinelandii
    • Money, T., Barrett, J., Dixon, R. & Austin, S. (2001) Protein-protein interactions in the complex between the enhancer binding protein NifA and the sensor NifL from Azotobacter vinelandii. J. Bacteriol. 183, 1359-1368.
    • (2001) J. Bacteriol. , vol.183 , pp. 1359-1368
    • Money, T.1    Barrett, J.2    Dixon, R.3    Austin, S.4
  • 8
    • 0032428697 scopus 로고    scopus 로고
    • Physiological role for the GlnK protein of enteric bacteria: Relief of NifL inhibition under nitrogen-limiting conditions
    • He, L., Soupene, E., Ninfa, A. & Kustu, S. (1998) Physiological role for the GlnK 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
  • 9
    • 0033061058 scopus 로고    scopus 로고
    • The signal transduction protein GlnK is required for NifL-dependent nitrogen control of nif gene expression in Klebsiella pneumoniae
    • Jack, R., De Zamaroczy, M. & Merrick, M. (1999) The signal transduction protein GlnK 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
  • 10
    • 2542509740 scopus 로고    scopus 로고
    • Studies on the roles of GlnK & GlnB in regulating Klebsiella pneumoniae NifL-dependent nitrogen control
    • Arcondeguy, T., van Heeswijk, W.C. & Merrick, M. (1999) Studies on the roles of GlnK & 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
  • 11
    • 0034623985 scopus 로고    scopus 로고
    • Two residues in the T-loop of GlnK determine NifL-dependent nitrogen control of nif gene expression
    • Arcondeguy, T., Lawson, D. & Merrick, M. (2000) Two residues in the T-loop of GlnK determine NifL-dependent nitrogen control of nif gene expression. J. Biol. Chem. 275, 38452-38456.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38452-38456
    • Arcondeguy, T.1    Lawson, D.2    Merrick, M.3
  • 12
    • 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., Reyes-Ramirez, F., Zhang, Y., van Heeswijk, W.C. & Dixon, R. (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
  • 13
    • 0035025555 scopus 로고    scopus 로고
    • Role of Escherichia coli nitrogen regulatory genes in the nitrogen response of the Azotobacter vinelandii NifL-NifA complex
    • Reyes-Ramirez, F., Little, R. & Dixon, R. (2001) Role of Escherichia coli nitrogen regulatory genes in the nitrogen response of the Azotobacter vinelandii NifL-NifA complex. J. Bacteriol. 183, 3076-3082.
    • (2001) J. Bacteriol. , vol.183 , pp. 3076-3082
    • Reyes-Ramirez, F.1    Little, R.2    Dixon, R.3
  • 14
    • 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., Colombo, V., Leech, A. & Dixon, R. (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
  • 15
    • 0036174645 scopus 로고    scopus 로고
    • Role of GlnK in NifL-mediated regulation of NifA activity in Azotobacter vinelandii
    • Rudnick, P., Kunz, C., Gunatilaka, M.K., Hines, E.R. & Kennedy, C. (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
    • Rudnick, P.1    Kunz, C.2    Gunatilaka, M.K.3    Hines, E.R.4    Kennedy, C.5
  • 16
    • 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., Austin, S., Eydmann, T., Jones, T. & Dixon, R. (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
  • 17
    • 0031573763 scopus 로고    scopus 로고
    • NifL of Klebsiella pneumoniae carries an N-terminally bound FAD cofactor, which is not directly required for the inhibitory function of NifL
    • Schmitz, R.A. (1997) NifL of Klebsiella pneumoniae carries an N-terminally bound FAD cofactor, which is not directly required for the inhibitory function of NifL. FEMS Microbiol. Lett. 157, 313-318.
