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Volumn 191, Issue 5, 2009, Pages 1595-1603

Regulation and activity of a zinc uptake regulator, zur, in Corynebacterium diphtheriae

Author keywords

[No Author keywords available]

Indexed keywords

FERRIC UPTAKE REGULATOR; IRON; MANGANESE; MESSENGER RNA; METAL ION; PEROXIDE; PROTEIN; REPRESSOR PROTEIN; UNCLASSIFIED DRUG; ZINC; ZUR PROTEIN; BACTERIAL PROTEIN; DNA BINDING PROTEIN; HYDROGEN PEROXIDE;

EID: 62649162905     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01392-08     Document Type: Article
Times cited : (45)

References (44)
  • 2
    • 0000280261 scopus 로고    scopus 로고
    • Barksdale, L., and M. Pappenheimer, Jr. 1954. Phage-host relationships in nontoxigenic and toxigenic diphtheria bacilli. J. Bacteriol. 67:220-232.
    • Barksdale, L., and M. Pappenheimer, Jr. 1954. Phage-host relationships in nontoxigenic and toxigenic diphtheria bacilli. J. Bacteriol. 67:220-232.
  • 3
    • 0029086474 scopus 로고
    • Inhibition of the cytochrome bd-terminated NADH oxidase system in Escherichia coli K-12 by divalent metal cations
    • Beard, S. J., M. N. Hughes, and R. K. Poole. 1995. Inhibition of the cytochrome bd-terminated NADH oxidase system in Escherichia coli K-12 by divalent metal cations. FEMS Microbiol. Lett. 131:205-210.
    • (1995) FEMS Microbiol. Lett , vol.131 , pp. 205-210
    • Beard, S.J.1    Hughes, M.N.2    Poole, R.K.3
  • 4
    • 27744497470 scopus 로고    scopus 로고
    • Analysis of a heme-dependent signal transduction system in Corynebactetium diphtheriae: Deletion of the chrAS genes results in heme sensitivity and diminished heme-dependent activation of the hmuO promoter
    • Bibb, L. A., N. D. King, C. A. Kunkle, and M. P. Schmitt. 2005. Analysis of a heme-dependent signal transduction system in Corynebactetium diphtheriae: deletion of the chrAS genes results in heme sensitivity and diminished heme-dependent activation of the hmuO promoter. Infect. Immun. 73:7406-7412.
    • (2005) Infect. Immun , vol.73 , pp. 7406-7412
    • Bibb, L.A.1    King, N.D.2    Kunkle, C.A.3    Schmitt, M.P.4
  • 5
    • 0025239795 scopus 로고
    • The physiological role of zinc as an antioxidant
    • Bray, T. M., and W. J. Bettger. 1990. The physiological role of zinc as an antioxidant. Free Radic Biol. Med. 8:281-291.
    • (1990) Free Radic Biol. Med , vol.8 , pp. 281-291
    • Bray, T.M.1    Bettger, W.J.2
  • 6
    • 0037565104 scopus 로고    scopus 로고
    • The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance
    • Busenlehner, L. S., M. A. Pennella, and D. P. Giedroc. 2003. The SmtB/ArsR family of metalloregulatory transcriptional repressors: structural insights into prokaryotic metal resistance. FEMS Microbiol. Rev. 27:131-143.
    • (2003) FEMS Microbiol. Rev , vol.27 , pp. 131-143
    • Busenlehner, L.S.1    Pennella, M.A.2    Giedroc, D.P.3
  • 7
    • 0036073696 scopus 로고    scopus 로고
    • Role of the high-affinity zinc uptake znuABC system in Salmonella enterica serovar Typhimurium virulence
    • Campoy, S., M. Jara, N. Busquets, A. M. Perez De Rozas, I. Badiola, and J. Barbe. 2002. Role of the high-affinity zinc uptake znuABC system in Salmonella enterica serovar Typhimurium virulence. Infect. Immun. 70:4721-725.
    • (2002) Infect. Immun , vol.70 , pp. 4721-4725
    • Campoy, S.1    Jara, M.2    Busquets, N.3    Perez De Rozas, A.M.4    Badiola, I.5    Barbe, J.6
  • 8
    • 23644435460 scopus 로고    scopus 로고
    • Rv2358 and FurB: Two transcriptional regulators from Mycobacterium tuberculosis which respond to zinc
    • Canneva, F., M. Branzoni, G. Riccardi, R. Provvedi, and A. Milano. 2005. Rv2358 and FurB: two transcriptional regulators from Mycobacterium tuberculosis which respond to zinc. J. Bacteriol. 187:5837-5840.
