메뉴 건너뛰기




Volumn 94, Issue 4, 2012, Pages 1041-1047

Interaction of GlnK with the GAF domain of Herbaspirillum seropedicae NifA mediates NH 4 +-regulation

Author keywords

GAF domain; GlnK; Herbaspirillum seropedicae; NifA; Nitrogen fixation

Indexed keywords

AMMONIA; BACTERIAL PROTEIN; CHIMERIC PROTEIN; CYSTEINE; GAF PROTEIN; GLNK PROTEIN; NIFA PROTEIN; OXYGEN; UNCLASSIFIED DRUG;

EID: 84857457694     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2012.01.007     Document Type: Article
Times cited : (16)

References (48)
  • 2
    • 0037332383 scopus 로고    scopus 로고
    • 54-dependent transcriptional activators
    • DOI 10.1128/JB.185.6.1757-1767.2003
    • D.J. Studholme, and R. Dixon Domain architectures of sigma54-dependent transcriptional activators J. Bacteriol. 185 2003 1757 1767 (Pubitemid 36297874)
    • (2003) Journal of Bacteriology , vol.185 , Issue.6 , pp. 1757-1767
    • Studholme, D.J.1    Dixon, R.2
  • 3
    • 0034676026 scopus 로고    scopus 로고
    • Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor
    • Y.S. Ho, L.M. Burden, and J.H. Hurley Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor EMBO J. 19 2000 5288 5299
    • (2000) EMBO J. , vol.19 , pp. 5288-5299
    • Ho, Y.S.1    Burden, L.M.2    Hurley, J.H.3
  • 4
    • 33846895023 scopus 로고    scopus 로고
    • 54- dependent gene transcription
    • DOI 10.1016/j.sbi.2006.11.002, PII S0959440X06002077, Foldinf and Binding / Protein-Nucleic Interactions
    • M. Rappas, D. Bose, and X. Zhang Bacterial enhancer-binding proteins: unlocking sigma54-dependent gene transcription Curr. Opin. Struct. Biol. 17 2007 110 116 (Pubitemid 46240806)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.1 , pp. 110-116
    • Rappas, M.1    Bose, D.2    Zhang, X.3
  • 6
    • 0022668501 scopus 로고
    • Sequence and domain relationships of ntrC and nifA from Klebsiella pneumoniae: Homologies to other regulatory proteins
    • M. Drummond, P. Whitty, and J. Wooton Sequence and domain relationships of ntrC and nifA from Klebsiella pneumoniae: homologies to other regulatory proteins EMBO J. 5 1986 441 447
    • (1986) EMBO J. , vol.5 , pp. 441-447
    • Drummond, M.1    Whitty, P.2    Wooton, J.3
  • 7
    • 0037106322 scopus 로고    scopus 로고
    • Secondary structure and DNA binding by the C-terminal domain of the transcriptional activator NifA from Klebsiella pneumoniae
    • P. Ray, K.J. Smith, R.A. Parslow, R. Dixon, and E.I. Hyde Secondary structure and DNA binding by the C-terminal domain of the transcriptional activator NifA from Klebsiella pneumoniae Nucleic Acids Res. 30 2002 3972 3980
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3972-3980
    • Ray, P.1    Smith, K.J.2    Parslow, R.A.3    Dixon, R.4    Hyde, E.I.5
  • 8
    • 0037296115 scopus 로고    scopus 로고
    • Expression, purification, and functional analysis of the C-terminal domain of Herbaspirillum seropedicae NifA protein
    • DOI 10.1016/S1046-5928(02)00635-6, PII S1046592802006356
    • R.A. Monteiro, E.M. Souza, M.G. Yates, M.B. Steffens, F.O. Pedrosa, and L.S. Chubastsu Expression, purification and functional analysis of the C-terminal domain of Herbaspirillum seropedicae NifA protein Protein Expr. Purif. 27 2003 313 318 (Pubitemid 36339303)
    • (2003) Protein Expression and Purification , vol.27 , Issue.2 , pp. 313-318
    • Monteiro, R.A.1    Souza, E.M.2    Yates, M.G.3    Steffens, M.B.R.4    Pedrosa, F.O.5    Chubatsu, L.S.6
  • 9
    • 1642500165 scopus 로고    scopus 로고
    • The NifL-NifA System: A Multidomain Transcriptional Regulatory Complex That Integrates Environmental Signals
    • DOI 10.1128/JB.186.3.601-610.2004
