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Volumn 65, Issue 11, 1997, Pages 4634-4641

Transcription of the Corynebacterium diphtheriae hmuO gene is regulated by iron and heme

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; HEME; HEME OXYGENASE; HEMOGLOBIN; IRON; MESSENGER RNA; TRANSFERRIN;

EID: 0030732290     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.65.11.4634-4641.1997     Document Type: Article
Times cited : (89)

References (56)
  • 1
    • 0025300518 scopus 로고
    • Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebactcriutn diphtheria
    • Boyd, J. M., O. N. Manish, and J. R. Murphy. 1990. Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebactcriutn diphtheria. Proc. Natl. Acad. Sci. USA 87:5968-5972.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5968-5972
    • Boyd, J.M.1    Manish, O.N.2    Murphy, J.R.3
  • 2
    • 46549099023 scopus 로고
    • The unusual features of the iron transport systems of Escherichia coli
    • Braun, V. 1985. The unusual features of the iron transport systems of Escherichia coli. Trends Biochcm. Sci. 10:76-77.
    • (1985) Trends Biochcm. Sci. , vol.10 , pp. 76-77
    • Braun, V.1
  • 3
    • 0029044848 scopus 로고
    • A gene cluster involved in the utilization of both free heme and heme:hemopexin by Haemophilus influenzae type b
    • Cope, L. D., R. Yogev, U. Muller-Eberhard, and E. J. Hansen. 1995. A gene cluster involved in the utilization of both free heme and heme:hemopexin by Haemophilus influenzae type b. J. Bacteriol. 177:2644-2653.
    • (1995) J. Bacteriol. , vol.177 , pp. 2644-2653
    • Cope, L.D.1    Yogev, R.2    Muller-Eberhard, U.3    Hansen, E.J.4
  • 4
    • 0020539684 scopus 로고
    • Regulation of toxinogenesis in Corynebacterium diphthenae: Mutations in the bacterial genome that alter the effects of iron on toxin production
    • Cryz, S. J., Jr., L. M. Russell, and R. K. Holmes. 1983. Regulation of toxinogenesis in Corynebacterium diphthenae: mutations in the bacterial genome that alter the effects of iron on toxin production. J. Bacteriol. 154: 245-252.
    • (1983) J. Bacteriol. , vol.154 , pp. 245-252
    • Cryz Jr., S.J.1    Russell, L.M.2    Holmes, R.K.3
  • 6
    • 0029846868 scopus 로고    scopus 로고
    • Acquisition of iron from host proteins by the group A streptococcus
    • Eichenbaum, Z., K. Muller, S. A. Morse, and J. R. Scott. 1996. Acquisition of iron from host proteins by the group A streptococcus. Infect. Immun. 64:5428-5429.
    • (1996) Infect. Immun. , vol.64 , pp. 5428-5429
    • Eichenbaum, Z.1    Muller, K.2    Morse, S.A.3    Scott, J.R.4
  • 7
    • 0028905674 scopus 로고
    • Identification and purification of a conserved heme-regulated hemoglobin-binding outer membrane protein from Haemophilus ducreyi
    • Elkins, C. 1995. Identification and purification of a conserved heme-regulated hemoglobin-binding outer membrane protein from Haemophilus ducreyi. Infect. Immun. 63:1241-1245.
    • (1995) Infect. Immun. , vol.63 , pp. 1241-1245
    • Elkins, C.1
  • 8
    • 0025370615 scopus 로고
    • Construction of broad-hostrange plasmid vectors for easily visible selection and analysis of promoters
    • Farinha, M. A., and A. M. Kropinski. 1990. Construction of broad-hostrange plasmid vectors for easily visible selection and analysis of promoters. J. Bacteriol. 172:3496-3499.
    • (1990) J. Bacteriol. , vol.172 , pp. 3496-3499
    • Farinha, M.A.1    Kropinski, A.M.2
  • 9
    • 0022258046 scopus 로고
    • Uptake of iron from hemoglobin and the haptoglobin-hemoglobin complex by hemolytic bacteria
    • Francis, R. T., Jr., J. W. Booth, and R. R. Becker. 1985. Uptake of iron from hemoglobin and the haptoglobin-hemoglobin complex by hemolytic bacteria. Int. J. Biochem. 17:767-773.
    • (1985) Int. J. Biochem. , vol.17 , pp. 767-773
    • Francis Jr., R.T.1    Booth, J.W.2    Becker, R.R.3
  • 11
    • 0028360093 scopus 로고    scopus 로고
    • Binding and accumulation of hemin in Porphyromonas gingivalis arc induced by hemin
    • Genco, C. A., B. M. Odusanya, and G. Brown. Binding and accumulation of hemin in Porphyromonas gingivalis arc induced by hemin. Infect. Immun. 62:2885-2892.