    • (2005) J. Bacteriol , vol.187 , pp. 5837-5840
    • Canneva, F.1    Branzoni, M.2    Riccardi, G.3    Provvedi, R.4    Milano, A.5
  • 9
    • 10744229660 scopus 로고    scopus 로고
    • Cerdeno-Tarraga, A. M., A. Efstratiou, L. G. Dover, M. T. Holden, M. Pallen, S. D. Bentley, G. S. Besra, C. Churcher, K. D. James, A. De Zoysa, T. Chillingworth, A. Cronin, L. Dowd, T. Feltwell, N. Hamlin, S. Holroyd, K. Jagels, S. Moule, M. A. Quail, E. Rabbinowitsch, K. M. Rutherford, N. R. Thomson, L. Unwin, S. Whitehead, B. G. Barrell, and J. Parkhill. 2003. The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129. Nucleic Acids Res. 31:6516-6523.
    • Cerdeno-Tarraga, A. M., A. Efstratiou, L. G. Dover, M. T. Holden, M. Pallen, S. D. Bentley, G. S. Besra, C. Churcher, K. D. James, A. De Zoysa, T. Chillingworth, A. Cronin, L. Dowd, T. Feltwell, N. Hamlin, S. Holroyd, K. Jagels, S. Moule, M. A. Quail, E. Rabbinowitsch, K. M. Rutherford, N. R. Thomson, L. Unwin, S. Whitehead, B. G. Barrell, and J. Parkhill. 2003. The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129. Nucleic Acids Res. 31:6516-6523.
  • 11
    • 0037373315 scopus 로고    scopus 로고
    • Bacterial [Cu,Zn]-cofactored superoxide dismutase protects opsonized, encapsulated Neisseria meningitidis from phagocytosis by human monocytes/macrophages
    • Dunn, K. L., J. L. Farrant, P. R. Langford, and J. S. Kroll. 2003. Bacterial [Cu,Zn]-cofactored superoxide dismutase protects opsonized, encapsulated Neisseria meningitidis from phagocytosis by human monocytes/macrophages. Infect. Immun. 71:1604-1607.
    • (2003) Infect. Immun , vol.71 , pp. 1604-1607
    • Dunn, K.L.1    Farrant, J.L.2    Langford, P.R.3    Kroll, J.S.4
  • 12
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: Transcriptional metalloregulation by the Fur protein
    • Escolar, L., J. Perez-Martin, and V. de Lorenzo. 1999. Opening the iron box: transcriptional metalloregulation by the Fur protein. J. Bacteriol. 181:6223-6229.
    • (1999) J. Bacteriol , vol.181 , pp. 6223-6229
    • Escolar, L.1    Perez-Martin, J.2    de Lorenzo, V.3
  • 13
    • 0036041795 scopus 로고    scopus 로고
    • A peroxide-induced zinc uptake system plays an important role in protection against oxidative stress in Bacillus subtilis
    • Gaballa, A., and J. D. Helmann. 2002. A peroxide-induced zinc uptake system plays an important role in protection against oxidative stress in Bacillus subtilis. Mol. Microbiol. 45:997-1005.
    • (2002) Mol. Microbiol , vol.45 , pp. 997-1005
    • Gaballa, A.1    Helmann, J.D.2
  • 14
    • 0031733646 scopus 로고    scopus 로고
    • Identification of a zinc-specific metalloregulatory protein. Zur. controlling zinc transport Operons in Bacillus subtilb
    • Gaballa, A., and J. D. Helmann. 1998. Identification of a zinc-specific metalloregulatory protein. Zur. controlling zinc transport Operons in Bacillus subtilb. J. Bacteriol. 180:5815-5821.
    • (1998) J. Bacteriol , vol.180 , pp. 5815-5821
    • Gaballa, A.1    Helmann, J.D.2
  • 15
    • 0036889461 scopus 로고    scopus 로고
    • Functional analysis of the Bacillus subtilis Zur regulon
    • Gaballa, A., T. Wang, R. W. Ye, and J. D. Helmann. 2002. Functional analysis of the Bacillus subtilis Zur regulon. J. Bacteriol. 184:6508-6514.
    • (2002) J. Bacteriol , vol.184 , pp. 6508-6514
    • Gaballa, A.1    Wang, T.2    Ye, R.W.3    Helmann, J.D.4
  • 16
    • 0035696323 scopus 로고    scopus 로고
    • Bacterial zinc transporters and regulators
    • Hantke, K. 2001. Bacterial zinc transporters and regulators. Biometals 14: 239-249.
