메뉴 건너뛰기




Volumn 46, Issue 6, 2008, Pages 670-680

Cys-92, Cys-95, and the C-terminal 12 residues of the Vibrio harveyi ferric uptake regulator (Fur) are functionally inessential

Author keywords

Ferric uptake regulator; Mutagenesis; Transcriptional regulator; Vibrio harveyi

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; IRON UPTAKE REGULATION PROTEIN, BACTERIA; IRON-UPTAKE REGULATION PROTEIN, BACTERIA; REPRESSOR PROTEIN;

EID: 58149117801     PISSN: 12258873     EISSN: 12258873     Source Type: Journal    
DOI: 10.1007/s12275-008-0113-3     Document Type: Article
Times cited : (10)

References (33)
  • 1
  • 2
    • 0023664923 scopus 로고
    • Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli
    • A. Bagg J.B. Neilands 1987 Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli Biochemistry 26 5471 5477
    • (1987) Biochemistry , vol.26 , pp. 5471-5477
    • Bagg, A.1    Neilands, J.B.2
  • 3
    • 0029798283 scopus 로고    scopus 로고
    • Ferric uptake regulator mutants of Pseudomonas aeruginosa with distinct alterations in the iron-dependent repression of exotoxin A and siderophores in aerobic and microaerobic environments
    • H.A. Barton Z. Johnson C.D. Cox A.I. Vasil M.L. Vasil 1996 Ferric uptake regulator mutants of Pseudomonas aeruginosa with distinct alterations in the iron-dependent repression of exotoxin A and siderophores in aerobic and microaerobic environments Mol. Microbiol. 21 1001 1017
    • (1996) Mol. Microbiol. , vol.21 , pp. 1001-1017
    • Barton, H.A.1    Johnson, Z.2    Cox, C.D.3    Vasil, A.I.4    Vasil, M.L.5
  • 4
    • 1842870790 scopus 로고    scopus 로고
    • Cloning, characterisation and phylogenetic analysis of the fur gene in Vibrio salmonicida and Vibrio logei
    • D.J. Colquhoun H. Sorum 2002 Cloning, characterisation and phylogenetic analysis of the fur gene in Vibrio salmonicida and Vibrio logei Gene 296 213 220
    • (2002) Gene , vol.296 , pp. 213-220
    • Colquhoun, D.J.1    Sorum, H.2
  • 5
    • 0028151003 scopus 로고
    • Site-directed mutagenesis of the ferric uptake regulation gene of Escherichia coli
    • M. Coy C. Doyle J. Besser B.J. Neiland 1994 Site-directed mutagenesis of the ferric uptake regulation gene of Escherichia coli BioMetals 7 292 298
    • (1994) BioMetals , vol.7 , pp. 292-298
    • Coy, M.1    Doyle, C.2    Besser, J.3    Neiland, B.J.4
  • 6
    • 0025942194 scopus 로고
    • Structural dynamics and functional domains of the fur protein
    • M. Coy B.J. Neilands 1991 Structural dynamics and functional domains of the Fur protein Biochemistry 30 8201 8210
    • (1991) Biochemistry , vol.30 , pp. 8201-8210
    • Coy, M.1    Neilands, B.J.2
  • 7
    • 0031407137 scopus 로고    scopus 로고
    • Signal transduction and transcriptional and post-transcriptional control of iron-regulated genes in bacteria
    • J.H. Crosa 1997 Signal transduction and transcriptional and post-transcriptional control of iron-regulated genes in bacteria Microbiol. Mol. Biol. Rev. 61 319 336
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 319-336
    • Crosa, J.H.1
  • 8
    • 0036151995 scopus 로고    scopus 로고
    • Identification and characterization of pvuA, a gene encoding the ferric vibrioferrin receptor protein in Vibrio parahaemolyticus
    • T. Funahashi K. Moriya S. Uemura S. Miyoshi S. Shinoda S. Narimatsu S. Yamamoto 2002 Identification and characterization of pvuA, a gene encoding the ferric vibrioferrin receptor protein in Vibrio parahaemolyticus J. Bacteriol. 184 936 946
    • (2002) J. Bacteriol. , vol.184 , pp. 936-946
    • Funahashi, T.1    Moriya, K.2    Uemura, S.3    Miyoshi, S.4    Shinoda, S.5    Narimatsu, S.6    Yamamoto, S.7
  • 9
    • 0000311380 scopus 로고    scopus 로고
    • Identification of the two zinc-bound cysteines in the ferric uptake regulation protein from Escherichia coli: Chemical modification and mass spectrometry analysis
    • A. Gonzalez De Peredo C. Saint-Pierre A. Adrait L. Jacquamet J.M. Latour I. Michaud-Soret E. Forest 1999 Identification of the two zinc-bound cysteines in the ferric uptake regulation protein from Escherichia coli: chemical modification and mass spectrometry analysis Biochemistry 38 582 589
    • (1999) Biochemistry , vol.38 , pp. 582-589
    • Gonzalez De Peredo, A.1    Saint-Pierre, C.2    Adrait, A.3    Jacquamet, L.4    Latour, J.M.5    Michaud-Soret, I.6    Forest, E.7
