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Volumn 73, Issue 11, 2005, Pages 7406-7412

Analysis of a heme-dependent signal transduction system in Corynebactenum diphtheriae: Deletion of the chrAS genes results in heme sensitivity and diminished heme-dependent activation of the hmuO promoter

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE; HEME; HEME OXYGENASE; HEMOGLOBIN; IRON; PHOSPHOTRANSFERASE;

EID: 27744497470     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.73.11.7406-7412.2005     Document Type: Article
Times cited : (33)

References (36)
  • 2
    • 0000280261 scopus 로고
    • Phage-host relationships in nontoxigenic and toxigenic diphtheria bacilli
    • Barksdale, W. L., and A. M. Pappenheimer, Jr. 1954. Phage-host relationships in nontoxigenic and toxigenic diphtheria bacilli. J. Bacteriol. 67:220-232.
    • (1954) J. Bacteriol. , vol.67 , pp. 220-232
    • Barksdale, W.L.1    Pappenheimer Jr., A.M.2
  • 3
    • 0025300518 scopus 로고
    • Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae
    • 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 Corynebacterium diphtheriae. 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
  • 5
    • 0034128270 scopus 로고    scopus 로고
    • Corynebacterium diphtheriae genes required for acquisition of iron from hemin and hemoglobin are homologous to ABC hemin transporters
    • Drazek, E. S., C. A. Hammack, and M. P. Schmitt. 2000. Corynebacterium diphtheriae genes required for acquisition of iron from hemin and hemoglobin are homologous to ABC hemin transporters. Mol. Microbiol. 36:68-84.
    • (2000) Mol. Microbiol. , vol.36 , pp. 68-84
    • Drazek, E.S.1    Hammack, C.A.2    Schmitt, M.P.3
  • 6
    • 0031056208 scopus 로고    scopus 로고
    • The toxicities of native and modified hemoglobins
    • Everse, J., and H. Nelson. 1997. The toxicities of native and modified hemoglobins. Free Radical Biol. Med. 22:1075-1099.
    • (1997) Free Radical Biol. Med. , vol.22 , pp. 1075-1099
    • Everse, J.1    Nelson, H.2
  • 7
    • 0003116644 scopus 로고    scopus 로고
    • Iron-dependent regulators
    • A. Messerschmidt, R. Huber, T. Poulos, and K. Wieghardt (ed.). John Wiley & Sons, Ltd., Chichester, United Kingdom
    • Feese, M. D., E. Pohl, R. K. Holmes, and W. G. J. Hol. 2001. Iron-dependent regulators, p. 850-863. In A. Messerschmidt, R. Huber, T. Poulos, and K. Wieghardt (ed.), Handbook of metalloproteins. John Wiley & Sons, Ltd., Chichester, United Kingdom.
    • (2001) Handbook of Metalloproteins , pp. 850-863
    • Feese, M.D.1    Pohl, E.2    Holmes, R.K.3    Hol, W.G.J.4
  • 8
    • 15744394198 scopus 로고    scopus 로고
    • Bacterial zinc uptake and regulators
    • Hantke, K. 2005. Bacterial zinc uptake and regulators. Curr. Opin. Microbiol. 8:196-202.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 196-202
    • Hantke, K.1
  • 9
    • 0034783889 scopus 로고    scopus 로고
    • Heme utilization in Bordetella avium is regulated by RhuI, a heme responsive extracytoplasmic function sigma factor
    • Kirby, A. E., D. J. Metzger, E. R. Murphy, and T. D. Connell. 2001. Heme utilization in Bordetella avium is regulated by RhuI, a heme responsive extracytoplasmic function sigma factor. Infect. Immun. 69:6951-6961.