    • (1997) FEMS Microbiol. Lett. , vol.157 , pp. 313-318
    • Schmitz, R.A.1
  • 19
    • 0032898919 scopus 로고    scopus 로고
    • NifL of Klebsiella pneumoniae: Redox characterization in relation to the nitrogen source
    • Klopprogge, K. & Schmitz, R.A. (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
  • 20
    • 0035140627 scopus 로고    scopus 로고
    • FNR Is required for NifL-dependent oxygen control of nif gene expression in Klebsiella pneumoniae
    • Grabbe, R., Klopprogge, K. & Schmitz, R.A. (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
  • 21
    • 0036191810 scopus 로고    scopus 로고
    • Membrane association of Klebsiella pneumoniae NifL is affected by molecular oxygen and combined nitrogen
    • Klopprogge, K., Grabbe, R., Hoppert, M. & Schmitz, R.A. (2002) Membrane association of Klebsiella pneumoniae NifL is affected by molecular oxygen and combined nitrogen. Arch. Microbiol. 177, 223-234.
    • (2002) Arch. Microbiol. , vol.177 , pp. 223-234
    • Klopprogge, K.1    Grabbe, R.2    Hoppert, M.3    Schmitz, R.A.4
  • 22
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue, H., Nojima, H. & Okayama, H. (1990) High efficiency transformation of Escherichia coli with plasmids. Gene 96, 23-28.
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 24
    • 0030722642 scopus 로고    scopus 로고
    • NtrC is required for control of Klebsiella pneumoniae NifL activity
    • He, L., Soupene, E. & Kustu, S. (1997) NtrC is required for control of Klebsiella pneumoniae NifL activity. J. Bacteriol. 179, 7446-7455.
    • (1997) J. Bacteriol. , vol.179 , pp. 7446-7455
    • He, L.1    Soupene, E.2    Kustu, S.3
  • 25
    • 0029086244 scopus 로고
    • A metabolic enzyme that rapidly produces superoxide, fumarate reductase of Escherichia coli
    • Imlay, J.A. (1995) A metabolic enzyme that rapidly produces superoxide, fumarate reductase of Escherichia coli. J. Biol. Chem. 270, 19767-19777.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19767-19777
    • Imlay, J.A.1
  • 26
    • 0019459906 scopus 로고
    • Regulation of nitrogen fixation in Klebsiella pneumoniae: Isolation and characterization of strains with nif-lac fusions
    • MacNeil, D., Zhu, J. & Brill, W.J. (1981) Regulation of nitrogen fixation in Klebsiella pneumoniae: isolation and characterization of strains with nif-lac fusions. J. Bacteriol. 145, 348-357.
    • (1981) J. Bacteriol. , vol.145 , pp. 348-357
    • MacNeil, D.1    Zhu, J.2    Brill, W.J.3
  • 27
    • 0029926274 scopus 로고    scopus 로고
    • Positive selection vectors for allelic exchange
    • Skorupsky, K. & Taylor, R.K. (1996) Positive selection vectors for allelic exchange. Gene 169, 47-52.
    • (1996) Gene , vol.169 , pp. 47-52
    • Skorupsky, K.1    Taylor, R.K.2
  • 28
    • 0025195680 scopus 로고
    • Mini-Tn5 Transposon Derivatives for Insertion Mutagenesis, Promoter Probing, and Chromosomal Insertion of Cloned DNA in Gram-Negative Eubacteria
    • DeLorenzo, V., Herrero, M., Jakubzik, U. & Timmis, K.N. (1990) Mini-Tn5 Transposon Derivatives for Insertion Mutagenesis, Promoter Probing, and Chromosomal Insertion of Cloned DNA in Gram-Negative Eubacteria. J. Bacteriol. 172, 6568-6572.
    • (1990) J. Bacteriol. , vol.172 , pp. 6568-6572
    • DeLorenzo, V.1    Herrero, M.2    Jakubzik, U.3    Timmis, K.N.4
  • 30
    • 9344269892 scopus 로고    scopus 로고
    • Iron is required to relieve inhibitory effects of NifL on transcriptional activation by NifA in Klebsiella pneumoniae
    • Schmitz, R.A., He, L. & Kustu, S. (1996) Iron is required to relieve inhibitory effects of NifL on transcriptional activation by NifA in Klebsiella pneumoniae. J. Bacteriol. 178, 4679-4687.
