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Volumn 48, Issue 2, 2010, Pages 174-183

Experimental and computational characterization of the ferric uptake regulator from Aliivibrio salmonicida (Vibrio salmonicida)

Author keywords

A. salmonicida; Ferric uptake regulator; Fur; Iron homeostasis; V. salmonicida

Indexed keywords

BACTERIAL DNA; BACTERIAL PROTEIN; FERRIC ION; IRON UPTAKE REGULATION PROTEIN, BACTERIA; IRON-UPTAKE REGULATION PROTEIN, BACTERIA; REPRESSOR PROTEIN;

EID: 77951996341     PISSN: 12258873     EISSN: 12258873     Source Type: Journal    
DOI: 10.1007/s12275-010-9199-5     Document Type: Article
Times cited : (5)

References (32)
  • 1
    • 65949100228 scopus 로고    scopus 로고
    • Ferric uptake regulator protein: Binding free energy calculations and per-residue free energy decomposition
    • Ahmad, R., B. O. Brandsdal, I. Michaud-Soret, and N. P. Willassen. 2009a. Ferric uptake regulator protein: Binding free energy calculations and per-residue free energy decomposition. Proteins 75, 373-386.
    • (2009) Proteins , vol.75 , pp. 373-386
    • Ahmad, R.1    Brandsdal, B.O.2    Michaud-Soret, I.3    Willassen, N.P.4
  • 3
    • 0036035079 scopus 로고    scopus 로고
    • Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon
    • Baichoo, N., T. Wang, R. Ye, and J. D. Helmann. 2002. Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon. Mol. Microbiol. 45, 1613-1629.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1613-1629
    • Baichoo, N.1    Wang, T.2    Ye, R.3    Helmann, J.D.4
  • 6
    • 0035183674 scopus 로고    scopus 로고
    • Temperature dependent siderophore production in Vibrio salmonicida
    • Colquhoun, D. J. and H. Søum. 2001. Temperature dependent siderophore production in Vibrio salmonicida. Microb. Pathog. 31, 213-219.
    • (2001) Microb. Pathog. , vol.31 , pp. 213-219
    • Colquhoun, D.J.1    Søum, H.2
  • 8
    • 0023258960 scopus 로고
    • Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor
    • de Lorenzo, V., S. Wee, M. Herrero, and J. B. Neilands. 1987. Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor. J. Bacteriol. 169, 2624-2630.
    • (1987) J. Bacteriol. , vol.169 , pp. 2624-2630
    • de Lorenzo, V.1    Wee, S.2    Herrero, M.3    Neilands, J.B.4
  • 9
    • 3042816068 scopus 로고    scopus 로고
    • Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis
    • Delany, I., R. Rappuoli, and V. Scarlato. 2004. Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis. Mol. Microbiol. 52, 1081-1090.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1081-1090
    • Delany, I.1    Rappuoli, R.2    Scarlato, V.3
  • 10
    • 0142214661 scopus 로고    scopus 로고
    • Recognition of DNA by three ferric uptake regulator (Fur) homologs in Bacillus subtilis
    • Fuangthong, M. and J. D. Helmann. 2003. Recognition of DNA by three ferric uptake regulator (Fur) homologs in Bacillus subtilis. J. Bacteriol. 185, 6348-6357.
    • (2003) J. Bacteriol. , vol.185 , pp. 6348-6357
    • Fuangthong, M.1    Helmann, J.D.2
  • 13
    • 0019447069 scopus 로고
    • Regulation of ferric iron transport in Escherichia coli K12: Isolation of a constitutive mutant
    • Hantke, K. 1981. Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant. Mol. Gen. Genet. 182, 288-292.
    • (1981) Mol. Gen. Genet. , vol.182 , pp. 288-292
    • Hantke, K.1
  • 14
    • 59449093840 scopus 로고    scopus 로고
    • The genome sequence of the fish pathogen Aliivibrio salmonicida strain LFI1238 shows extensive evidence of gene decay
    • Hjerde, E., M. S. Lorentzen, M. T. Holden, K. Seeger, S. Paulsen, N. Bason, C. Churcher, and et al. 2008. The genome sequence of the fish pathogen Aliivibrio salmonicida strain LFI1238 shows extensive evidence of gene decay. BMC Genomics 9, 616.
    • (2008) BMC Genomics , vol.9 , pp. 616
    • Hjerde, E.1    Lorentzen, M.S.2    Holden, M.T.3    Seeger, K.4    Paulsen, S.5    Bason, N.6    Churcher, C.7
  • 15
    • 0034521981 scopus 로고    scopus 로고
    • Calculating structures and free energies of complex molecules: Combining molecular mechanics and continuum models
