메뉴 건너뛰기




Volumn 271, Issue 16, 2004, Pages 3379-3388

GlnK effects complex formation between NifA and NifL in Klebsiella pneumoniae

Author keywords

GlnK; Klebsiella pneumoniae; NifA; NifL; Nitrogen fixation

Indexed keywords

AMMONIA; NITROGEN; OXYGEN; PROTEIN GLNK; REGULATOR PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR NIFA; TRANSCRIPTION FACTOR NIFL; UNCLASSIFIED DRUG;

EID: 4344695224     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04272.x     Document Type: Article
Times cited : (17)

References (44)
  • 1
    • 0000703950 scopus 로고    scopus 로고
    • Mechanism of molybdenum nitrogenase
    • Burgess, B.K. & Lowe, D.J. (1996) Mechanism of molybdenum nitrogenase. Chem. Rev. 96, 2983-3012.
    • (1996) Chem. Rev. , vol.96 , pp. 2983-3012
    • Burgess, B.K.1    Lowe, D.J.2
  • 2
    • 0032751576 scopus 로고    scopus 로고
    • Structural bioenergetics and energy transduction mechanisms
    • Rees, D.C. & Howard, J.B. (1999) Structural bioenergetics and energy transduction mechanisms. J. Mol. Biol. 293, 343-350.
    • (1999) J. Mol. Biol. , vol.293 , pp. 343-350
    • Rees, D.C.1    Howard, J.B.2
  • 3
    • 0025012093 scopus 로고
    • The integration host factor stimulates interaction of RNA polymerase with NIFA, the transcriptional activator for nitrogen fixation operons
    • Hoover, T.R., Santero, E., Porter, S. & Kustu, S. (1990) The integration host factor stimulates interaction of RNA polymerase with NIFA, the transcriptional activator for nitrogen fixation operons. Cell 63, 11-22.
    • (1990) Cell , vol.63 , pp. 11-22
    • Hoover, T.R.1    Santero, E.2    Porter, S.3    Kustu, S.4
  • 4
    • 0024449796 scopus 로고
    • In vivo studies on the interaction of RNA polymerase-sigma 54 with the Klebsiella pneumoniae and Rhizobium meliloti nifH promoters
    • Morett, E. & Buck, M. (1989) In vivo studies on the interaction of RNA polymerase-sigma 54 with the Klebsiella pneumoniae and Rhizobium meliloti nifH promoters. J. Mol. Biol. 210, 65-77.
    • (1989) J. Mol. Biol. , vol.210 , pp. 65-77
    • Morett, E.1    Buck, M.2
  • 6
    • 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
  • 7
    • 0019421071 scopus 로고
    • Nitrogen fixation gene (nifL) involved in oxygen regulation of nitrogenase synthesis in K. pneumoniae
    • Hill, S., Kennedy, C., Kavanagh, E., Goldberg, R.B. & Hanau, R. (1981) Nitrogen fixation gene (nifL) involved in oxygen regulation of nitrogenase synthesis in K. pneumoniae. Nature 290, 424-426.
    • (1981) Nature , vol.290 , pp. 424-426
    • Hill, S.1    Kennedy, C.2    Kavanagh, E.3    Goldberg, R.B.4    Hanau, R.5
  • 8
    • 0036773120 scopus 로고    scopus 로고
    • Identification of a NifL-like protein in a diazotroph of the beta-subgroup of the Proteobacteria, Azoarcus sp. strain BH72
    • Egener, T., Sarkar, A., Martin, D.E. & Reinhold-Hurek, B. (2002) Identification of a NifL-like protein in a diazotroph of the beta-subgroup of the Proteobacteria, Azoarcus sp. strain BH72. Microbiology 148, 3203-3212.
    • (2002) Microbiology , vol.148 , pp. 3203-3212
    • Egener, T.1    Sarkar, A.2    Martin, D.E.3    Reinhold-Hurek, B.4
  • 9
    • 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. (1989) Role of metal ions in negative regulation of nitrogen fixation by the nifL gene product from Klebsiella pneumoniae. Mol. Gen. Genet. 216, 484-491.
    • (1989) Mol. Gen. Genet. , vol.216 , pp. 484-491
    • Henderson, N.1    Austin, S.2    Dixon, R.3
  • 10
    • 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
  • 11
    • 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
  • 12
    • 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
  • 13
    • 0036947218 scopus 로고    scopus 로고
