메뉴 건너뛰기




Volumn 30, Issue 18, 2002, Pages 3972-3980

Secondary structure and DNA binding by the C-terminal domain of the transcriptional activator NifA from Klebsiella pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

HELIX LOOP HELIX PROTEIN; HOLOENZYME; PROTEIN NIFA; RNA POLYMERASE; SIGMA FACTOR; UNCLASSIFIED DRUG;

EID: 0037106322     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkf528     Document Type: Article
Times cited : (18)

References (40)
  • 1
    • 0024393946 scopus 로고
    • In vitro activity of the nitrogen fixation regulatory protein NifA
    • Santero,E., Hoover,T., Keener,J. and Kustu,S. (1989) In vitro activity of the nitrogen fixation regulatory protein NifA. Proc. Natl Acad. Sci. USA, 86, 7346-7350.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 7346-7350
    • Santero, E.1    Hoover, T.2    Keener, J.3    Kustu, S.4
  • 4
    • 0033938884 scopus 로고    scopus 로고
    • Isomerization of a binary sigma-promoter DNA complex by transcription activators
    • Cannon,W.V., Gallegos,M.T. and Buck,M. (2000) Isomerization of a binary sigma-promoter DNA complex by transcription activators. Nature Struct. Biol., 7, 594-601.
    • (2000) Nature Struct. Biol , vol.7 , pp. 594-601
    • Cannon, W.V.1    Gallegos, M.T.2    Buck, M.3
  • 5
    • 0031924101 scopus 로고    scopus 로고
    • The oxygen-responsive NifL-NifA complex: A novel two-component regulatory system controlling nitrogenase synthesis in γ-proteobacteria
    • Dixon,R. (1998) The oxygen-responsive NifL-NifA complex: a novel two-component regulatory system controlling nitrogenase synthesis in γ-proteobacteria. Arch. Microbiol., 169, 371-380.
    • (1998) Arch. Microbiol , vol.169 , pp. 371-380
    • Dixon, R.1
  • 6
    • 0344710723 scopus 로고
    • NifA-dependent in vivo protection demonstrates that the upstream activator sequence of nif promoters is a protein binding site
    • Morett,E. and Buck,M. (1988) NifA-dependent in vivo protection demonstrates that the upstream activator sequence of nif promoters is a protein binding site. Proc. Natl Acad. Sci. USA, 85, 9401-9405.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 9401-9405
    • Morett, E.1    Buck, M.2
  • 7
    • 0020823127 scopus 로고
    • The nif promoters of Klebsiella have a characteristic primary structure
    • Beynon,J., Cannon,M., Buchanan-Wollaston,V. and Cannon,F. (1983) The nif promoters of Klebsiella have a characteristic primary structure. Cell, 44, 665-671.
    • (1983) Cell , vol.44 , pp. 665-671
    • Beynon, J.1    Cannon, M.2    Buchanan-Wollaston, V.3    Cannon, F.4
  • 8
    • 0024240949 scopus 로고
    • The DNA-binding domain of the transcriptional activator protein NifA resides in its carboxy terminus, recognises the upstream activator sequences of nif promoters and can be separated from the positive control function of NifA
    • Morett,E., Cannon,W. and Buck,M. (1988) The DNA-binding domain of the transcriptional activator protein NifA resides in its carboxy terminus, recognises the upstream activator sequences of nif promoters and can be separated from the positive control function of NifA. Nucleic Acids Res., 16, 11469-11488.
    • (1988) Nucleic Acids Res , vol.16 , pp. 11469-11488
    • Morett, E.1    Cannon, W.2    Buck, M.3
  • 9
    • 0025012093 scopus 로고
    • The integration host factor stimulates interactions of RNA polymerase with NifA, the transcriptional activator for nitrogen fixation operons
    • Hoover,T.R., Santero,E., Porter,S. and Kustu,S. (1990) The integration host factor stimulates interactions 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
  • 10
    • 0034676026 scopus 로고    scopus 로고
    • Structure of the GAF domain, a ubiquitous signalling motif and a new class of cyclic GMP receptor
    • Ho,Y.S., Burden,L.M. and Hurley,J.H. (2000) Structure of the GAF domain, a ubiquitous signalling motif and a new class of cyclic GMP receptor. EMBO J., 19, 5288-5299.
    • (2000) EMBO J , vol.19 , pp. 5288-5299
    • Ho, Y.S.1    Burden, L.M.2    Hurley, J.H.3
  • 11
    • 0024403543 scopus 로고
    • The Q-linker: A class of interdomain sequences found in bacterial multidomain regulatory proteins
    • Wootton,J.C. and Drummond,M.H. (1989) The Q-linker: a class of interdomain sequences found in bacterial multidomain regulatory proteins. Protein Eng., 2, 535-543.
    • (1989) Protein Eng , vol.2 , pp. 535-543
    • Wootton, J.C.1    Drummond, M.H.2
  • 12
    • 0027340543 scopus 로고
    • 54 bacterial enhancer-binding protein family: Mechanism of action and phylogenetic relationship of their functional domains