    • (2001) Biometals , vol.14 , pp. 239-249
    • Hantke, K.1
  • 17
    • 0030766168 scopus 로고    scopus 로고
    • Identification and transcriptional analysis of a Treponema pallidum operon encoding a putative ABC transport system, an iron-activated repressor protein homolog, and a glycolytic pathway enzyme homolog
    • Hardham, J. M., L. V. Stamm, S. F. Porcella, J. G. Frye, N. Y. Barnes, J. K. Howell, S. L. Mueller, J. D. Radolf, G. M. Weinstock, and S. J. Norris. 1997. Identification and transcriptional analysis of a Treponema pallidum operon encoding a putative ABC transport system, an iron-activated repressor protein homolog, and a glycolytic pathway enzyme homolog. Gene 197:47-64.
    • (1997) Gene , vol.197 , pp. 47-64
    • Hardham, J.M.1    Stamm, L.V.2    Porcella, S.F.3    Frye, J.G.4    Barnes, N.Y.5    Howell, J.K.6    Mueller, S.L.7    Radolf, J.D.8    Weinstock, G.M.9    Norris, S.J.10
  • 18
    • 0034107745 scopus 로고    scopus 로고
    • Biology and molecular epidemiology of diphtheria toxin and the tox gene
    • Holmes, R. K. 2000. Biology and molecular epidemiology of diphtheria toxin and the tox gene. J. Infect. Dis. 181(Suppl. 1):S156-S167.
    • (2000) J. Infect. Dis , vol.181 , Issue.SUPPL. 1
    • Holmes, R.K.1
  • 19
    • 48349136542 scopus 로고    scopus 로고
    • The Zur of Xanthomo-nas campestris functions as a repressor and an activator of putative zinc homeostasis genes via recognizing two distinct sequences within its target promoters
    • Huang, D. L., D. J. Tang, Q. Liao, H. C. Li, Q. Chen, Y. Q. He, J. X. Feng, B. L. Jiang, G. T. Lu, B. Chen, and J. L. Tang. 2008. The Zur of Xanthomo-nas campestris functions as a repressor and an activator of putative zinc homeostasis genes via recognizing two distinct sequences within its target promoters. Nucleic Acids Res. 36:4295-4309.
    • (2008) Nucleic Acids Res , vol.36 , pp. 4295-4309
    • Huang, D.L.1    Tang, D.J.2    Liao, Q.3    Li, H.C.4    Chen, Q.5    He, Y.Q.6    Feng, J.X.7    Jiang, B.L.8    Lu, G.T.9    Chen, B.10    Tang, J.L.11
  • 20
    • 0034687698 scopus 로고    scopus 로고
    • Identification of motifs in cholera toxin A1 polypeptide that are required for its interaction with human ADP-ribosylation factor 6 in a bacterial two-hybrid system
    • Jobling, M. G., and R. K. Holmes. 2000. Identification of motifs in cholera toxin A1 polypeptide that are required for its interaction with human ADP-ribosylation factor 6 in a bacterial two-hybrid system. Proc. Natl. Acad. Sci. USA 97:14662-14667.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14662-14667
    • Jobling, M.G.1    Holmes, R.K.2
  • 22
    • 34248669001 scopus 로고    scopus 로고
    • Functional specialization within the Fur family of metalloregulators
    • Lee, J. W., and J. D. Helmann. 2007. Functional specialization within the Fur family of metalloregulators. Biometals 20:485-499.
    • (2007) Biometals , vol.20 , pp. 485-499
    • Lee, J.W.1    Helmann, J.D.2
  • 24
    • 1842575639 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis Rv2358-furB Operon is induced by zinc
    • Milano, A., M. Branzoni, F. Canneva, A. Profumo, and G. Riccardi. 2004. The Mycobacterium tuberculosis Rv2358-furB Operon is induced by zinc. Res. Microbiol. 155:192-200.
    • (2004) Res. Microbiol , vol.155 , pp. 192-200
    • Milano, A.1    Branzoni, M.2    Canneva, F.3    Profumo, A.4    Riccardi, G.5
  • 26
    • 0037177829 scopus 로고    scopus 로고
    • Membrane potential-controlled inhibition of cytochrome c oxidase by zinc
    • Mills, D. A., B. Schmidt, C. Hiser, E. Westley, and S. Ferguson-Miller. 2002. Membrane potential-controlled inhibition of cytochrome c oxidase by zinc. J. Biol. Chem. 277:14894-14901.