    • Infect. Immun. , vol.62 , pp. 2885-2892
    • Genco, C.A.1    Odusanya, B.M.2    Brown, G.3
  • 12
    • 0028858577 scopus 로고
    • Cloning and sequence analysis of the Corynebacterium diphtheriae dtxR homologue from Streptomyces lividans and S. pilosus encoding a putative iron repressor protein
    • Gunter-Seeboth, K., and T. Schupp. 1995. Cloning and sequence analysis of the Corynebacterium diphtheriae dtxR homologue from Streptomyces lividans and S. pilosus encoding a putative iron repressor protein. Gene 166:117-119.
    • (1995) Gene , vol.166 , pp. 117-119
    • Gunter-Seeboth, K.1    Schupp, T.2
  • 13
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 14
    • 0021699534 scopus 로고
    • Cloning of the repressor protein gene of iron-regulated systems in Escherichia coli K-12
    • Hantke, K. 1984. Cloning of the repressor protein gene of iron-regulated systems in Escherichia coli K-12. Mol. Gen. Genet. 197:337-341.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 337-341
    • Hantke, K.1
  • 15
    • 0023650609 scopus 로고
    • Analysis of E. coli promoter sequences
    • Harley, C. B., and R. P. Reynolds. 1987. Analysis of E. coli promoter sequences. Nucleic Acids Res. 15:2343-2361.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 2343-2361
    • Harley, C.B.1    Reynolds, R.P.2
  • 16
    • 0000173524 scopus 로고
    • Electrotransformation of Brevibacterium lactofermentum and Corynebacterium glutamicum: Growth in Tween 80 increases transformation frequencies
    • Haynes, J. A., and M. L. Britz. 1989. Electrotransformation of Brevibacterium lactofermentum and Corynebacterium glutamicum: growth in Tween 80 increases transformation frequencies. FEMS Microbiol. Lett. 61:329-334.
    • (1989) FEMS Microbiol. Lett. , vol.61 , pp. 329-334
    • Haynes, J.A.1    Britz, M.L.2
  • 17
    • 0028338619 scopus 로고
    • Characterization of the Vibrio cholerae outer membrane heme transport protein HutA: Sequence of the gene, regulation of expression, and homology to the family of TonB-dependent proteins
    • Henderson, D. P., and S. M. Payne. 1994. Characterization of the Vibrio cholerae outer membrane heme transport protein HutA: sequence of the gene, regulation of expression, and homology to the family of TonB-dependent proteins. J. Bacteriol. 176:3269-3277.
    • (1994) J. Bacteriol. , vol.176 , pp. 3269-3277
    • Henderson, D.P.1    Payne, S.M.2
  • 18
    • 0014530734 scopus 로고
    • + and tox bacteriophages of Corynebacterium diphtheriae
    • + and tox bacteriophages of Corynebacterium diphtheriae. J. Virol. 3:586-598.
    • (1969) J. Virol. , vol.3 , pp. 586-598
    • Holmes, R.K.1    Barksdale, L.2
  • 19
    • 0029955633 scopus 로고    scopus 로고
    • The hmu locus of Yersinia pestis is essential for utilization of free hemin and heme-protein complexes as iron sources
    • Hornung, J. M., H. A. Jones, and R. D. Perry. 1996 The hmu locus of Yersinia pestis is essential for utilization of free hemin and heme-protein complexes as iron sources. Mol. Microbiol. 20:725-739.
    • (1996) Mol. Microbiol. , vol.20 , pp. 725-739
    • Hornung, J.M.1    Jones, H.A.2    Perry, R.D.3
  • 20
    • 0030056385 scopus 로고    scopus 로고
    • Cloning of a DNA fragment encoding a heme-repressible hemoglobin-binding outer membrane protein from Haemophilus influenzae
    • Jin, H., Z. Ren, J. M. Pozsgay, C. Elkins, P. W. Whitby, D. J. Morton, and T. L. Stull. 1996. Cloning of a DNA fragment encoding a heme-repressible hemoglobin-binding outer membrane protein from Haemophilus influenzae. Infect. Immun. 64:3134-3141.