    • (2001) Infect. Immun. , vol.69 , pp. 6951-6961
    • Kirby, A.E.1    Metzger, D.J.2    Murphy, E.R.3    Connell, T.D.4
  • 10
    • 0344825084 scopus 로고    scopus 로고
    • Analysis of the Corynebacterium diphtheriae DtxR regulon: Identification of a putative siderophore synthesis and transport system that is similar to the Yersinia high-pathogenicity island-encoded yersiniabactin synthesis and uptake system
    • Kunkle, C. A., and M. P. Schmitt. 2003. Analysis of the Corynebacterium diphtheriae DtxR regulon: identification of a putative siderophore synthesis and transport system that is similar to the Yersinia high-pathogenicity island-encoded yersiniabactin synthesis and uptake system. J. Bacteriol. 185:6826-6840.
    • (2003) J. Bacteriol. , vol.185 , pp. 6826-6840
    • Kunkle, C.A.1    Schmitt, M.P.2
  • 11
    • 11844281592 scopus 로고    scopus 로고
    • Analysis of a DtxR-regulated iron transport and siderophore biosynthesis gene cluster in Corynebacterium diphtheriae
    • Kunkle, C. A., and M. P. Schmitt. 2005. Analysis of a DtxR-regulated iron transport and siderophore biosynthesis gene cluster in Corynebacterium diphtheriae. J. Bacteriol. 187:422-433.
    • (2005) J. Bacteriol. , vol.187 , pp. 422-433
    • Kunkle, C.A.1    Schmitt, M.P.2
  • 12
    • 0036194664 scopus 로고    scopus 로고
    • A two-component signal transduction system involved in nickel sensing in the cyanobacterium Synechocystis sp. PCC 6803
    • Lopez-Maury, L., M. Dominguez, F. J. Florencio, and J. C. Reyes. 2002. A two-component signal transduction system involved in nickel sensing in the cyanobacterium Synechocystis sp. PCC 6803. Mol. Microbiol. 43:247-256.
    • (2002) Mol. Microbiol. , vol.43 , pp. 247-256
    • Lopez-Maury, L.1    Dominguez, M.2    Florencio, F.J.3    Reyes, J.C.4
  • 14
    • 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
  • 15
    • 0033813832 scopus 로고    scopus 로고
    • Identification of a copper-responsive two-component system on the chromosome of Escherichia coli K-12
    • Munson, G. P., D. L. Lam, F. W. Outten, and T. V. O'Halloran. 2000. Identification of a copper-responsive two-component system on the chromosome of Escherichia coli K-12. J. Bacteriol. 182:5864-5871.
    • (2000) J. Bacteriol. , vol.182 , pp. 5864-5871
    • Munson, G.P.1    Lam, D.L.2    Outten, F.W.3    O'Halloran, T.V.4
  • 16
    • 0029966305 scopus 로고    scopus 로고
    • Gene repression by the ferric uptake regulator in Pseudomonas aeruginosa: Cycle selection of iron regulated genes
    • Ochsner, U. A., and M. L. Vasil. 1996. Gene repression by the ferric uptake regulator in Pseudomonas aeruginosa: cycle selection of iron regulated genes. Proc. Natl. Acad. Sci. USA 93:4409-4414.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4409-4414
    • Ochsner, U.A.1    Vasil, M.L.2
  • 18
    • 0035283403 scopus 로고    scopus 로고
    • An embarrassment of sortases - A richness of substrates?
    • Pallen, M. J., A. C. Lam, M. Antonio, and K. Dunbar. 2001. An embarrassment of sortases-a richness of substrates? Trends Microbiol. 9:97-102.
    • (2001) Trends Microbiol. , vol.9 , pp. 97-102
    • Pallen, M.J.1    Lam, A.C.2    Antonio, M.3    Dunbar, K.4
  • 19
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson, J. S., and E. C. Kofoid. 1992. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26:71-112.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 20
    • 0036718574 scopus 로고    scopus 로고
    • Identification of a DtxR-regulated operon that is essential for siderophore-dependent iron uptake in Corynebacterium diphtheriae
    • Qian, Y., J. H. Lee, and R. K. Holmes. 2002. Identification of a DtxR-regulated operon that is essential for siderophore-dependent iron uptake in Corynebacterium diphtheriae. J. Bacteriol. 184:4846-4856.