    • (2002) J. Biol. Chem , vol.277 , pp. 14894-14901
    • Mills, D.A.1    Schmidt, B.2    Hiser, C.3    Westley, E.4    Ferguson-Miller, S.5
  • 27
    • 0018140198 scopus 로고
    • Evidence that the regulation of diphtheria toxin production is directed at the level of transcription
    • Murphy, J. R., J. L. Michel, and M. Teng. 1978. Evidence that the regulation of diphtheria toxin production is directed at the level of transcription. J. Bacteriol. 135:511-516.
    • (1978) J. Bacteriol , vol.135 , pp. 511-516
    • Murphy, J.R.1    Michel, J.L.2    Teng, M.3
  • 28
    • 0036786304 scopus 로고    scopus 로고
    • Construction and characterization of transposon insertion mutations in Corynebacterium diph-theriae that affect expression of the diphtheria toxin repressor (DtxR)
    • Oram, D. M., A. Avdalovic, and R. K. Holmes. 2002. Construction and characterization of transposon insertion mutations in Corynebacterium diph-theriae that affect expression of the diphtheria toxin repressor (DtxR). J. Bacteriol. 184:5723-5732.
    • (2002) J. Bacteriol , vol.184 , pp. 5723-5732
    • Oram, D.M.1    Avdalovic, A.2    Holmes, R.K.3
  • 29
    • 33645977164 scopus 로고    scopus 로고
    • Transcription of the contiguous sigB, dtxR, and galE genes in Corynebacterium diphtheriae: Evidence for multiple transcripts and regulation by environmental factors
    • Oram, D. M., A. D. Jacobson, and R. K. Holmes. 2006. Transcription of the contiguous sigB, dtxR, and galE genes in Corynebacterium diphtheriae: evidence for multiple transcripts and regulation by environmental factors. J. Bacteriol. 188:2959-2973.
    • (2006) J. Bacteriol , vol.188 , pp. 2959-2973
    • Oram, D.M.1    Jacobson, A.D.2    Holmes, R.K.3
  • 30
    • 33847653735 scopus 로고    scopus 로고
    • Bacteriophage-based vectors for site-specific insertion of DNA in the chromosome of corynebacteria
    • Oram, M., J. E. Woolston, A. D. Jacobson, R. K. Holmes, and D. M. Oram. 2007. Bacteriophage-based vectors for site-specific insertion of DNA in the chromosome of corynebacteria. Gene 391:53-62.
    • (2007) Gene , vol.391 , pp. 53-62
    • Oram, M.1    Woolston, J.E.2    Jacobson, A.D.3    Holmes, R.K.4    Oram, D.M.5
  • 31
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of met-alloregulatory proteins controlling zinc homeostasis
    • Outten, C. E., and T. V. O'Halloran. 2001. Femtomolar sensitivity of met-alloregulatory proteins controlling zinc homeostasis. Science 292:2488-2492.
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 32
    • 0043193943 scopus 로고    scopus 로고
    • Comparative genomics of bacterial zinc regulons: Enhanced ion transport, pathogenesis, and rearrangement of ribosomal proteins
    • Panina, E. M., A. A. Mironov, and M. S. Gelfand. 2003. Comparative genomics of bacterial zinc regulons: enhanced ion transport, pathogenesis, and rearrangement of ribosomal proteins. Proc. Natl. Acad. Sci. USA 100:9912-9917.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9912-9917
    • Panina, E.M.1    Mironov, A.A.2    Gelfand, M.S.3
  • 33
    • 0034902162 scopus 로고    scopus 로고
    • 2+ transporter in Escherichia coli
    • 2+ transporter in Escherichia coli, J. Bacteriol. 183:4806-4813.
    • (2001) J. Bacteriol , vol.183 , pp. 4806-4813
    • Patzer, S.I.1    Hantke, K.2
  • 34
    • 0031798662 scopus 로고    scopus 로고
    • The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli
    • Patzer, S. I., and K. Hantke. 1998. The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol. Microbiol. 28:1199-1210.
    • (1998) Mol. Microbiol , vol.28 , pp. 1199-1210
    • Patzer, S.I.1    Hantke, K.2
  • 35
    • 24944453275 scopus 로고    scopus 로고
    • Structural determinants of metal selectivity in prokaryotic metal-responsive transcriptional regulators
    • Pennella, M. A., and D. P. Giedroc. 2005. Structural determinants of metal selectivity in prokaryotic metal-responsive transcriptional regulators. Bio-metals 18:413-28.