    • (1996) Infect. Immun. , vol.64 , pp. 3134-3141
    • Jin, H.1    Ren, Z.2    Pozsgay, J.M.3    Elkins, C.4    Whitby, P.W.5    Morton, D.J.6    Stull, T.L.7
  • 21
    • 0017642895 scopus 로고
    • Isolation from Corynebacterium diphthenae C7(β) of bacterial mutants that produce toxin in medium with excess iron
    • Kanei, C., T. Uchida, and M. Yoneda. 1977. Isolation from Corynebacterium diphthenae C7(β) of bacterial mutants that produce toxin in medium with excess iron. Infect. Immun 18:203-209.
    • (1977) Infect. Immun , vol.18 , pp. 203-209
    • Kanei, C.1    Uchida, T.2    Yoneda, M.3
  • 22
    • 0030904023 scopus 로고    scopus 로고
    • Isolation and characterization of a hemin-regulated gene. hemR. from Porphyromonas gingiva tis
    • Karunakaran T., T. Maden, and H. Kuramitsu. 1997 Isolation and characterization of a hemin-regulated gene. hemR. from Porphyromonas gingiva tis. J. Bacteriol. 179:1898-1908.
    • (1997) J. Bacteriol. , vol.179 , pp. 1898-1908
    • Karunakaran, T.1    Maden, T.2    Kuramitsu, H.3
  • 23
    • 0029560596 scopus 로고
    • Quelling the red menace: Heme capture by bacteria
    • Lee, C. B. 1995. Quelling the red menace: heme capture by bacteria. Mol. Microbiol. 18:383-390.
    • (1995) Mol. Microbiol. , vol.18 , pp. 383-390
    • Lee, C.B.1
  • 25
    • 0018846636 scopus 로고
    • Sequencing end-labeled DNA with base-specific chemical cleavages
    • Maxam, A., and W. Gilbert. 1980. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 65:499-560.
    • (1980) Methods Enzymol. , vol.65 , pp. 499-560
    • Maxam, A.1    Gilbert, W.2
  • 26
  • 27
    • 0028070009 scopus 로고
    • The role of iron-binding proteins in the survival of pathogenic bacteria
    • Mietzner, T. A., and S. A. Morse. 1994. The role of iron-binding proteins in the survival of pathogenic bacteria. Annu. Rev. Nutr. 14:471-493.
    • (1994) Annu. Rev. Nutr. , vol.14 , pp. 471-493
    • Mietzner, T.A.1    Morse, S.A.2
  • 29
    • 0029019563 scopus 로고
    • Genetics and regulation of heme iron transport in Shigella dysenteriae and detection of an analogous system in Escherichia coli O157:H7
    • Mills, M., and S. M. Payne. 1995. Genetics and regulation of heme iron transport in Shigella dysenteriae and detection of an analogous system in Escherichia coli O157:H7. J. Bacteriol. 177:3004-3009.
    • (1995) J. Bacteriol. , vol.177 , pp. 3004-3009
    • Mills, M.1    Payne, S.M.2
  • 30
    • 0028133393 scopus 로고
    • Staphylococci express a receptor for human transferrin: Identification of a 42-kilodalton cell wall transferrin-binding protein
    • Modun, B., D. Kendall, and P. Williams. 1994. Staphylococci express a receptor for human transferrin: identification of a 42-kilodalton cell wall transferrin-binding protein. Infect. Immun. 62:3850-3858.
    • (1994) Infect. Immun. , vol.62 , pp. 3850-3858
    • Modun, B.1    Kendall, D.2    Williams, P.3
  • 31
    • 0027519573 scopus 로고
    • Expression of the Haemoplulus influenzae transferrin receptor is repressible by hemin but not elemental iron alone
    • Morton, D. J., J. M. Musser, and T. L. Stull. 1993 Expression of the Haemoplulus influenzae transferrin receptor is repressible by hemin but not elemental iron alone. Infect. Immun. 61:4033-4037.
    • (1993) Infect. Immun. , vol.61 , pp. 4033-4037
    • Morton, D.J.1    Musser, J.M.2    Stull, T.L.3
  • 32
    • 0028855065 scopus 로고
    • Molecular cloning. DNA sequence analysis, and characterization of the Corynebacterium diphtheriae dtxR homolog from Brevibactenum lactofermentum
    • Oguiza, J. A., X. Tao, A. T. Marcos, and J. R. Murphy. 1995. Molecular cloning. DNA sequence analysis, and characterization of the Corynebacterium diphtheriae dtxR homolog from Brevibactenum lactofermentum. J. Bacteriol. 177:465-467.