    • (1996) J. Bacteriol. , vol.178 , pp. 4679-4687
    • Schmitz, R.A.1    He, L.2    Kustu, S.3
  • 31
    • 0029143019 scopus 로고
    • The C-terminal domain of NifL is sufficient to inhibit NifA activity
    • Narberhaus, F., Lee, H.S., Schmitz, R.A., He, L. & Kustu, S. (1995) The C-terminal domain of NifL is sufficient to inhibit NifA activity. J. Bacteriol. 177, 5078-5087.
    • (1995) J. Bacteriol. , vol.177 , pp. 5078-5087
    • Narberhaus, F.1    Lee, H.S.2    Schmitz, R.A.3    He, L.4    Kustu, S.5
  • 32
    • 0021921011 scopus 로고
    • Maximizing gene expression from plasmid vectors containing the lambda PL promoter: Strategies for overproducing transcription termination factor-ρ
    • Mott, J.E., Grant, R.A., Ho, Y.S. & Platt, T. (1985) Maximizing gene expression from plasmid vectors containing the lambda PL promoter: Strategies for overproducing transcription termination factor-ρ. Proc. Natl. Acad. Sci. USA 82, 88-92.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 88-92
    • Mott, J.E.1    Grant, R.A.2    Ho, Y.S.3    Platt, T.4
  • 33
    • 0000171230 scopus 로고
    • A new method for preparing ravin-adenine dinucleotide
    • Whitby, L.G. (1953) A new method for preparing ravin-adenine dinucleotide. Biochem. J. 54, 437-442.
    • (1953) Biochem. J. , vol.54 , pp. 437-442
    • Whitby, L.G.1
  • 34
    • 0032781876 scopus 로고    scopus 로고
    • Na + translocation by the NADH:ubiquinone oxidoreductase (complex I) from Klebsiella pneumoniae
    • Krebs, W., Steuber, J., Gemperli, A.C. & Dimroth, P. (1999) Na + translocation by the NADH:ubiquinone oxidoreductase (complex I) from Klebsiella pneumoniae. Mol. Microbiol. 33, 590-598.
    • (1999) Mol. Microbiol. , vol.33 , pp. 590-598
    • Krebs, W.1    Steuber, J.2    Gemperli, A.C.3    Dimroth, P.4
  • 35
    • 0024635450 scopus 로고
    • A small isoform of NADH:ubiquinone oxidoreductase (complex I) without mitochondrially encoded subunits is made in chloramphenicol-treated Neurospora crassa
    • Friedrich, T., Hofhaus, G., Ise, W., Nehls, U., Schmitz, B. & Weiss, H. (1989) A small isoform of NADH:ubiquinone oxidoreductase (complex I) without mitochondrially encoded subunits is made in chloramphenicol-treated Neurospora crassa. Eur. J. Biochem. 180, 173-180.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 173-180
    • Friedrich, T.1    Hofhaus, G.2    Ise, W.3    Nehls, U.4    Schmitz, B.5    Weiss, H.6
  • 36
    • 0014949207 scopus 로고
    • Cleavage of the structural proteins during the assembly of the head of the Bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of the structural proteins during the assembly of the head of the Bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0021044309 scopus 로고
    • On the redox control of synthesis of anaerobically induced enzymes in enterobacteriaceae
    • Pecher, A., Zinoni, F., Jatisatienr, C., Wirth, R., Hennecke, H. & Böck, A. (1983) On the redox control of synthesis of anaerobically induced enzymes in enterobacteriaceae. Arch. Microbiol. 136, 131-136.
    • (1983) Arch. Microbiol. , vol.136 , pp. 131-136
    • Pecher, A.1    Zinoni, F.2    Jatisatienr, C.3    Wirth, R.4    Hennecke, H.5    Böck, A.6
  • 38
    • 0031909029 scopus 로고    scopus 로고
    • Genetic analysis of the nuo locus, which encodes the proton-translocating NADH dehydrogenase in Escherichia coli
    • Falk-Krzesinski, H.J. & Wolfe, A. (1998) Genetic analysis of the nuo locus, which encodes the proton-translocating NADH dehydrogenase in Escherichia coli. J. Bacteriol. 180, 1174-1184.