    • (2005) Bio-metals , vol.18 , pp. 413-428
    • Pennella, M.A.1    Giedroc, D.P.2
  • 36
    • 0028118548 scopus 로고
    • Increased fertility of Corynebacterium glutamicum recipients in intergeneric matings with Escherichia coli after stress exposure
    • Schafer, A., J. Kalinowski, and A. Puhler. 1994. Increased fertility of Corynebacterium glutamicum recipients in intergeneric matings with Escherichia coli after stress exposure. Appl. Environ. Microbiol. 60:756-759.
    • (1994) Appl. Environ. Microbiol , vol.60 , pp. 756-759
    • Schafer, A.1    Kalinowski, J.2    Puhler, A.3
  • 37
    • 0036947742 scopus 로고    scopus 로고
    • 2+-dependent mechanism. J. Bacteriol. 184: 6882-6892.
    • 2+-dependent mechanism. J. Bacteriol. 184: 6882-6892.
  • 38
    • 0025809889 scopus 로고
    • Iron-dependent regulation of diphtheria toxin and siderophore expression by the cloned Corynebacterium diphtheriae repressor gene dtxR in C. diphtheriae C7 strains
    • Schmitt, M. P., and R. K. Holmes. 1991. Iron-dependent regulation of diphtheria toxin and siderophore expression by the cloned Corynebacterium diphtheriae repressor gene dtxR in C. diphtheriae C7 strains. Infect. Immun. 59:1899-1904.
    • (1991) Infect. Immun , vol.59 , pp. 1899-1904
    • Schmitt, M.P.1    Holmes, R.K.2
  • 39
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram-negative bacteria
    • Simon, R., U. Reifer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram-negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Reifer, U.2    Pühler, A.3
  • 40
    • 64149131518 scopus 로고    scopus 로고
    • Corynebacteria (including diphtheria),
    • M. Schaechter ed, 3rd ed. Elsevier, New York, NY
    • Smith, K. F., and D. M. Oram. Corynebacteria (including diphtheria), in press. In M. Schaechter (ed.), The encyclopedia of microbiology, 3rd ed. Elsevier, New York, NY.
    • The encyclopedia of microbiology
    • Smith, K.F.1    Oram, D.M.2
  • 41
    • 0026652564 scopus 로고
    • Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family
    • Sun, H. W., and B. V. Plapp. 1992. Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family. J. Mol. Evol. 34:522-535.
    • (1992) J. Mol. Evol , vol.34 , pp. 522-535
    • Sun, H.W.1    Plapp, B.V.2
  • 42
    • 0025696065 scopus 로고
    • Coordinate regulation of siderophore and diphtheria toxin production by iron in Corynebacterium diphtheriae
    • Tai, S. P., A. E. Kraffit, P. Nootheti, and R. K. Holmes. 1990. Coordinate regulation of siderophore and diphtheria toxin production by iron in Corynebacterium diphtheriae. Microb. Pathog. 9:267-273.
    • (1990) Microb. Pathog , vol.9 , pp. 267-273
    • Tai, S.P.1    Kraffit, A.E.2    Nootheti, P.3    Holmes, R.K.4
  • 43
    • 20644469022 scopus 로고    scopus 로고
    • The zinc uptake regulator Zur is essential for the full virulence of Xanthomonas campestris pv. campestris
    • Tang, D. J., X. J. Li, Y. Q. He, J. X. Feng, B. Chen, and J. L. Tang. 2005. The zinc uptake regulator Zur is essential for the full virulence of Xanthomonas campestris pv. campestris. Mol. Plant-Microbe Interact. 18:652-658.
    • (2005) Mol. Plant-Microbe Interact , vol.18 , pp. 652-658
    • Tang, D.J.1    Li, X.J.2    He, Y.Q.3    Feng, J.X.4    Chen, B.5    Tang, J.L.6
  • 44
    • 0345689425 scopus 로고    scopus 로고
    • Assembly of pili on the surface of Corynebacterium diphtheriae
    • Ton-That, H., and O. Schneewind. 2003. Assembly of pili on the surface of Corynebacterium diphtheriae. Mol. Microbiol. 50:1429-1438.
    • (2003) Mol. Microbiol , vol.50 , pp. 1429-1438
    • Ton-That, H.1    Schneewind, O.2


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