    • (1995) J. Bacteriol. , vol.177 , pp. 465-467
    • Oguiza, J.A.1    Tao, X.2    Marcos, A.T.3    Murphy, J.R.4
  • 35
    • 0015596536 scopus 로고
    • Iron-binding catechols and virulence in Escherichia coli
    • Rogers, H. J. 1973. Iron-binding catechols and virulence in Escherichia coli. Infect. Immun. 7:445-458.
    • (1973) Infect. Immun. , vol.7 , pp. 445-458
    • Rogers, H.J.1
  • 36
    • 0021152606 scopus 로고
    • Genetic and biochemical evidence for a siderophore-dependent iron transport system in Corynebacterium diphtheriae
    • Russell, L. M., S. J. Cryz, Jr., and R. K. Holmes. 1984. Genetic and biochemical evidence for a siderophore-dependent iron transport system in Corynebacterium diphtheriae. Infect. Immun. 45:143-149.
    • (1984) Infect. Immun. , vol.45 , pp. 143-149
    • Russell, L.M.1    Cryz Jr., S.J.2    Holmes, R.K.3
  • 39
    • 0031034090 scopus 로고    scopus 로고
    • Utilization of host iron sources by Corynebacterium diphtheriae: Identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin
    • Schmitt, M. P. 1997. Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin. J. Bacteriol. 179:838-845.
    • (1997) J. Bacteriol. , vol.179 , pp. 838-845
    • Schmitt, M.P.1
  • 40
    • 1842308476 scopus 로고    scopus 로고
    • Unpublished data
    • a.Schmitt, M. P. Unpublished data.
    • Schmitt, M.P.1
  • 41
    • 0025809889 scopus 로고
    • Iron-dependent regulation of diphtheria toxin and siderophore expression by the cloned Corynebacterium diphteriae 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 diphteriae 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
  • 42
    • 0025999830 scopus 로고
    • Characterization of a defective diphtheria toxin repressor (dtxR) allele and analysis of dtxR transcription in wild-type and mutant strains of Corynebacterium diphtheriae
    • Schmitt, M. P., and R. K. Holmes. 1991. Characterization of a defective diphtheria toxin repressor (dtxR) allele and analysis of dtxR transcription in wild-type and mutant strains of Corynebacterium diphtheriae. Infect. Immun. 59:3903-3908.
    • (1991) Infect. Immun. , vol.59 , pp. 3903-3908
    • Schmitt, M.P.1    Holmes, R.K.2
  • 43
    • 0027210121 scopus 로고
    • Analysis of diphtheria toxin repressor-operator interactions and characterization of a mutant repressor with decreased binding activity for divalent metals
    • Schmitt, M. P., and R. K. Holmes. 1993. Analysis of diphtheria toxin repressor-operator interactions and characterization of a mutant repressor with decreased binding activity for divalent metals. Mol. Microbiol. 9:173-181.
    • (1993) Mol. Microbiol. , vol.9 , pp. 173-181
    • Schmitt, M.P.1    Holmes, R.K.2
  • 44
    • 0028006022 scopus 로고
    • Cloning, sequence, and footprint analysis of two promoter/operators from Corynebacterium diphtheriae that arc regulated by the diphtheria toxin repressor (DtxR) and iron
    • Schmitt, M. P., and R. K. Holmes. 1994. Cloning, sequence, and footprint analysis of two promoter/operators from Corynebacterium diphtheriae that arc regulated by the diphtheria toxin repressor (DtxR) and iron. J. Bacteriol. 176:1141-1149.
    • (1994) J. Bacteriol. , vol.176 , pp. 1141-1149
    • Schmitt, M.P.1    Holmes, R.K.2
  • 45
    • 0028822995 scopus 로고
    • Characterization of an iron-dependent regulatory protein (IdeR) of Mycobacterium tuberculosis as a functional homolog of the diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae
    • Schmitt, M. P., M. Predich, L. Doukhan, I. Smith, and R. K. Holmes. 1995. Characterization of an iron-dependent regulatory protein (IdeR) of Mycobacterium tuberculosis as a functional homolog of the diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae. Infect. Immun. 63:4284-4289.
    • (1995) Infect. Immun. , vol.63 , pp. 4284-4289
    • Schmitt, M.P.1    Predich, M.2    Doukhan, L.3    Smith, I.4    Holmes, R.K.5
  • 46
    • 0026666051 scopus 로고
    • Purification and characterization of the diphtheria toxin repressor
    • Schmitt, M. P., E. M. Twiddy, and R. K. Holmes. 1992. Purification and characterization of the diphtheria toxin repressor. Proc. Natl. Acad. Sci. USA 89:7576-7580.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7576-7580
    • Schmitt, M.P.1    Twiddy, E.M.2    Holmes, R.K.3
  • 47
    • 0025157752 scopus 로고
    • Localization of an origin of replication in Corynebacterium diphtheriae broad host range plasmid pNG2 that also functions in Escherichia coli
    • Serwold-Davis, T. M., N. B. Groman, and C. C. Kao. 1990. Localization of an origin of replication in Corynebacterium diphtheriae broad host range plasmid pNG2 that also functions in Escherichia coli. FEMS Microbiol. Lett. 66:119-124.