    • I. Martinez-Argudo, R. Little, N. Shearer, P. Johnson, and R. Dixon The NifL-NifA system: a multidomain transcriptional regulatory complex that Integrates environmental signals J. Bacteriol. 186 2004 601 610 (Pubitemid 38129636)
    • (2004) Journal of Bacteriology , vol.186 , Issue.3 , pp. 601-610
    • Martinez-Argudo, I.1    Little, R.2    Shearer, N.3    Johnson, P.4    Dixon, R.5
  • 10
    • 4344704870 scopus 로고    scopus 로고
    • Genetic regulation of biological nitrogen fixation
    • DOI 10.1038/nrmicro954
    • R. Dixon, and D. Kahn Genetic regulation of biological nitrogen fixation Nat. Rev. Microbiol. 2 2004 621 631 (Pubitemid 39200045)
    • (2004) Nature Reviews Microbiology , vol.2 , Issue.8 , pp. 621-631
    • Dixon, R.1    Kahn, D.2
  • 11
    • 0024296535 scopus 로고
    • Essential and non-essential domains in the Bradirhizobium japonicum NifA protein: Identification of indispensable cysteine residues potentially involved in redox reactivity and/or metal binding
    • H. Fischer, T. Bruderer, and H. Hennecke Essential and non-essential domains in the Bradirhizobium japonicum NifA protein: identification of indispensable cysteine residues potentially involved in redox reactivity and/or metal binding Nucleic Acids Res. 16 1988 2207 2224
    • (1988) Nucleic Acids Res. , vol.16 , pp. 2207-2224
    • Fischer, H.1    Bruderer, T.2    Hennecke, H.3
  • 12
    • 0024967319 scopus 로고
    • Critical spacing between two essential cysteine residues in the interdomain linker of the Bradirhizobium japonicum NifA protein
    • H. Fischer, S. Fritsche, B. Herzog, and H. Hennek Critical spacing between two essential cysteine residues in the interdomain linker of the Bradirhizobium japonicum NifA protein FEBS Lett. 225 1989 167 171
    • (1989) FEBS Lett. , vol.225 , pp. 167-171
    • Fischer, H.1    Fritsche, S.2    Herzog, B.3    Hennek, H.4
  • 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
    • DOI 10.1074/jbc.M112262200
    • R. Little, V. Colombo, A. Leech, and R. Dixon 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 2002 15472 15481 (Pubitemid 34967813)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15472-15481
    • Little, R.1    Colombo, V.2    Leech, A.3    Dixon, R.4
  • 15
    • 0031921952 scopus 로고    scopus 로고
    • The redox- and fixed nitrogen-responsive regulatory protein NIFL from Azotobacter vinelandii comprises discrete flavin and nucleotide-binding domains
    • DOI 10.1046/j.1365-2958.1998.00788.x
    • E. Söderback, F. Reyes-Ramirez, T. Eydmann, S. Austin, S. Hill, and R. Dixon The redox- and fixed nitrogen- responsive regulatory NIFL form Azotobacter vinelandii comprises discrete flavin and nucleotide-binding domains Mol. Microbiol. 28 1998 179 192 (Pubitemid 28160123)
    • (1998) Molecular Microbiology , vol.28 , Issue.1 , pp. 179-192
    • Soderback, E.1    Reyes-Ramirez, F.2    Eydmann, T.3    Austin, S.4    Hill, S.5    Dixon, R.6
  • 16
    • 0032765524 scopus 로고    scopus 로고
    • Isolation and properties of the complex between the enhancer binding protein NIFA and the sensor NIFL
    • T. Money, T. Jones, R. Dixon, and S. Austin Isolation and properties of the complex between the enhancer binding protein NifA and the sensor NifL J. Bacteriol. 181 1999 4461 4468 (Pubitemid 29357923)
    • (1999) Journal of Bacteriology , vol.181 , Issue.15 , pp. 4461-4468
    • Money, T.1    Jones, T.2    Dixon, R.3    Austin, S.4
  • 17
    • 0034669188 scopus 로고    scopus 로고
    • Signal transduction to the Azotobacter vinelandii NIFL-NIFA regulatory system is influenced directly by interaction with 2-oxoglutarate and PII regulatory protein