  • 10
    • 33748426375 scopus 로고    scopus 로고
    • Iron(II) triggered conformational changes in Escherichia coli fur upon DNA binding: A study using molecular modeling
    • M.Y. Hamed S. Al-Jabour 2006 Iron(II) triggered conformational changes in Escherichia coli fur upon DNA binding: a study using molecular modeling J. Mol. Graph. Model. 25 234 246
    • (2006) J. Mol. Graph. Model. , vol.25 , pp. 234-246
    • Hamed, M.Y.1    Al-Jabour, S.2
  • 11
    • 0035069457 scopus 로고    scopus 로고
    • Iron and metal regulation in bacteria
    • K. Hantke 2001 Iron and metal regulation in bacteria Curr. Opin. Microbiol. 4 172 177
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 172-177
    • Hantke, K.1
  • 12
    • 0030199715 scopus 로고    scopus 로고
    • Identification and analysis of a gene encoding a Fur-like protein of Staphylococcus epidermis
    • C. Heidrich K. Hantke G. Bierbaum H.G. Sahl 1996 Identification and analysis of a gene encoding a Fur-like protein of Staphylococcus epidermis FEMS Microbiol. Lett. 140 253 259
    • (1996) FEMS Microbiol. Lett. , vol.140 , pp. 253-259
    • Heidrich, C.1    Hantke, K.2    Bierbaum, G.3    Sahl, H.G.4
  • 13
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • S.N. Ho H.D. Hunt R.M. Horton J.K. Pullen L.R. Pease 1989 Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 77 51 59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 15
    • 33645037891 scopus 로고    scopus 로고
    • 2 by metal-catalysed histidine oxidation
    • 2 by metal-catalysed histidine oxidation Nature 440 363 367
    • (2006) Nature , vol.440 , pp. 363-367
    • Lee, J.W.1    Helmann, J.D.2
  • 16
    • 0036667431 scopus 로고    scopus 로고
    • The ferric uptake regulator of Pseudomonas aeruginosa has no essential cysteine residues and does not contain a structural zinc ion
    • A.C. Lewin P.A. Doughty L. Flegg G.R. Moore S. Spiro 2002 The ferric uptake regulator of Pseudomonas aeruginosa has no essential cysteine residues and does not contain a structural zinc ion Microbiology 148 2449 2456
    • (2002) Microbiology , vol.148 , pp. 2449-2456
    • Lewin, A.C.1    Doughty, P.A.2    Flegg, L.3    Moore, G.R.4    Spiro, S.5
  • 17
    • 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
    • Q. Liu P. Wang Y. Ma 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
  • 18
    • 1442306069 scopus 로고    scopus 로고
    • Genetic and biophysical studies of diphtheria toxin repressor (DtxR) and the hyperactive mutant DtxR(E175K) support a multistep model of activation
    • J.F. Love J.C. vanderSpek V. Marin L. Guerrero T.M. Logan J.R. Murphy 2004 Genetic and biophysical studies of diphtheria toxin repressor (DtxR) and the hyperactive mutant DtxR(E175K) support a multistep model of activation Proc. Natl. Acad. Sci. USA 101 2506 2511
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2506-2511
    • Love, J.F.1    Vanderspek, J.C.2    Marin, V.3    Guerrero, L.4    Logan, T.M.5    Murphy, J.R.6
  • 19
    • 4844220209 scopus 로고    scopus 로고
    • Involvement of genes of genome maintenance in the regulation of phase variation frequencies in Neisseria meningitides
    • P. Martin L. Sun D. Hood E.R. Moxon 2004 Involvement of genes of genome maintenance in the regulation of phase variation frequencies in Neisseria meningitides Microbiology 150 3001 3012
    • (2004) Microbiology , vol.150 , pp. 3001-3012
    • Martin, P.1    Sun, L.2    Hood, D.3    Moxon, E.R.4
  • 20
    • 0003842951 scopus 로고
    • Cold Spring Harbor, Cold Spring Harbor Laboratory New York, N.Y., USA
    • Miller, J.H. 1992. A Short Course in Bacterial Genetics. Cold Spring Harbor, Cold Spring Harbor Laboratory, New York, N.Y., USA.
    • (1992) A Short Course in Bacterial Genetics
    • Miller, J.H.1
  • 21
    • 0028789238 scopus 로고
    • Role of the ferric uptake regulator of Pseudomonas aeruginosa in the regulation of siderophores and exotoxin A expression: Purification and activity on iron-regulated promoters
    • U.A. Ochsner A.I. Vasil M.L. Vasil 1995 Role of the ferric uptake regulator of Pseudomonas aeruginosa in the regulation of siderophores and exotoxin A expression: purification and activity on iron-regulated promoters J. Bacteriol. 177 7194 7201
    • (1995) J. Bacteriol. , vol.177 , pp. 7194-7201
