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Volumn 67, Issue 4, 1999, Pages 1806-1811

Anion-coordinating residues at binding site 1 are essential for the biological activity of the diphtheria toxin repressor

Author keywords

[No Author keywords available]

Indexed keywords

DIPHTHERIA TOXIN; REPRESSOR PROTEIN;

EID: 0033051018     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.67.4.1806-1811.1999     Document Type: Article
Times cited : (24)

References (40)
  • 1
    • 0016381709 scopus 로고
    • Persisting bacteriophage infections, lysogeny, and phage conversion
    • Barksdale, L., and S. B. Arden. 1974. Persisting bacteriophage infections, lysogeny, and phage conversion. Annu. Rev. Microbiol. 28:265-299.
    • (1974) Annu. Rev. Microbiol. , vol.28 , pp. 265-299
    • Barksdale, L.1    Arden, S.B.2
  • 2
    • 0025300518 scopus 로고
    • Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from corynebacterium diphtheriae
    • Boyd, J., M. N. Oza, 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.1    Oza, M.N.2    Murphy, J.R.3
  • 3
    • 0029964556 scopus 로고    scopus 로고
    • Identification of the primary metal ion-activation sites of the diphtheria tox represser by X-ray crystallography and site-directed mutational analysis
    • Ding, X., H. Zeng, N. Schiering, D. Ringe, and J. R. Murphy. 1996. Identification of the primary metal ion-activation sites of the diphtheria tox represser by X-ray crystallography and site-directed mutational analysis. Nat. Struct. Biol. 3:382-387.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 382-387
    • Ding, X.1    Zeng, H.2    Schiering, N.3    Ringe, D.4    Murphy, J.R.5
  • 5
    • 72949125244 scopus 로고
    • The uptake of iron by Corynebacterium diphtheriae growing in submerged medium
    • Edwards, D. C., and P. A. Seamer. 1960. The uptake of iron by Corynebacterium diphtheriae growing in submerged medium. J. Gen. Microbiol. 22:715-721.
    • (1960) J. Gen. Microbiol. , vol.22 , pp. 715-721
    • Edwards, D.C.1    Seamer, P.A.2
  • 6
    • 0001396162 scopus 로고
    • Studies on the virulence of bacteriophage-infected strains of Corynebacterium diphtheriae
    • Freeman, V. J. 1951. Studies on the virulence of bacteriophage-infected strains of Corynebacterium diphtheriae. J. Bacteriol. 61:675-688.
    • (1951) J. Bacteriol , vol.61 , pp. 675-688
    • Freeman, V.J.1
  • 7
    • 0345366401 scopus 로고
    • Further observations on the change to virulence of bacteriophage-infected avirulent strains of Corynebacterium diphtheriae
    • Freeman, V. J., and I. U. Morse. 1952. Further observations on the change to virulence of bacteriophage-infected avirulent strains of Corynebacterium diphtheriae. J. Bacteriol. 63:407-414.
    • (1952) J. Bacteriol. , vol.63 , pp. 407-414
    • Freeman, V.J.1    Morse, I.U.2
  • 8
    • 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
  • 10
    • 0030879821 scopus 로고    scopus 로고
    • Identification and characterization of three new promoter/operators from Corynebacterium diphtheriae that are regulated by the diphtheria toxin repressor (DtxR) and iron
    • Lee, J. H., T. Wang, K. Ault, J. Liu, M. P. Schmitt, and R. K. Holmes. 1997. Identification and characterization of three new promoter/operators from Corynebacterium diphtheriae that are regulated by the diphtheria toxin repressor (DtxR) and iron. Infect. Immun. 65:4273-4280.
    • (1997) Infect. Immun. , vol.65 , pp. 4273-4280
    • Lee, J.H.1    Wang, T.2    Ault, K.3    Liu, J.4    Schmitt, M.P.5    Holmes, R.K.6
  • 11
    • 0345366400 scopus 로고
    • The relation of copper and iron to the production of toxin and enzyme action
    • Locke, A., and E. R. Main. 1931. The relation of copper and iron to the production of toxin and enzyme action. J. Infect. Dis. 48:419-435.
    • (1931) J. Infect. Dis. , vol.48 , pp. 419-435
    • Locke, A.1    Main, E.R.2
  • 12
  • 13
    • 0002598131 scopus 로고
    • Production of diphtheria toxin of high potency (100 LF) on a reproducible medium
    • Mueller, J. H., and P. A. Miller. 1941. Production of diphtheria toxin of high potency (100 LF) on a reproducible medium. J. Immunol. 40:21-32.