    • Kollman, P. A., I. Massova, C. Reyes, B. Kuhn, S. Huo, L. Chong, M. Lee, and et al. 2000. Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models. Acc. Chem. Res. 33, 889-897.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 889-897
    • Kollman, P.A.1    Massova, I.2    Reyes, C.3    Kuhn, B.4    Huo, S.5    Chong, L.6    Lee, M.7
  • 16
    • 0028113847 scopus 로고
    • Observation of binding and polymerization of Fur repressor onto operator-containing DNA with electron and atomic force microscopes
    • Le Cam, E., D. Frechon, M. Barray, A. Fourcade, and E. Delain. 1994. Observation of binding and polymerization of Fur repressor onto operator-containing DNA with electron and atomic force microscopes. Proc. Natl. Acad. Sci. USA 91, 11816-11820.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11816-11820
    • Le Cam, E.1    Frechon, D.2    Barray, M.3    Fourcade, A.4    Delain, E.5
  • 17
    • 34147151006 scopus 로고    scopus 로고
    • Positive regulation of fur gene expression via direct interaction of Fur in a pathogenic bacterium, Vibrio vulnificus
    • Lee, H. J., S. H. Bang, K. H. Lee, and S. J. Park. 2007. Positive regulation of fur gene expression via direct interaction of Fur in a pathogenic bacterium, Vibrio vulnificus. J. Bacteriol. 189, 2629-2636.
    • (2007) J. Bacteriol. , vol.189 , pp. 2629-2636
    • Lee, H.J.1    Bang, S.H.2    Lee, K.H.3    Park, S.J.4
  • 18
    • 34548666597 scopus 로고    scopus 로고
    • Characterization of the Vibrio alginolyticus fur gene and localization of essential amino acid sites in fur by site-directed mutagenesis
    • Liu, Q., P. Wang, Y. Ma, and Y. Zhang. 2007. Characterization of the Vibrio alginolyticus fur gene and localization of essential amino acid sites in fur by site-directed mutagenesis. J. Mol. Microbiol. Biotechnol. 13, 15-21.
    • (2007) J. Mol. Microbiol. Biotechnol. , vol.13 , pp. 15-21
    • Liu, Q.1    Wang, P.2    Ma, Y.3    Zhang, Y.4
  • 19
    • 0141860088 scopus 로고    scopus 로고
    • Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli
    • Massé, E., F. E. Escorcia, and S. Gottesman. 2003. Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli. Genes Dev. 17, 2374-2383.
    • (2003) Genes Dev. , vol.17 , pp. 2374-2383
    • Massé, E.1    Escorcia, F.E.2    Gottesman, S.3
  • 20
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • Massé, E. and S. Gottesman. 2002. A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc. Natl. Acad. Sci. USA 99, 4620-4625.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4620-4625
    • Massé, E.1    Gottesman, S.2
  • 21
    • 23944509113 scopus 로고    scopus 로고
    • Characterization of Vibrio cholerae RyhB: The RyhB regulon and role of ryhB in biofilm formation
    • Mey, A. R., S. A. Craig, and S. M. Payne. 2005a. Characterization of Vibrio cholerae RyhB: the RyhB regulon and role of ryhB in biofilm formation. Infect. Immun. 73, 5706-5719.
    • (2005) Infect. Immun. , vol.73 , pp. 5706-5719
    • Mey, A.R.1    Craig, S.A.2    Payne, S.M.3
  • 22
    • 28444438519 scopus 로고    scopus 로고
    • Iron and Fur regulation in Vibrio cholerae and the role of Fur in virulence
    • Mey, A. R., E. E. Wyckoff, V. Kanukurthy, C. R. Fisher, and S. M. Payne. 2005b. Iron and Fur regulation in Vibrio cholerae and the role of Fur in virulence. Infect. Immun. 73, 8167-8178.
    • (2005) Infect. Immun. , vol.73 , pp. 8167-8178
    • Mey, A.R.1    Wyckoff, E.E.2    Kanukurthy, V.3    Fisher, C.R.4    Payne, S.M.5
  • 23
    • 33746455962 scopus 로고    scopus 로고
    • Structural changes of Escherichia coli ferric uptake regulator during metaldependent dimerization and activation explored by NMR and X-ray crystallography
    • Pecqueur, L., B. D'Autréaux, J. Dupuy, Y. Nicolet, L. Jacquamet, B. Brutscher, I. Michaud-Soret, and B. Bersch. 2006. Structural changes of Escherichia coli ferric uptake regulator during metaldependent dimerization and activation explored by NMR and X-ray crystallography. J. Biol. Chem. 281, 21286-21295.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21286-21295
    • Pecqueur, L.1    D'Autréaux, B.2    Dupuy, J.3    Nicolet, Y.4    Jacquamet, L.5    Brutscher, B.6    Michaud-Soret, I.7    Bersch, B.8