    • R. Little, F. Reyes-Ramirez, Y. Zhang, W.C. van Heeswijk, and R. Dixon Signal transduction to the Azotobacter vinelandii NIFL-NIFA regulatory system is influenced directly by interaction with 2-oxoglutarate and PII regulatory protein EMBO J. 19 2000 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
  • 18
    • 3042640724 scopus 로고    scopus 로고
    • Role of the amino-terminal GAF domain of the NifA activator in controlling the response to the antiactivator protein NifL
    • DOI 10.1111/j.1365-2958.2004.04089.x
    • I. Martinez-Argudo, R. Little, and R. Dixon Role of the amino-terminal GAF domain of the NifA activator in controlling the response to antiactivator protein NifL Mol. Microbiol. 52 2004 1731 1744 (Pubitemid 38822681)
    • (2004) Molecular Microbiology , vol.52 , Issue.6 , pp. 1731-1744
    • Martinez-Argudo, I.1    Little, R.2    Dixon, R.3
  • 19
    • 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
    • DOI 10.1074/jbc.M301992200
    • R. Little, and R. Dixon The amino-terminal GAF domain of Azotobacter vinelandii binds 2-Oxoglutarate to resist inhibition by NifL under nitrogen-limiting conditions J. Biol. Chem. 278 2003 28711 28718 (Pubitemid 36935778)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 28711-28718
    • Little, R.1    Dixon, R.2
  • 20
    • 0029743218 scopus 로고    scopus 로고
    • Modulation of NifA activity by P(II) in Azospirillum brasilense: Evidence for a regulatory role of the NifA N-terminal domain
    • F. Arsene, P.A. Kaminski, and C. Elmerich Modulation of NifA activity by PII in Azospirillum brasilense: evidence by a regulatory role of the NifA N-terminal domain J. Bacteriol. 178 1996 4830 4838 (Pubitemid 26321282)
    • (1996) Journal of Bacteriology , vol.178 , Issue.16 , pp. 4830-4838
    • Arsene, F.1    Kaminski, P.A.2    Elmerich, C.3
  • 21
    • 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
    • DOI 10.1016/S0378-1097(99)00426-7, PII S0378109799004267
    • F. Arsene, P.A. Kaminski, and C. Elmerich Control of Azospirillum brasilense NifA activity by PII: effect of replacing Tyr residues of the NifA N-terminal domain on NifA activity FEMS Microbiol. Lett. 179 1999 339 343 (Pubitemid 29460697)
    • (1999) FEMS Microbiology Letters , vol.179 , Issue.2 , pp. 339-343
    • Arsene, F.1    Kaminski, P.A.2    Elmerich, C.3
  • 22
  • 23
    • 0032587948 scopus 로고    scopus 로고
    • Azorhizobium caulinodans P(II) and GlnK proteins control nitrogen fixation and ammonia assimilation
    • N. Michel-Reydellet, and A. Kaminski Azorhizobium caulinodans PII and GlnK proteins control nitrogen fixation and ammonia assimilation J. Bacteriol. 181 1999 2655 2658 (Pubitemid 29181597)
    • (1999) Journal of Bacteriology , vol.181 , Issue.8 , pp. 2655-2658
    • Michel-Reydellet, N.1    Kaminski, P.A.2
  • 24
    • 0042008057 scopus 로고    scopus 로고
    • Role of GlnB and GlnK in ammonium control of both nitrogenase systems in the phototrophic bacterium Rhodobacter capsulatus
    • T. Drepper, S. Gross, A.F. Yakunin, P.C. Hallenbeck, B. Masepohl, and W. Klipp Role of GlnB and GlnK in ammonium control of both nitrogenase systems in the phototrophic bacterium Rhodobacter capsulatus Microbiology 149 2003 2203 2212 (Pubitemid 37038426)
    • (2003) Microbiology , vol.149 , Issue.8 , pp. 2203-2212
    • Drepper, T.1    Gross, S.2    Yakunin, A.F.3    Hallenbeck, P.C.4    Masepohl, B.5    Klipp, W.6
  • 25
    • 21544471853 scopus 로고    scopus 로고
    • Functional analysis of the GAF domain of NifA in Azospirillum brasilense: Effects of Tyr → Phe mutations on NifA and its interaction with GlnB
    • DOI 10.1007/s00438-005-1146-5
    • S. Chen, L. Liu, X. Zhou, C. Elmerich, and J. Li Functional analysis of the GAF domain of NifA in Azospirillum brasilense: effects of Tyr→Phe mutations on NifA and its interaction with GlnB Mol. Gen. Genomics 273 2005 415 422 (Pubitemid 40922406)