    • 54 bacterial enhancer-binding protein family: mechanism of action and phylogenetic relationship of their functional domains. J. Bacteriol., 175, 6067-6074.
    • (1993) J. Bacteriol , vol.175 , pp. 6067-6074
    • Morett, E.1    Segovia, L.2
  • 13
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald,A.F. Aravind,L., Spouge,J.L. and Koonin,E.V. (1999) AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res., 9, 27-43.
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 14
    • 0027958569 scopus 로고
    • The isolated catalytic domain of NifA, a bacterial enhancer protein, activates transcription in vitro: Activation is inhibited by NifL
    • Berger,D.K., Narberhaus,F. and Kustu,S. (1994) The isolated catalytic domain of NifA, a bacterial enhancer 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
  • 15
    • 0035150957 scopus 로고    scopus 로고
    • Concerted inhibition of the transcriptional activation functions of the enhancer-binding protein NIFA by the anti-activator NIFL
    • Barrett,J., Ray,P., Sobczyk,A., Little,R. and Dixon,R. (2001) Concerted inhibition of the transcriptional activation functions of the enhancer-binding protein NIFA by the anti-activator NIFL. Mol. Microbiol., 39, 480-494.
    • (2001) Mol. Microbiol , vol.39 , pp. 480-494
    • Barrett, J.1    Ray, P.2    Sobczyk, A.3    Little, R.4    Dixon, R.5
  • 17
    • 0022668501 scopus 로고
    • Sequence and domain relationships of NtrC and NifA from Klebsiella pneumoniae: Jomologies to other regulatory proteins
    • Drummond,M., Whitty,P. and Wootton,J. (1986) Sequence and domain relationships of NtrC and NifA from Klebsiella pneumoniae: homologies to other regulatory proteins. EMBO J., 5, 441-447.
    • (1986) EMBO J , vol.5 , pp. 441-447
    • Drummond, M.1    Whitty, P.2    Wootton, J.3
  • 18
    • 0033536573 scopus 로고    scopus 로고
    • Solution structure of the DNA-binding domain of NtrC with three alanine substitutions
    • Pelton,J.G., Kustu,S. and Wemmer,D.E. (1999) Solution structure of the DNA-binding domain of NtrC with three alanine substitutions. J. Mol. Biol., 292, 1095-1110.
    • (1999) J. Mol. Biol , vol.292 , pp. 1095-1110
    • Pelton, J.G.1    Kustu, S.2    Wemmer, D.E.3
  • 19
    • 0030842186 scopus 로고    scopus 로고
    • The transactivation of the Fis protein that controls site-specific DNA inversion contains extended mobile β-hairpin arms
    • Safo,M.K., Yang,W.Z., Corselli,L., Cramton,S.E., Yuan,H.S. and Johnson,R.C. (1997) The transactivation of the Fis protein that controls site-specific DNA inversion contains extended mobile β-hairpin arms. EMBO J., 16, 6860-6873.
    • (1997) EMBO J , vol.16 , pp. 6860-6873
    • Safo, M.K.1    Yang, W.Z.2    Corselli, L.3    Cramton, S.E.4    Yuan, H.S.5    Johnson, R.C.6
  • 20
    • 0028122355 scopus 로고
    • The major dimerisation determinants of the nitrogen rgulatory protein NtrC from enteric bacteria lie in its carboxy-terminal domain
    • Klose,K.E., North,A.K., Stedman,K.M. and Kustu,S. (1994) The major dimerisation determinants of the nitrogen rgulatory protein NtrC from enteric bacteria lie in its carboxy-terminal domain. J. Mol. Biol., 241, 233-245.
    • (1994) J. Mol. Biol , vol.241 , pp. 233-245
    • Klose, K.E.1    North, A.K.2    Stedman, K.M.3    Kustu, S.4
  • 21
    • 0033555143 scopus 로고    scopus 로고
    • Secondary structure of the C-terminal DNA-binding domain of the transcriptional activator NifA from Klebsiella pneumoniae: Spectroscopic analyses
    • Missaillidis,S., Jaseja,M., Ray,P., Chittock,R., Wharton,C.W., Drake,A.F., Buck,M. and Hyde,E.I. (1999) Secondary structure of the C-terminal DNA-binding domain of the transcriptional activator NifA from Klebsiella pneumoniae: spectroscopic analyses. Arch. Biochem. Biophys., 361, 173-182.
    • (1999) Arch. Biochem. Biophys , vol.361 , pp. 173-182
    • Missaillidis, S.1    Jaseja, M.2    Ray, P.3    Chittock, R.4    Wharton, C.W.5    Drake, A.F.6    Buck, M.7    Hyde, E.I.8
  • 22
    • 0027468370 scopus 로고
    • Activity of purified NifA, a transcriptional activator of nitrogen fixation genes
    • Lee,H.S., Berger,D.K. and 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
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding
    • Bradford,M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem., 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0022545682 scopus 로고
    • Upstream activator sequences are present in the promoter of nitrogen fixation genes