    • Mutant forms of the Azotobacter vinelandii transcriptional activator NifA resistant to inhibition by the NifL regulatory protein
    • Reyes-Ramirez, F., Little, R. & Dixon, R. (2002) Mutant forms of the Azotobacter vinelandii transcriptional activator NifA resistant to inhibition by the NifL regulatory protein. J. Bacteriol. 184, 6777-6785.
    • (2002) J. Bacteriol. , vol.184 , pp. 6777-6785
    • Reyes-Ramirez, F.1    Little, R.2    Dixon, R.3
  • 14
    • 0043209062 scopus 로고    scopus 로고
    • The amino-terminal GAF domain of Azotobacter vinelandii NifA binds 2-oxoglutarate to resist inhibition by NifL under nitrogen-limiting conditions
    • Little, R. & Dixon, R. (2003) The amino-terminal GAF domain of Azotobacter vinelandii NifA binds 2-oxoglutarate to resist inhibition by NifL under nitrogen-limiting conditions. J. Biol. Chem. 278, 28711-28718.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28711-28718
    • Little, R.1    Dixon, R.2
  • 16
    • 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
  • 17
    • 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
  • 18
    • 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
  • 19
    • 0037392283 scopus 로고    scopus 로고
    • 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
    • Grabbe, R. & Schmitz, R.A. (2003) 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. Eur. J. Biochem. 270, 1555-1566.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1555-1566
    • Grabbe, R.1    Schmitz, R.A.2
  • 20
    • 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
  • 21
    • 0033061058 scopus 로고    scopus 로고
    • The signal transduction protein GlnK is required for NifL-dependent nitrogen control of nif gene expression in Klebsiella pneumonia
    • 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 pneumonia. J. Bacteriol. 181, 1156-1162.
    • (1999) J. Bacteriol. , vol.181 , pp. 1156-1162
    • Jack, R.1    De Zamaroczy, M.2    Merrick, M.3
  • 22
    • 2542509740 scopus 로고    scopus 로고
    • Studies on the roles of GlnK and GlnB in regulating Klebsiella pneumoniae NifL-dependent nitrogen control
    • Arcondeguy, T., van Heeswijk, W.C. & Merrick, M. (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
  • 23
    • 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
  • 24
    • 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
  • 25
    • 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
  • 26
    • 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
  • 27
    • 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
  • 28
    • 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
  • 29
    • 0025195680 scopus 로고
    • Mini-Tn5 transposon derivatives for insertion mutagenesis, promoter probing, and chromosomal insertion of cloned DNA in gram-negative eubacteria
    • de Lorenzo, 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
    • De Lorenzo, V.1    Herrero, M.2    Jakubzik, U.3    Timmis, K.N.4
  • 30
    • 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
  • 31
    • 0027468370 scopus 로고
    • Activity of purified NIFA, a transcriptional activator of nitrogen fixation genes
    • Lee, H.S., Berger, D.K. & Kustu, S. (1993) Activity of purified NIFA, a transcriptional activator of nitrogen fixation genes. Proc. Natl Acad. Sci. USA 90, 2266-2270.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2266-2270
    • Lee, H.S.1    Berger, D.K.2    Kustu, S.3
  • 33
    • 9344269892 scopus 로고    scopus 로고
    • Iron is required to relieve inhibitory effects on NifL on transcriptional activation by NifA in Klebsiella pneumoniae
    • Schmitz, R.A., He, L. & Kustu, S. (1996) Iron is required to relieve inhibitory effects on 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