    • (2005) Molecular Genetics and Genomics , vol.273 , Issue.5 , pp. 415-422
    • Chen, S.1    Liu, L.2    Zhou, X.3    Elmerich, C.4    Li, J.-L.5
  • 26
    • 0042130559 scopus 로고    scopus 로고
    • Yeast two-hybrid studies on interaction of proteins involved in regulation of nitrogen fixation in the phototrophic bacterium Rhodobacter capsulatus
    • DOI 10.1128/JB.185.17.5240-5247.2003
    • A. Pawlowski, K.U. Riedel, W. Klipp, P. Dreiskemper, S. Gross, H. Bierhoff, T. Drepper, and B. Masepohl Yeast two-hybrid studies on interaction of proteins involved in regulation of nitrogen fixation in the phototrophic bacterium Rhodobacter capsulatus J. Bacteriol. 185 2003 5240 5247 (Pubitemid 37021985)
    • (2003) Journal of Bacteriology , vol.185 , Issue.17 , pp. 5240-5247
    • Pawlowski, A.1    Riedel, K.-U.2    Klipp, W.3    Dreiskemper, P.4    Gross, S.5    Bierhoff, H.6    Drepper, T.7    Masepohl, B.8
  • 27
    • 0032956540 scopus 로고    scopus 로고
    • Control of Herbaspirillum seropedicae NifA activity by ammonium ions and oxygen
    • E.M. Souza, F.O. Pedrosa, M. Drummmond, L.U. Rigo, and M.G. Yates Control of Herbaspirillum seropedicae NifA activity by ammonium ions and oxygen J. Bacteriol. 181 1999 681 684 (Pubitemid 29045165)
    • (1999) Journal of Bacteriology , vol.181 , Issue.2 , pp. 681-684
    • Souza, E.M.1    Pedrosa, F.O.2    Drummond, M.3    Rigo, L.U.4    Yates, M.G.5
  • 28
    • 0033046312 scopus 로고    scopus 로고
    • Expression and functional analysis of an N-truncated NifA protein of Herbaspirillum seropedicae
    • DOI 10.1016/S0014-5793(99)00314-2, PII S0014579399003142
    • R.A. Monteiro, E.M. Souza, S. Funayama, M.G. Yates, F.O. Pedrosa, and L.S. Chubatsu Expression and functional analysis of an N-truncated NifA protein of Herbaspirillum seropedicae FEBS Lett. 447 1999 283 286 (Pubitemid 29146102)
    • (1999) FEBS Letters , vol.447 , Issue.2-3 , 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
  • 29
    • 0032733250 scopus 로고    scopus 로고
    • In-trans regulation of the N-truncated-NIFA protein of Herbaspirillum seropedicae by the N-terminal domain
    • DOI 10.1016/S0378-1097(99)00475-9, PII S0378109799004759
    • R.A. Monteiro, E.M. Souza, M.G. Yates, F.O. Pedrosa, and L.S. Chubatsu In-trans regulation of the N-truncated-NIFA protein of Heraspirillum seropedicae by the N-terminal domain FEMS Microbiol. Lett 180 1999 157 161 (Pubitemid 29507561)
    • (1999) FEMS Microbiology Letters , vol.180 , Issue.2 , pp. 157-161
    • Monteiro, R.A.1    Souza, E.M.2    Yates, M.G.3    Pedrosa, F.O.4    Chubatsu, L.S.5
  • 30
    • 0015951556 scopus 로고
    • Chromosomal integration of Klebsiella pneumoniae nitrogen fixation genes in E. coli
    • F.C. Cannon, R.A. Dixon, and J.R. Postgate Chromosomal integration of Klebsiella pneumoniae nitrogen fixation genes in E. coli J. Gen. Microbiol. 80 1974 227 239
    • (1974) J. Gen. Microbiol. , vol.80 , pp. 227-239
    • Cannon, F.C.1    Dixon, R.A.2    Postgate, J.R.3
  • 32
    • 34548444161 scopus 로고    scopus 로고
    • Purification and characterization of the bifunctional uridylyltransferase and the signal transducing proteins GlnB and GlnK from Herbaspirillum seropedicae
    • DOI 10.1016/j.pep.2007.04.012, PII S1046592807001131
    • A.C. Bonatto, G.H. Couto, E.M. Souza, L.M. Araujo, F.O. Pedrosa, L. Noindorf, and E.M. Benelli Purification and characterization of the bifunctional uridylyltransferase and the signals transducing proteins GlnB and GlnK from Herbaspirillum seropedicae Prot. Exp. Pur 55 2007 293 299 (Pubitemid 47369648)
    • (2007) Protein Expression and Purification , vol.55 , Issue.2 , pp. 293-299