    • (2002) J. Bacteriol. , vol.184 , pp. 4846-4856
    • Qian, Y.1    Lee, J.H.2    Holmes, R.K.3
  • 21
    • 0035688874 scopus 로고    scopus 로고
    • Homologues of neisserial heme oxygenases in gram-negative bacteria: Degradation of heme by the product of the pigA gene of Pseudomonas aeruginosa
    • Ratliff, M., W. Zhu, R. Deshmukh, A. Wilks, and I. Stojilkovic. 2001. Homologues of neisserial heme oxygenases in gram-negative bacteria: degradation of heme by the product of the pigA gene of Pseudomonas aeruginosa. J. Bacteriol. 183:6394-6403.
    • (2001) J. Bacteriol. , vol.183 , pp. 6394-6403
    • Ratliff, M.1    Zhu, W.2    Deshmukh, R.3    Wilks, A.4    Stojilkovic, I.5
  • 22
    • 0038236453 scopus 로고    scopus 로고
    • Haemophore-mediated signal transduction across the bacterial cell envelope in Serratia marcescens: The inducer and the transported substrate are different molecules
    • Rossi, M.-S., A. Paquelin, J. M. Ghigo, and C. Wandersman. 2003. Haemophore-mediated signal transduction across the bacterial cell envelope in Serratia marcescens: the inducer and the transported substrate are different molecules. Mol. Microbiol. 48:1467-1480.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1467-1480
    • Rossi, M.-S.1    Paquelin, A.2    Ghigo, J.M.3    Wandersman, C.4
  • 23
    • 0031034090 scopus 로고    scopus 로고
    • Utilization of host iron sources by Corynebacterium diphtheriae: Identification of a gene whose product is homologous to eukaryotic heme oxygenaese 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 oxygenaese 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
  • 24
    • 0030732290 scopus 로고    scopus 로고
    • Transcription of the Corynebacterium diphtheriae hmuO gene is regulated by iron and heme
    • Schmitt, M. P. 1997. Transcription of the Corynebacterium diphtheriae hmuO gene is regulated by iron and heme. Infect. Immun. 65:4634-4641.
    • (1997) Infect. Immun. , vol.65 , pp. 4634-4641
    • Schmitt, M.P.1
  • 25
    • 0032833084 scopus 로고    scopus 로고
    • Identification of a two-component signal transduction system from Corynebacterium diphtheriae that activates gene expression in response to the presence of heme and hemoglobin
    • Schmitt, M. P. 1999. Identification of a two-component signal transduction system from Corynebacterium diphtheriae that activates gene expression in response to the presence of heme and hemoglobin. J. Bacteriol. 181:5330-5340.
    • (1999) J. Bacteriol. , vol.181 , pp. 5330-5340
    • Schmitt, M.P.1
  • 26
    • 27744535908 scopus 로고    scopus 로고
    • J. H. Crosa, A. R. Mey, and S. M. Payne (ed.), Iron transport in bacteria. ASM Press, Washington, D.C.
    • Schmitt, M. P. 2004. Corynebacterium diphtheriae p. 344-359. In J. H. Crosa, A. R. Mey, and S. M. Payne (ed.), Iron transport in bacteria. ASM Press, Washington, D.C.
    • (2004) Corynebacterium Diphtheriae , pp. 344-359
    • Schmitt, M.P.1
  • 27
    • 0035139975 scopus 로고    scopus 로고
    • Construction and consequences of directed mutations affecting the hemin receptor in pathogenic Corynebacterium species
    • Schmitt, M. P., and E. S. Drazek. 2001. Construction and consequences of directed mutations affecting the hemin receptor in pathogenic Corynebacterium species. J. Bacteriol. 183:1476-1481.