    • (1998) J. Bacteriol. , vol.180 , pp. 1174-1184
    • Falk-Krzesinski, H.J.1    Wolfe, A.2
  • 39
    • 0017243175 scopus 로고
    • Glycerol dissimilation and its regulation in bacteria
    • Lin, E.C.C. (1976) Glycerol dissimilation and its regulation in bacteria. Ann. Rev. Microbiol. 30, 535-578.
    • (1976) Ann. Rev. Microbiol. , vol.30 , pp. 535-578
    • Lin, E.C.C.1
  • 40
    • 0032518432 scopus 로고    scopus 로고
    • Changes in the proton potential and the cellular energetics of Escherichia coli during growth by aerobic and anaerobic respiration or by fermentation
    • Tran, Q.H. & Unden, G. (1998) Changes in the proton potential and the cellular energetics of Escherichia coli during growth by aerobic and anaerobic respiration or by fermentation. Eur. J. Biochem. 251, 538-543.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 538-543
    • Tran, Q.H.1    Unden, G.2
  • 41
    • 0033761635 scopus 로고    scopus 로고
    • Internal glutamine and glutamate pools in Klebsiella pneumoniae grown under different conditions of nitrogen availablity
    • Schmitz, R.A. (2000) Internal glutamine and glutamate pools in Klebsiella pneumoniae grown under different conditions of nitrogen availablity. Current Microbiol. 41, 357-362.
    • (2000) Current Microbiol. , vol.41 , pp. 357-362
    • Schmitz, R.A.1
  • 42
    • 0018900343 scopus 로고
    • Regulation of nitrogenase biosynthesis in Klebsiella pneumoniae: Effect of nitrate
    • Horn, S.S., Hennecke, H. & Shanmugam, K.T. (1980) Regulation of nitrogenase biosynthesis in Klebsiella pneumoniae: effect of nitrate. J. General Microbiol. 117, 169-179.
    • (1980) J. General Microbiol. , vol.117 , pp. 169-179
    • Horn, S.S.1    Hennecke, H.2    Shanmugam, K.T.3
  • 43
    • 0021144978 scopus 로고
    • The respiratory chains of Escherichia coli
    • Ingledew, W.J. & Poole, R.K. (1984) The respiratory chains of Escherichia coli. Microbiol. Rev. 48, 222-721.
    • (1984) Microbiol. Rev. , vol.48 , pp. 222-721
    • Ingledew, W.J.1    Poole, R.K.2
  • 44
    • 0019319527 scopus 로고
    • Isolation and functional aspects of the fumarate reductase involved in the phosphorylative electron transport of Vibrio succinogenes
    • Unden, G., Hackenberg, H. & Kröger, A. (1980) Isolation and functional aspects of the fumarate reductase involved in the phosphorylative electron transport of Vibrio succinogenes. Biochem. Biophyis. Acta 591, 275-288.
    • (1980) Biochem. Biophyis. Acta , vol.591 , pp. 275-288
    • Unden, G.1    Hackenberg, H.2    Kröger, A.3
  • 45
    • 0031047287 scopus 로고    scopus 로고
    • Requirement for the proton-pumping NADH dehydrogenase I of Escherichia coli in respiration of NADH to fumarate and its bioenergetic implications
    • Tran, Q.H., Bongaerts, J., Vlad, D. & Unden, G. (1997) Requirement for the proton-pumping NADH dehydrogenase I of Escherichia coli in respiration of NADH to fumarate and its bioenergetic implications. Eur. J. Biochem. 244, 155-160.
    • (1997) Eur. J. Biochem , vol.244 , pp. 155-160
    • Tran, Q.H.1    Bongaerts, J.2    Vlad, D.3    Unden, G.4
  • 46
    • 0034153610 scopus 로고    scopus 로고
    • Bacterial respiration: A flexible process for a changing environment
    • Richardson, D.J. (2000) Bacterial respiration: a flexible process for a changing environment. Microbiology 146, 551-571.