  • 34
    • 0030615317 scopus 로고    scopus 로고
    • Phosphoprotein PII from cyanobacteria -analysis of functional conservation with the PII signal-transduction protein from Escherichia coli
    • Forchhammer, K. & Hedler, A. (1997) Phosphoprotein PII from cyanobacteria -analysis of functional conservation with the PII signal-transduction protein from Escherichia coli. Eur. J. Biochem. 244, 869-875.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 869-875
    • Forchhammer, K.1    Hedler, A.2
  • 36
    • 0027958569 scopus 로고
    • The isolated catalytic domain of NIFA, a bacterial enhancer-binding protein, activates transcription in vitro: Activation is inhibited by NIFL
    • Berger, D.K., Narberhaus, F. & Kustu, S. (1994) The isolated catalytic domain of NIFA, a bacterial enhancer-binding protein, activates transcription in vitro: activation is inhibited by NIFL. Proc. Natl Acad. Sci. USA 91, 103-107.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 103-107
    • Berger, D.K.1    Narberhaus, F.2    Kustu, S.3
  • 38
    • 0029149909 scopus 로고
    • Redox-cycling detection of dialyzable pyrroloquinoline quinone and quinoproteins
    • Fluckiger, R., Paz, M.A. & Gallop, P.M. (1995) Redox-cycling detection of dialyzable pyrroloquinoline quinone and quinoproteins. Methods Enzymol. 258, 140-149.
    • (1995) Methods Enzymol. , vol.258 , pp. 140-149
    • Fluckiger, R.1    Paz, M.A.2    Gallop, P.M.3
  • 39
    • 0028888881 scopus 로고
    • In vitro studies of the domains of the nitrogen fixation regulatory protein NIFA
    • Berger, D.K., Narberhaus, F., Lee, H.S. & Kustu, S. (1995) In vitro studies of the domains of the nitrogen fixation regulatory protein NIFA. J. Bacteriol. 177, 191-199.
    • (1995) J. Bacteriol. , vol.177 , pp. 191-199
    • Berger, D.K.1    Narberhaus, F.2    Lee, H.S.3    Kustu, S.4
  • 40
    • 0027121372 scopus 로고
    • Regulation of nitrogen fixation in Azospirillum brasilense Sp7: Involvement of nifA, glnA and glnB gene products
    • Liang, Y.Y., de Zamaroczy, M., Arsene, F., Paquelin, A. & Elmerich, C. (1992) Regulation of nitrogen fixation in Azospirillum brasilense Sp7: involvement of nifA, glnA and glnB gene products. FEMS Microbiol. Lett. 79, 113-119.
    • (1992) FEMS Microbiol. Lett. , vol.79 , pp. 113-119
    • Liang, Y.Y.1    De Zamaroczy, M.2    Arsene, F.3    Paquelin, A.4    Elmerich, C.5
  • 41
    • 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., Kaminski, P.A. & Elmerich, C. (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
  • 42
    • 0344131897 scopus 로고    scopus 로고
    • Control of Azospirillum brasilense NifA activity by P (II): Effect of replacing Tyr residues of the NifA N-terminal domain on NifA activity
    • Arsene, F., Kaminski, P.A. & Elmerich, C. (1999) Control of Azospirillum brasilense NifA activity by P (II): effect of replacing Tyr residues of the NifA N-terminal domain on NifA activity. FEMS Microbiol. Lett. 179, 339-343.
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 339-343
    • Arsene, F.1    Kaminski, P.A.2    Elmerich, C.3
  • 43
    • 0042008057 scopus 로고    scopus 로고
    • Role of GlnB and GlnK in ammonium control of both nitrogenase systems in the phototrophic bacterium Rhodobacter capsulatus
    • Drepper, T., Gross, S., Yakunin, A.F., Hallenbeck, P.C., Masepohl, B. & Klipp, W. (2003) Role of GlnB and GlnK in ammonium control of both nitrogenase systems in the phototrophic bacterium Rhodobacter capsulatus. Microbiology 149, 2203-2212.
    • (2003) Microbiology , vol.149 , pp. 2203-2212
    • Drepper, T.1    Gross, S.2    Yakunin, A.F.3    Hallenbeck, P.C.4    Masepohl, B.5    Klipp, W.6
  • 44
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.