  • 24
    • 0344321893 scopus 로고    scopus 로고
    • Architecture of a protein central to iron homeostasis: Crystal structure and spectroscopic analysis of the ferric uptake regulator
    • Pohl, E., J. C. Haller, A. Mijovilovich, W. Meyer-Klaucke, E. Garman, and M. L. Vasil. 2003. Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator. Mol. Microbiol. 47, 903-915.
    • (2003) Mol. Microbiol. , vol.47 , pp. 903-915
    • Pohl, E.1    Haller, J.C.2    Mijovilovich, A.3    Meyer-Klaucke, W.4    Garman, E.5    Vasil, M.L.6
  • 25
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. and T. L. Blundell. 1993. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 26
    • 65949087462 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co-ordination
    • Sheikh, A. and G. L. Taylor. 2009. Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co-ordination. Mol. Microbiol. 75, 1208-1220.
    • (2009) Mol. Microbiol. , vol.75 , pp. 1208-1220
    • Sheikh, A.1    Taylor, G.L.2
  • 27
    • 0032560959 scopus 로고    scopus 로고
    • Continuum solvent studies of the stability of DNA, RNA, and phosphoramidate-DNA helices
    • Srinivasan, J., T. E. Cheatham, 3rd, P. Cieplak, P. A. Kollman, and D. A. Case. 1998. Continuum solvent studies of the stability of DNA, RNA, and phosphoramidate-DNA helices. J. Am. Chem. Soc. 120, 9401-9409.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9401-9409
    • Srinivasan, J.1    Cheatham 3rd, T.E.2    Cieplak, P.3    Kollman, P.A.4    Case, D.A.5
  • 28
    • 0028327173 scopus 로고
    • Fur regulon in Gram-negative bacteria Identification and characterization of new iron-regulated Escherichia coli genes by a fur titration assay
    • Stojiljkovic, I., A. J. Bäumler, and K. Hantke. 1994. Fur regulon in Gram-negative bacteria Identification and characterization of new iron-regulated Escherichia coli genes by a fur titration assay. J. Mol. Biol. 236, 531-545. Erratum in: J. Mol. Biol. 1994. 240, 271.
    • (1994) J. Mol. Biol. , vol.236 , pp. 531-545
    • Stojiljkovic, I.1    Bäumler, A.J.2    Hantke, K.3
  • 29
    • 58149117801 scopus 로고    scopus 로고
    • Cys-92, Cys-95, and the C-terminal 12 residues of the Vibrio harveyi ferric uptake regulator (Fur) are functionally inessential
    • Sun, K., S. Cheng, M. Zhang, F. Wang, and L. Sun. 2008. Cys-92, Cys-95, and the C-terminal 12 residues of the Vibrio harveyi ferric uptake regulator (Fur) are functionally inessential. J. Microbiol. 46, 670-680.
    • (2008) J. Microbiol. , vol.46 , pp. 670-680
    • Sun, K.1    Cheng, S.2    Zhang, M.3    Wang, F.4    Sun, L.5
  • 30
    • 36549007472 scopus 로고    scopus 로고
    • Phylogenetic analysis of vibrios and related species by means of atpA gene sequences
    • Thompson, C. C., F. L. Thompson, A. C. Vicente, and J. Swings. 2007. Phylogenetic analysis of vibrios and related species by means of atpA gene sequences. Int. J. Syst. Evol. Microbiol. 57, 2480-2484.
    • (2007) Int. J. Syst. Evol. Microbiol. , vol.57 , pp. 2480-2484
    • Thompson, C.C.1    Thompson, F.L.2    Vicente, A.C.3    Swings, J.4
  • 31
    • 26844508470 scopus 로고    scopus 로고
    • Characterization of the DNA-binding site in the ferric uptake regulator protein from Escherichia coli by UV crosslinking and mass spectrometry
    • Tiss, A., O. Barre, I. Michaud-Soret, and E. Forest. 2005. Characterization of the DNA-binding site in the ferric uptake regulator protein from Escherichia coli by UV crosslinking and mass spectrometry. FEBS Lett. 579, 5454-5460.
    • (2005) FEBS Lett. , vol.579 , pp. 5454-5460
    • Tiss, A.1    Barre, O.2    Michaud-Soret, I.3    Forest, E.4
  • 32
    • 33645461831 scopus 로고    scopus 로고
    • Global analysis of iron assimilation and fur regulation in Yersinia pestis
    • Zhou, D., L. Qin, Y. Han, J. Qiu, Z. Chen, B. Li, Y. Song, and et al. 2006. Global analysis of iron assimilation and fur regulation in Yersinia pestis. FEMS Microbiol. Lett. 258, 9-17.
    • (2006) FEMS Microbiol. Lett. , vol.258 , pp. 9-17
    • Zhou, D.1    Qin, L.2    Han, Y.3    Qiu, J.4    Chen, Z.5    Li, B.6    Song, Y.7


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