    • (1990) FEMS Microbiol. Lett. , vol.66 , pp. 119-124
    • Serwold-Davis, T.M.1    Groman, N.B.2    Kao, C.C.3
  • 48
    • 0026445951 scopus 로고
    • Hemin uptake system of Yersinia enterocolitica: Similarities with other TonB-dependent systems in gram negative bacteria
    • Stoljiljkovic I., and K. Hantke. 1992. Hemin uptake system of Yersinia enterocolitica: similarities with other TonB-dependent systems in gram negative bacteria. EMBO J. 11:4359-4367.
    • (1992) EMBO J. , vol.11 , pp. 4359-4367
    • Stoljiljkovic, I.1    Hantke, K.2
  • 49
    • 0028086537 scopus 로고
    • Transport of hemin across the cytoplasmic membrane through a hemin-specific periplasmic binding-protein-dependent transport system in Yersinia enterocolitica
    • Stoljiljkovic I., and K. Hantke. 1994. Transport of hemin across the cytoplasmic membrane through a hemin-specific periplasmic binding-protein-dependent transport system in Yersinia enterocolitica. Mol Microbiol. 13: -719-732.
    • (1994) Mol Microbiol. , vol.13 , pp. 719-732
    • Stoljiljkovic, I.1    Hantke, K.2
  • 50
    • 0025696065 scopus 로고
    • Coordinate regulation of siderophore and diphtheria toxin production by iron in Coryne-bacterium diphtheriae
    • Tai, S.-P., A. E. Krafft, P. Nootheti, and R. K. Holmes. 1990. Coordinate regulation of siderophore and diphtheria toxin production by iron in Coryne-bacterium diphtheriae. Microb. Pathog. 9:267-273.
    • (1990) Microb. Pathog. , vol.9 , pp. 267-273
    • Tai, S.-P.1    Krafft, A.E.2    Nootheti, P.3    Holmes, R.K.4
  • 51
    • 0031038360 scopus 로고    scopus 로고
    • Characterization of hemin binding activity of Streptococcus pneumoniae
    • Tai, S.-P., T. Wang, and C.-J. Lee. 1997. Characterization of hemin binding activity of Streptococcus pneumoniae. Infect. Immun. 65:1083-1087.
    • (1997) Infect. Immun. , vol.65 , pp. 1083-1087
    • Tai, S.-P.1    Wang, T.2    Lee, C.-J.3
  • 52
    • 0028149973 scopus 로고
    • Iron, DtxR and the regulation of diphtheria toxin expression
    • Tao, X., S. Nikolaus, H. Zeng, D. Ringe, and J. R. Murphy. 1994. Iron, DtxR and the regulation of diphtheria toxin expression. Mol. Microbiol. 14:191-197.
    • (1994) Mol. Microbiol. , vol.14 , pp. 191-197
    • Tao, X.1    Nikolaus, S.2    Zeng, H.3    Ringe, D.4    Murphy, J.R.5
  • 53
    • 0024574001 scopus 로고
    • Oxidative effects of heme and porphyrins on proteins and lipids
    • Vincent, S. H. 1989. Oxidative effects of heme and porphyrins on proteins and lipids. Semin. Hematol. 26:105-113.
    • (1989) Semin. Hematol. , vol.26 , pp. 105-113
    • Vincent, S.H.1
  • 54
    • 0018102319 scopus 로고
    • Iron and infection
    • Weinberg, E. D. 1978. Iron and infection. Microbiol. Rev. 42:45-66.
    • (1978) Microbiol. Rev. , vol.42 , pp. 45-66
    • Weinberg, E.D.1
  • 55
    • 0018710740 scopus 로고
    • Novel iron uptake system specified by ColV plasmids: An important component in the virulence of invasive strains of Escherichia coli
    • Williams, P. 1979. Novel iron uptake system specified by ColV plasmids: an important component in the virulence of invasive strains of Escherichia coli. Infect. Immun. 26:925-932.
    • (1979) Infect. Immun. , vol.26 , pp. 925-932
    • Williams, P.1


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