    • Bonatto, A.C.1    Couto, G.H.2    Souza, E.M.3    Araujo, L.M.4    Pedrosa, F.O.5    Noindorf, L.6    Benelli, E.M.7
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembling of the head of the bacteriophage T7
    • U.K. Laemmli Cleavage of structural proteins during the assembling of the head of the bacteriophage T7 Nature 277 1970 680 685
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • DOI 10.1016/0003-2697(87)90587-2
    • H. Schägger, and G. Von Jagow Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Anal. Biochem. 166 1987 368 379 (Pubitemid 18004907)
    • (1987) Analytical Biochemistry , vol.166 , Issue.2 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein-dye binding
    • M.M.A. Bradford A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.A.1
  • 38
  • 40
    • 39049106044 scopus 로고    scopus 로고
    • P(II) signal transducers: Novel function and structure insights
    • K. Forchhammer P(II) signal transducers: novel function and structure insights J. Mol. Biol. 16 2008 65 72
    • (2008) J. Mol. Biol. , vol.16 , pp. 65-72
    • Forchhammer, K.1
  • 42
    • 79551484042 scopus 로고    scopus 로고
    • The role of effector molecules in signal transduction by PII proteins
    • M. Radchenko, and M. Merrick The role of effector molecules in signal transduction by PII proteins Biochem. Soc. Trans. 39 2011 189 194
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 189-194
    • Radchenko, M.1    Merrick, M.2
  • 43
    • 27744559527 scopus 로고    scopus 로고
    • Effect of the over-expression of PII and PZ proteins on the nitrogenase activity of Azospirillum brasilense
    • DOI 10.1016/j.femsle.2005.09.026, PII S0378109705006609
    • L.F. Huergo, A. Filipaki, L.S. Chubatsu, M.G. Yates, M.B. Steffens, F.O. Pedrosa, and E.M. Souza Effect of the over-expression of PII and PZ proteins on the nitrogenase activity of Azospirillum brasilense FEMS Microbiol. Lett. 253 2005 47 54 (Pubitemid 41605393)
    • (2005) FEMS Microbiology Letters , vol.253 , Issue.1 , pp. 47-54
    • Huergo, L.F.1    Filipaki, A.2    Chubatsu, L.S.3    Yates, M.G.4    Steffens, M.B.5    Pedrosa, F.O.6    Souza, E.M.7
  • 44
    • 0019960551 scopus 로고
    • Fine-structure deletion map and complementation analysis of the glnA-glnL-glnG region in Escherichia coli
    • T. Macneil, D. Macneil, and B. Tyler Fine-structure deletion map and complementation analysis of the glnA-glnL-glnG region in Escherichia coli J. Bacteriol. 150 1982 1302 1313 (Pubitemid 12015836)
    • (1982) Journal of Bacteriology , vol.150 , Issue.3 , pp. 1302-1313
    • MacNeil, T.1    MacNeil, D.2    Tyler, B.3
  • 45
    • 0035025555 scopus 로고    scopus 로고
    • Role of Escherichia coli nitrogen regulatory genes in the nitrogen response of the Azotobacter vinelandii NifL-NifA complex
    • DOI 10.1128/JB.183.10.3076-3082.2001
    • F. Reyes-Ramirez, R. Little, and R. Dixon Role of Escherichia coli nitrogen regulatory genes in the nitrogen response of Azotobacter vinelandii NifL-NifA complex J. Bacteriol. 183 2001 3076 3082 (Pubitemid 32433524)
    • (2001) Journal of Bacteriology , vol.183 , Issue.10 , pp. 3076-3082
    • Reyes-Ramirez, F.1    Little, R.2    Dixon, R.3
  • 48
    • 0023957525 scopus 로고
    • Over-production and characterisation of the nifA gene product of Klebsiella pneumoniae-The transcription activator of nif gene expression
    • R. Tuli, and M.J. Merrick Over-production and characterisation of the nifA gene product of Klebsiella pneumoniae-the transcription activator of nif gene expression J. Gen. Microbiol. 134 1988 425 432
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 425-432
    • Tuli, R.1    Merrick, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.