    • (2001) J. Bacteriol. , vol.183 , pp. 1476-1481
    • Schmitt, M.P.1    Drazek, E.S.2
  • 28
    • 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
  • 29
    • 0025999830 scopus 로고
    • Characterization of a defective diphtheria toxin repressor (dtxR) allele and analysis of dtxR transcription in wildtype 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 wildtype 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
  • 30
    • 0028086537 scopus 로고
    • Transport of haemin across the cytoplasmic membrane through a haemin-specific periplasmic binding-protein-dependent transport system in Yersinia enterocolitica
    • Stojiljkovic, I., and K. Hantke. 1994. Transport of haemin across the cytoplasmic membrane through a haemin-specific periplasmic binding-protein- dependent transport system in Yersinia enterocolitica. Mol. Microbiol. 13:719-732.
    • (1994) Mol. Microbiol. , vol.13 , pp. 719-732
    • Stojiljkovic, I.1    Hantke, K.2
  • 31
    • 0036263269 scopus 로고    scopus 로고
    • Processing of heme and heme-containing proteins by bacteria
    • Stojiljkovic, I., and D. Perkins-Balding. 2002. Processing of heme and heme-containing proteins by bacteria. DNA Cell Biol. 21:281-295.
    • (2002) DNA Cell Biol. , vol.21 , pp. 281-295
    • Stojiljkovic, I.1    Perkins-Balding, D.2
  • 32
    • 0037309146 scopus 로고    scopus 로고
    • Heme-responsive transcriptional activation of Bordetella bhu genes
    • Vanderpool, C. K., and S. K. Armstrong. 2003. Heme-responsive transcriptional activation of Bordetella bhu genes. J. Bacteriol. 185:909-917.
    • (2003) J. Bacteriol. , vol.185 , pp. 909-917
    • Vanderpool, C.K.1    Armstrong, S.K.2
  • 33
    • 0035264043 scopus 로고    scopus 로고
    • The ShuS protein of Shigella dysenteriae is a heme-sequestering protein that also binds DNA
    • Wilks, A. 2001. The ShuS protein of Shigella dysenteriae is a heme-sequestering protein that also binds DNA. Arch. Biochem. Biophys. 387:137-142.
    • (2001) Arch. Biochem. Biophys. , vol.387 , pp. 137-142
    • Wilks, A.1
  • 34
    • 0036672234 scopus 로고    scopus 로고
    • Heme oxygenase: Evolution, structure, and mechanism
    • Wilks, A. 2002. Heme oxygenase: evolution, structure, and mechanism. Antioxid. Redox Signal. 4:603-614.
    • (2002) Antioxid. Redox Signal. , vol.4 , pp. 603-614
    • Wilks, A.1
  • 35
    • 0031984521 scopus 로고    scopus 로고
    • Expression and characterization of a heme oxygenase (HmuO) from Corynebacterium diphtheriae
    • Wilks, A., and M. P. Schmitt. 1998. Expression and characterization of a heme oxygenase (HmuO) from Corynebacterium diphtheriae. J. Biol. Chem. 273:837-841.
    • (1998) J. Biol. Chem. , vol.273 , pp. 837-841
    • Wilks, A.1    Schmitt, M.P.2
  • 36
    • 0033988059 scopus 로고    scopus 로고
    • Use of heme compounds as iron sources by pathogenic Neisseria requires the product of the hemO gene
    • Zhu, W., D. J. Hunt, A. R. Richardson, and I. Stojilkovic. 2000. Use of heme compounds as iron sources by pathogenic Neisseria requires the product of the hemO gene. J. Bacteriol. 182:439-447.
    • (2000) J. Bacteriol. , vol.182 , pp. 439-447
    • Zhu, W.1    Hunt, D.J.2    Richardson, A.R.3    Stojilkovic, I.4


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