    • (2000) Microbiology , vol.146 , pp. 551-571
    • Richardson, D.J.1
  • 47
    • 0028264349 scopus 로고
    • Purification and in vitro activities of the native nitrogen fixation control proteins NifA and NifL
    • Austin, S., Buck, M., Cannon, W., Eydmann, T. & Dixon, R. (1994) Purification and in vitro activities of the native nitrogen fixation control proteins NifA and NifL. J. Bacteriol. 176, 3460-3465.
    • (1994) J. Bacteriol. , vol.176 , pp. 3460-3465
    • Austin, S.1    Buck, M.2    Cannon, W.3    Eydmann, T.4    Dixon, R.5
  • 48
    • 0028048861 scopus 로고
    • Oxygen reactions with bacterial oxidases and globins: Binding, reduction and regulation
    • Poole, R.K. (1994) Oxygen reactions with bacterial oxidases and globins: binding, reduction and regulation. Antonie Van Leuwenhoek 65, 289-310.
    • (1994) Antonie Van Leuwenhoek , vol.65 , pp. 289-310
    • Poole, R.K.1
  • 50
    • 0025368950 scopus 로고
    • Structural genes for nitrate-inducible formate dehydrogenase in Escherichia coli K-12
    • Berg, B.L. & Stewart, V. (1990) Structural genes for nitrate-inducible formate dehydrogenase in Escherichia coli K-12. Genetics 125, 691-702.
    • (1990) Genetics , vol.125 , pp. 691-702
    • Berg, B.L.1    Stewart, V.2
  • 51
    • 0027251261 scopus 로고
    • Dual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12
    • Rabin, R.S. & Stewart, V. (1993) Dual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12. J. Bacteriol. 175, 3259-3268.
    • (1993) J. Bacteriol. , vol.175 , pp. 3259-3268
    • Rabin, R.S.1    Stewart, V.2
  • 52
    • 0026020333 scopus 로고
    • Interspecies compatibility of selenoprotein biosynthesis in Enterobacteriaceae
    • Heider, J., Forchhammer, K., Sawers, G. & Böck, A. (1991) Interspecies compatibility of selenoprotein biosynthesis in Enterobacteriaceae. Arch. Microbiol. 155, 221-228.
    • (1991) Arch. Microbiol. , vol.155 , pp. 221-228
    • Heider, J.1    Forchhammer, K.2    Sawers, G.3    Böck, A.4
  • 53
    • 0027519561 scopus 로고
    • The gene locus of the proton-translocating NADH: Ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I
    • Weidner, U., Geier, S., Ptock, A., Friedrich, T., Leif, H. & Weiss, H. (1993) The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I. J. Mol. Biol. 233, 109-122.
    • (1993) J. Mol. Biol. , vol.233 , pp. 109-122
    • Weidner, U.1    Geier, S.2    Ptock, A.3    Friedrich, T.4    Leif, H.5    Weiss, H.6
  • 54
    • 0027155827 scopus 로고
    • Energetic efficiency of Escherichia coli: Effects of mutations in components of the aerobic respiratory chain
    • Calhoun, M.W., Oden, K.L., Gennis, R.B., deMattos, M.J. & Neijssel, O.M. (1993) Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain. J. Bacteriol. 175, 3020-3025.
    • (1993) J. Bacteriol. , vol.175 , pp. 3020-3025
    • Calhoun, M.W.1    Oden, K.L.2    Gennis, R.B.3    DeMattos, M.J.4    Neijssel, O.M.5
  • 55
    • 0034782745 scopus 로고    scopus 로고
    • Complex I: A chimaera of a redox and conformation-driven proton pump?
    • Friedrich, T. (2001) Complex I: a chimaera of a redox and conformation-driven proton pump? J. Bioenerg. Biomembr. 33, 169-177.
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 169-177
    • Friedrich, T.1
  • 56
    • 0033395596 scopus 로고    scopus 로고
    • Growth phase-dependent regulation of nuoA-N expression in Escherichia coli K-12 by the Fis protein: Upstream binding sites and bioenergetic significance
    • Wackwitz, B., Bongaerts, J., Goodman, S.D. & Unden, G. (1999) Growth phase-dependent regulation of nuoA-N expression in Escherichia coli K-12 by the Fis protein: upstream binding sites and bioenergetic significance. Mol. General Genet. 262, 876-883.