    • (1941) J. Immunol. , vol.40 , pp. 21-32
    • Mueller, J.H.1    Miller, P.A.2
  • 14
    • 0028855065 scopus 로고
    • Molecular cloning, DNA sequence analysis, and characterization of the Corynebacterium diphtheriae dtxR homolog from Brevibacterium lactofermentum
    • Oguiza, J. A., X. Tao, A. T. Marcos, J. F. Martín, and J. R. Murphy. 1995. Molecular cloning, DNA sequence analysis, and characterization of the Corynebacterium diphtheriae dtxR homolog from Brevibacterium 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    Martín, J.F.4    Murphy, J.R.5
  • 16
    • 0001398811 scopus 로고
    • Studies in diphtheria toxin production. I. The effect of iron and copper
    • Pappenheimer, A. M., Jr., and S. J. Johnson. 1936. Studies in diphtheria toxin production. I. The effect of iron and copper. Br. J. Exp. Pathol. 17:335-341.
    • (1936) Br. J. Exp. Pathol. , vol.17 , pp. 335-341
    • Pappenheimer A.M., Jr.1    Johnson, S.J.2
  • 17
    • 0030902083 scopus 로고    scopus 로고
    • Comparison of high-resolution structures of the diphtheria toxin repressor in complex with cobalt and zinc at the cation-anion binding site
    • Pohl, E., X. Qiu, L. M. Must, R. K. Holmes, and W. G. J. Hol. 1997. Comparison of high-resolution structures of the diphtheria toxin repressor in complex with cobalt and zinc at the cation-anion binding site. Protein Sci. 6: 1114-1118.
    • (1997) Protein Sci. , vol.6 , pp. 1114-1118
    • Pohl, E.1    Qiu, X.2    Must, L.M.3    Holmes, R.K.4    Hol, W.G.J.5
  • 18
    • 0032575642 scopus 로고    scopus 로고
    • Motion of the DNA-binding domain with respect to the core of the diphtheria toxin repressor in the crystal structures of apo- and holo-DtxR
    • Pohl, E., R. K. Holmes, and W. G. J. Hol. 1998. Motion of the DNA-binding domain with respect to the core of the diphtheria toxin repressor in the crystal structures of apo- and holo-DtxR. J. Biol. Chem. 273:22420-22427.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22420-22427
    • Pohl, E.1    Holmes, R.K.2    Hol, W.G.J.3
  • 19
    • 0028993911 scopus 로고
    • Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors
    • Qiu, X., C. L. M. J. Verlinde, S. Zhang, M. P. Schmitt, R. K. Holmes, and W. G. J. Hol. 1995. Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors. Structure 3:87-100.
    • (1995) Structure , vol.3 , pp. 87-100
    • Qiu, X.1    Verlinde, C.L.M.J.2    Zhang, S.3    Schmitt, M.P.4    Holmes, R.K.5    Hol, W.G.J.6
  • 20
    • 0029739483 scopus 로고    scopus 로고
    • High-resolution structure of the diphtheria toxin repressor complexed with cobalt and manganese reveals an SH3-like third domain and suggests a possible role of phosphate as co-corepressor
    • Qiu, X., E. Pohl, R. K. Holmes, and W. G. J. Hol. 1996. High-resolution structure of the diphtheria toxin repressor complexed with cobalt and manganese reveals an SH3-like third domain and suggests a possible role of phosphate as co-corepressor. Biochemistry 35:12292-12302.
    • (1996) Biochemistry , vol.35 , pp. 12292-12302
    • Qiu, X.1    Pohl, E.2    Holmes, R.K.3    Hol, W.G.J.4
  • 23
    • 0028826149 scopus 로고
    • Structures of the apo- and the metal ion-activated forms of the diphtheria tax repressor from Corynebacterium diphtheriae
    • Schiering, N., X. Tao, H. Zeng, J. R. Murphy, G. A. Petsko, and D. Ringe. 1995. Structures of the apo- and the metal ion-activated forms of the diphtheria tax repressor from Corynebacterium diphtheriae. Proc. Natl. Acad. Sci. USA 92:9843-9850.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9843-9850
    • Schiering, N.1    Tao, X.2    Zeng, H.3    Murphy, J.R.4    Petsko, G.A.5    Ringe, D.6
  • 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
    • 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
  • 26
    • 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
  • 27
    • 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
  • 28
    • 0028006022 scopus 로고
    • Cloning, sequence, and footprint analysis of two promoter/operators from Corynebacterium diphtheriae that are 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 are 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