    • Ochsner, U.A.1    Vasil, A.I.2    Vasil, M.L.3
  • 22
    • 33746455962 scopus 로고    scopus 로고
    • Structural changes of Escherichia coli ferric uptake regulator during metal-dependent dimerization and activation explored by NMR and X-ray crystallography
    • L. Pecqueur B. D'Autreaux J. Dupuy Y. Nicolet L. Jacquamet B. Brutscher I. Michaud-Soret B. Bersch 2006 Structural changes of Escherichia coli ferric uptake regulator during metal-dependent 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'Autreaux, B.2    Dupuy, J.3    Nicolet, Y.4    Jacquamet, L.5    Brutscher, B.6    Michaud-Soret, I.7    Bersch, B.8
  • 23
    • 0344321893 scopus 로고    scopus 로고
    • Architecture of a protein central to iron homeostasis: Crystal structure and spectroscopic analysis of the ferric uptake regulator
    • E. Pohl J.C. Haller A. Mijovilovich W. Meyer-Klaucke E. German M.L. Vesil 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    German, E.5    Vesil, M.L.6
  • 24
    • 21344451201 scopus 로고    scopus 로고
    • The ferric iron uptake regulator (Fur) from the extreme acidophile Acidithiobacillus ferrooxidans
    • R. Quatrini C. Lefimil D.S. Holmes E. Jedlicki 2005 The ferric iron uptake regulator (Fur) from the extreme acidophile Acidithiobacillus ferrooxidans Microbiology 151 2005 2015
    • (2005) Microbiology , vol.151 , pp. 2005-2015
    • Quatrini, R.1    Lefimil, C.2    Holmes, D.S.3    Jedlicki, E.4
  • 25
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • C. Ratledge L.G. Dover 2000 Iron metabolism in pathogenic bacteria Annu. Rev. Microbiol. 54 881 941
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 26
    • 0025847932 scopus 로고
    • Some structural features of the iron-uptake regulation protein
    • T. Saito M.R. Womlad R.J.P. Williams 1991 Some structural features of the iron-uptake regulation protein Eur. J. Biochem. 197 29 39
    • (1991) Eur. J. Biochem. , vol.197 , pp. 29-39
    • Saito, T.1    Womlad, M.R.2    Williams, R.J.P.3
  • 27
    • 0028960213 scopus 로고
    • Functional domains of the Escherichia coli ferric uptake regulator protein (Fur)
    • I. Stojiljkovic K. Hantke 1995 Functional domains of the Escherichia coli ferric uptake regulator protein (Fur) Mol. Gen. Genet. 247 199 205
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 199-205
    • Stojiljkovic, I.1    Hantke, K.2
  • 28
    • 0032410749 scopus 로고    scopus 로고
    • Isolation and characterization of iron-independent positive dominant mutants of Diphtheria toxin repressor, DtxR
    • L. Sun J. vanderSpek J.R. Murphy 1998 Isolation and characterization of iron-independent positive dominant mutants of Diphtheria toxin repressor, DtxR Proc. Natl. Acad. Sci. USA 95 14985 14990
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14985-14990
    • Sun, L.1    Vanderspek, J.2    Murphy, J.R.3
  • 30
    • 46749152298 scopus 로고    scopus 로고
    • Molecular analysis of the fur (ferric uptake regulator) gene of a pathogenic Edwardsiella tarda strain
    • F. Wang S. Cheng K. Sun L. Sun 2008 Molecular analysis of the fur (ferric uptake regulator) gene of a pathogenic Edwardsiella tarda strain J. Microbiol. 46 350 355
    • (2008) J. Microbiol. , vol.46 , pp. 350-355
    • Wang, F.1    Cheng, S.2    Sun, K.3    Sun, L.4
  • 31
    • 34548660839 scopus 로고    scopus 로고
    • Isolation, sequencing and characterization of cluster genes involved in the biosynthesis and utilization of the siderophore of marine fish pathogen Vibrio alginolyticus
    • Q. Wang Q. Liu Y. Ma L. Zhou Y. Zhang 2007 Isolation, sequencing and characterization of cluster genes involved in the biosynthesis and utilization of the siderophore of marine fish pathogen Vibrio alginolyticus Arch. Microbiol. 188 433 439
    • (2007) Arch. Microbiol. , vol.188 , pp. 433-439
    • Wang, Q.1    Liu, Q.2    Ma, Y.3    Zhou, L.4    Zhang, Y.5
  • 32
    • 34248162825 scopus 로고    scopus 로고
    • Cloning, characterization and molecular application of a beta-agarase gene from Vibrio sp. strain V134
    • W. Zhang L. Sun 2007 Cloning, characterization and molecular application of a beta-agarase gene from Vibrio sp. strain V134 Appl. Environ. Microbiol. 73 2825 2831
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 2825-2831
    • Zhang, W.1    Sun, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.