    • (1999) Mol. General Genet , vol.262 , pp. 876-883
    • Wackwitz, B.1    Bongaerts, J.2    Goodman, S.D.3    Unden, G.4
  • 57
    • 0029062019 scopus 로고
    • Transcriptional regulation of the proton translocating NADH dehydrogenase genes (nuoA-N) of Escherichia coli electron acceptors, electron donors and gene regulators
    • Bongaerts, J., Zoske, S., Weidner, U. & Unden, G. (1995) Transcriptional regulation of the proton translocating NADH dehydrogenase genes (nuoA-N) of Escherichia coli electron acceptors, electron donors and gene regulators. Mol. Microbiol. 16, 521-534.
    • (1995) Mol. Microbiol. , vol.16 , pp. 521-534
    • Bongaerts, J.1    Zoske, S.2    Weidner, U.3    Unden, G.4
  • 59
    • 0023463947 scopus 로고
    • NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain
    • Matsushita, K., Ohnishi, T. & Kaback, H.R. (1987) NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry. 26, 7732-7737.
    • (1987) Biochemistry , vol.26 , pp. 7732-7737
    • Matsushita, K.1    Ohnishi, T.2    Kaback, H.R.3
  • 60
    • 0028276785 scopus 로고
    • Regulation of transcription at the ndh promoter of Escherichia coli by FNR and novel factors
    • Green, J. & Guest, J.R. (1994) Regulation of transcription at the ndh promoter of Escherichia coli by FNR and novel factors. Mol. Microbiol. 12, 433-444.
    • (1994) Mol. Microbiol. , vol.12 , pp. 433-444
    • Green, J.1    Guest, J.R.2
  • 61
    • 0024314879 scopus 로고
    • FNR-dependent repression of the ndh gene of Escherichia coli and metal ion requirement for FNR-regulated gene expression
    • Spiro, S., Roberts, R.E. & Guest, J.R. (1989) FNR-dependent repression of the ndh gene of Escherichia coli and metal ion requirement for FNR-regulated gene expression. Mol. Microbiol. 3, 601-608.
    • (1989) Mol. Microbiol. , vol.3 , pp. 601-608
    • Spiro, S.1    Roberts, R.E.2    Guest, J.R.3
  • 62
    • 0030997843 scopus 로고    scopus 로고
    • FNR-dependent repression of ndh gene expression requires two upstream FNR-binding sites
    • Meng, W., Green, J. & Guest, J.R. (1997) FNR-dependent repression of ndh gene expression requires two upstream FNR-binding sites. Microbiology 143, 1521-1532.
    • (1997) Microbiology , vol.143 , pp. 1521-1532
    • Meng, W.1    Green, J.2    Guest, J.R.3
  • 63
    • 0026625770 scopus 로고
    • Localization of upstream sequence elements required for nitrate and anaerobic induction of fdn (Formate Dehydrogenase-N) operon expression in Escherichia coli K-12
    • Li, J. & Steward, V. (1992) Localization of upstream sequence elements required for nitrate and anaerobic induction of fdn (Formate Dehydrogenase-N) operon expression in Escherichia coli K-12. J. Bacteriol. 174, 4935-4942.
    • (1992) J. Bacteriol. , vol.174 , pp. 4935-4942
    • Li, J.1    Steward, V.2
  • 64
    • 0037083882 scopus 로고    scopus 로고
    • Membrane sequestration of the signal transduction protein GlnK by the ammonium transporter AmtB
    • Coutts, G., Thomas, G., Blakey, D. & Merrick, M. (2002) Membrane sequestration of the signal transduction protein GlnK by the ammonium transporter AmtB. EMBO J. 21, 536-545.
    • (2002) EMBO J. , vol.21 , pp. 536-545
    • Coutts, G.1    Thomas, G.2    Blakey, D.3    Merrick, M.4


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