  • 29
    • 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
  • 30
    • 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
  • 31
    • 0030827610 scopus 로고    scopus 로고
    • Characterization of lipoprotein IRPl from Corynebacterium diphtheriae, which is regulated by the diphtheria toxin repressor (DtxR) and iron
    • Schmitt, M. P., B. G. Talley, and R. K. Holmes. 1997. Characterization of lipoprotein IRPl from Corynebacterium diphtheriae, which is regulated by the diphtheria toxin repressor (DtxR) and iron. Infect. Immun. 65:5364-5367.
    • (1997) Infect. Immun. , vol.65 , pp. 5364-5367
    • Schmitt, M.P.1    Talley, B.G.2    Holmes, R.K.3
  • 32
    • 0025696065 scopus 로고
    • Coordinate regulation of siderophote and diphtheria toxin production by iron in Corynebacterium diphtheriae
    • Tai, S.-P., A. E. Kraft, P. Nootheti, and R. K. Holmes. 1990. Coordinate regulation of siderophote 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    Kraft, A.E.2    Nootheti, P.3    Holmes, R.K.4
  • 33
    • 0026800843 scopus 로고
    • Binding of the metalloregulatory protein DtxR to the diphtheria tax operator requires a divalent heavy metal ion and protects the palindromic sequence from DNase I digestion
    • Tao, X., and J. R. Murphy. 1992. Binding of the metalloregulatory protein DtxR to the diphtheria tax operator requires a divalent heavy metal ion and protects the palindromic sequence from DNase I digestion. J. Biol. Chem. 267:21761-21764.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21761-21764
    • Tao, X.1    Murphy, J.R.2
  • 34
    • 0027294003 scopus 로고
    • Cysteine-102 is positioned in the metal binding activation site of the Corynebacterium diphtheriae regulatory element DtxR
    • Tao, X., and J. R. Murphy. 1993. Cysteine-102 is positioned in the metal binding activation site of the Corynebacterium diphtheriae regulatory element DtxR. Proc. Natl. Acad. Sci. USA 90:8524-8528.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8524-8528
    • Tao, X.1    Murphy, J.R.2
  • 35
    • 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
  • 36
    • 0029093731 scopus 로고
    • Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers
    • Tao, X., H. Zeng, and J. R. Murphy. 1995. Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers. Proc. Natl. Acad. Sci. USA 92:6803-6807.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6803-6807
    • Tao, X.1    Zeng, H.2    Murphy, J.R.3
  • 37
    • 0015124068 scopus 로고
    • Mutation in the structural gene for diphtheria toxin carried by temperate phage β
    • Uchida, T., D. M. Gill, and A. M. Pappenheimer, Jr. 1971. Mutation in the structural gene for diphtheria toxin carried by temperate phage β. Nat. New Biol. 233:8-11.
    • (1971) Nat. New Biol. , vol.233 , pp. 8-11
    • Uchida, T.1    Gill, D.M.2    Pappenheimer A.M., Jr.3
  • 38
    • 0025782890 scopus 로고
    • Construction of versatile low-copy-number vectors for cloning, sequencing, and gene expression in Escherichia coli
    • Wang, R. F., and S. R. Kushner. 1991. Construction of versatile low-copy-number vectors for cloning, sequencing, and gene expression in Escherichia coli. Gene 100:195-199.
    • (1991) Gene , vol.100 , pp. 195-199
    • Wang, R.F.1    Kushner, S.R.2
  • 39
    • 0028267429 scopus 로고
    • Characterization of mutations that inactivate the diphtheria toxin repressor gene (dtxR)
    • Wang, Z., M. P. Schmitt, and R. K. Holmes. 1994. Characterization of mutations that inactivate the diphtheria toxin repressor gene (dtxR). Infect. Immun. 62:1600-1608.
    • (1994) Infect. Immun. , vol.62 , pp. 1600-1608
    • Wang, Z.1    Schmitt, M.P.2    Holmes, R.K.3
  • 40
    • 0032581662 scopus 로고    scopus 로고
    • Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
    • White, A., X. Ding, J. C. vanderSpek, J. R. Murphy, and D. Ringe. 1998. Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex. Nature 394:502-506.
    • (1998) Nature , vol.394 , pp. 502-506
    • White, A.1    Ding, X.2    Vanderspek, J.C.3    Murphy, J.R.4    Ringe, D.5


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