    • Buck,M., Miller,S., Drummond,M. and Dixon,R. (1986) Upstream activator sequences are present in the promoter of nitrogen fixation genes. Nature, 320, 374-378.
    • (1986) Nature , vol.320 , pp. 374-378
    • Buck, M.1    Miller, S.2    Drummond, M.3    Dixon, R.4
  • 26
    • 0023650307 scopus 로고
    • Mutational analysis of upstream sequences are required for transcriptional activation of the Klebsiella pneumoniae nifH promoter
    • Buck,M., Cannon,W. and Woodcock,J. (1987) Mutational analysis of upstream sequences are required for transcriptional activation of the Klebsiella pneumoniae nifH promoter. Nucleic Acids Res., 15, 9945-9956.
    • (1987) Nucleic Acids Res , vol.15 , pp. 9945-9956
    • Buck, M.1    Cannon, W.2    Woodcock, J.3
  • 27
    • 0001689741 scopus 로고
    • Gradient-enhanced triple resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram,D.R. and Kay,L.E. (1994) Gradient-enhanced triple resonance three-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. B, 103, 203-216.
    • (1994) J. Magn. Reson. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 31
    • 0028545648 scopus 로고
    • α J-couplings in calcium-free calmodulin using new 2D and 3D water flip-back methods
    • α J-couplings in calcium-free calmodulin using new 2D and 3D water flip-back methods. J. Biomol. NMR, 4, 871-878.
    • (1994) J. Biomol. NMR , vol.4 , pp. 871-878
    • Kuboniwa, H.1    Grzesiek, S.2    Delaglio, F.3    Bax, A.4
  • 32
    • 0028541866 scopus 로고
    • Backbone H-1 and N-15 resonance assignments of the N-terminal SH3 domain of DRK in folded and unfolded states using enhance sensitivity pulsed-fielded gradient techniques
    • Zhang,O.W., Kay,L.E., Olivier,J.B. and Formankay,J.D. (1994) Backbone H-1 and N-15 resonance assignments of the N-terminal SH3 domain of DRK in folded and unfolded states using enhance sensitivity pulsed-fielded gradient techniques. J. Biomol. NMR, 4, 845-858.
    • (1994) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.W.1    Kay, L.E.2    Olivier, J.B.3    Formankay, J.D.4
  • 33
    • 0021754853 scopus 로고
    • Long range hydrogen bond mediated effects in peptides: 15N NMR study of gramicidin S in water and organic solvents
    • Live,D.H., Davis,D.G., Agosta,W.C. and Cowburn,D. (1984) Long range hydrogen bond mediated effects in peptides: 15N NMR study of gramicidin S in water and organic solvents. J. Am. Chem. Soc., 106, 1939-1943.
    • (1984) J. Am. Chem. Soc , vol.106 , pp. 1939-1943
    • Live, D.H.1    Davis, D.G.2    Agosta, W.C.3    Cowburn, D.4
  • 35
    • 0029338320 scopus 로고
    • Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation
    • Mori,S., Abeyguanawardana,C., Johnson,M.O. and Vanzyl,P. (1995) Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation. J. Magn. Reson. B, 108, 94-98.
    • (1995) J. Magn. Reson. B, , vol.108 , pp. 94-98
    • Mori, S.1    Abeyguanawardana, C.2    Johnson, M.O.3    Vanzyl, P.4
  • 36
    • 0000751590 scopus 로고
    • Effects of chemical exchange on NMR spectra
    • Roberts,G.C.K. (ed.), IRL Press, Oxford
    • Lian,L.-Y. and Roberts,G.C.K. (1993) Effects of chemical exchange on NMR spectra. In Roberts,G.C.K. (ed.), NMR of Macromolecules. A Practical Approach. IRL Press, Oxford, pp. 153-182.
    • (1993) NMR of Macromolecules. A Practical Approach , pp. 153-182
    • Lian, L.-Y.1    Roberts, G.C.K.2
  • 37
    • 0035103512 scopus 로고    scopus 로고
    • Solution structure of the DNA-binding domain of the TyrR protein of Haemophilus influenzae
    • Wang,Y., Zhao,S., Somerville,R.L. and Jardetzky,O. (2001) Solution structure of the DNA-binding domain of the TyrR protein of Haemophilus influenzae. Protein Sci., 10, 592-598.
    • (2001) Protein Sci , vol.10 , pp. 592-598
    • Wang, Y.1    Zhao, S.2    Somerville, R.L.3    Jardetzky, O.4
  • 38
    • 0010522432 scopus 로고
    • Structure of the repressor-operator complex of bacteriophage 434
    • Anderson,W., Ptashne,M. and Harrison,S. (1987) Structure of the repressor-operator complex of bacteriophage 434. Nature, 355, 87-89.
    • (1987) Nature , vol.355 , pp. 87-89
    • Anderson, W.1    Ptashne, M.2    Harrison, S.3
  • 40
    • 0028871814 scopus 로고
    • Evaluation of comparative protein modelling by MODELLER
    • Sali,A., Yuan,F., van Vlijmen,H. and Karplus,M. (1995) Evaluation of comparative protein modelling by MODELLER. Proteins, 23, 318-326.
    • (1995) Proteins , vol.23 , pp. 318-326
    • Sali, A.1    Yuan, F.2    van Vlijmen, H.3    Karplus, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.