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Volumn 191, Issue 1, 2000, Pages 1-5

The iron dependent regulatory protein IdeR (DtxR) of Rhodococcus equi

Author keywords

DtxR; GalE; IdeR; Iron repressor; Rhodococcus equi

Indexed keywords

BACTERIAL PROTEIN; HELIX LOOP HELIX PROTEIN; IRON DEPENDENT REGULATORY PROTEIN IDER; REGULATOR PROTEIN; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE;

EID: 0034307852     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(00)00354-2     Document Type: Article
Times cited : (35)

References (22)
  • 1
    • 0030030233 scopus 로고    scopus 로고
    • Rhodococcus equi: An emerging opportunistic pathogen
    • Mosser D.M., Hondalus M.K. Rhodococcus equi: an emerging opportunistic pathogen. Trends Microbiol. 4:1996;29-33.
    • (1996) Trends Microbiol. , vol.4 , pp. 29-33
    • Mosser, D.M.1    Hondalus, M.K.2
  • 2
    • 0025988312 scopus 로고
    • Association between a large plasmid and 15- To 17-kilodalton antigens in virulent Rhodococcus equi
    • Takai S., Sekizaki T., Ozawa T., Sugawara T., Watanabe Y., Tsubaki S. Association between a large plasmid and 15- to 17-kilodalton antigens in virulent Rhodococcus equi. Infect. Immun. 59:1991;4056-4060.
    • (1991) Infect. Immun. , vol.59 , pp. 4056-4060
    • Takai, S.1    Sekizaki, T.2    Ozawa, T.3    Sugawara, T.4    Watanabe, Y.5    Tsubaki, S.6
  • 3
    • 0027978053 scopus 로고
    • Survival and replication of Rhodococcus equi in macrophages
    • Hondalus M.K., Mosser D.M. Survival and replication of Rhodococcus equi in macrophages. Infect. Immun. 62:1994;4167-4175.
    • (1994) Infect. Immun. , vol.62 , pp. 4167-4175
    • Hondalus, M.K.1    Mosser, D.M.2
  • 4
    • 18844480411 scopus 로고    scopus 로고
    • Role of the 85-kilobase plasmid and plasmid-encoded virulence-associated protein A in intracellular survival and virulence of Rhodococcus equi
    • Giguere S., Hondalus M.K., Yager J.A., Darrah P., Mosser D.M., Prescott J.F. Role of the 85-kilobase plasmid and plasmid-encoded virulence-associated protein A in intracellular survival and virulence of Rhodococcus equi. Infect. Immun. 67:1999;3548-3557.
    • (1999) Infect. Immun. , vol.67 , pp. 3548-3557
    • Giguere, S.1    Hondalus, M.K.2    Yager, J.A.3    Darrah, P.4    Mosser, D.M.5    Prescott, J.F.6
  • 5
    • 0026695690 scopus 로고
    • Virulence-associated 15- To 17-kilodalton antigens in Rhodococcus equi: Temperature-dependent expression and location of the antigens
    • Takai S., Iie M., Watanabe Y., Tsubaki S., Sekizaki T. Virulence-associated 15- to 17-kilodalton antigens in Rhodococcus equi: temperature-dependent expression and location of the antigens. Infect. Immun. 60:1992;2995-2997.
    • (1992) Infect. Immun. , vol.60 , pp. 2995-2997
    • Takai, S.1    Iie, M.2    Watanabe, Y.3    Tsubaki, S.4    Sekizaki, T.5
  • 6
    • 0027435537 scopus 로고
    • Iron uptake mechanisms of pathogenic bacteria
    • Wooldridge K.G., Williams P.H. Iron uptake mechanisms of pathogenic bacteria. FEMS Microbiol Rev. 12:1993;325-348.
    • (1993) FEMS Microbiol Rev. , vol.12 , pp. 325-348
    • Wooldridge, K.G.1    Williams, P.H.2
  • 7
    • 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., Predich M., Doukhan L., Smith I., Holmes R.K. 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. 63:1995;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
  • 9
    • 0033607166 scopus 로고    scopus 로고
    • Attenuation of virulence in Mycobacterium tuberculosis expressing a constitutively active iron repressor
    • Manabe Y.C., Saviola B.J., Sun L., Murphy J.R., Bishai W.R. Attenuation of virulence in Mycobacterium tuberculosis expressing a constitutively active iron repressor. Proc. Natl. Acad. Sci. USA. 96:1999;12844-12848.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12844-12848
    • Manabe, Y.C.1    Saviola, B.J.2    Sun, L.3    Murphy, J.R.4    Bishai, W.R.5
  • 10
    • 0029809920 scopus 로고    scopus 로고
    • An ideR mutant of Mycobacterium smegmatis has derepressed siderophore production and an altered oxidative-stress response
    • Dussurget O., Rodriguez M., Smith I. An ideR mutant of Mycobacterium smegmatis has derepressed siderophore production and an altered oxidative-stress response. Mol. Microbiol. 22:1996;535-544.
    • (1996) Mol. Microbiol. , vol.22 , pp. 535-544
    • Dussurget, O.1    Rodriguez, M.2    Smith, I.3
  • 11
    • 0032461682 scopus 로고    scopus 로고
    • Molecular characterisation of a Rhodococcus ohp operon
    • Powell J.A., Archer J.A. Molecular characterisation of a Rhodococcus ohp operon. Antonie van Leeuwenhoek. 74:1998;175-188.
    • (1998) Antonie Van Leeuwenhoek , vol.74 , pp. 175-188
    • Powell, J.A.1    Archer, J.A.2
  • 12
    • 0001582410 scopus 로고
    • Development of improved Rhodococcus plasmid vectors and their use in cloning genes of potential commercial and medical importance
    • Dabbs, E.R., Gowan, B., Quan, S., Anderson, S.J. (1995) Development of improved Rhodococcus plasmid vectors and their use in cloning genes of potential commercial and medical importance. Biotekhnologiya 7-8, 129-135.
    • (1995) Biotekhnologiya , vol.7-8 , pp. 129-135
    • Dabbs, E.R.1    Gowan, B.2    Quan, S.3    Anderson, S.J.4
  • 13
    • 0025782890 scopus 로고
    • Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli
    • Wang R.F., Kushner S.R. Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli. Gene. 100:1991;195-199.
    • (1991) Gene , vol.100 , pp. 195-199
    • Wang, R.F.1    Kushner, S.R.2
  • 14
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening of recombinant plasmid DNA
    • Birnboim H.C., Doly J. A rapid alkaline extraction procedure for screening of recombinant plasmid DNA. Nucleic Acids Res. 7:1979;1513-1523.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 15
    • 0028950304 scopus 로고
    • Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase
    • Nagy I., Schoofs G., Compernolle F., Proost P., Vanderleyden J., De Mot R. Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase. J. Bacteriol. 177:1995;676-687.
    • (1995) J. Bacteriol. , vol.177 , pp. 676-687
    • Nagy, I.1    Schoofs, G.2    Compernolle, F.3    Proost, P.4    Vanderleyden, J.5    De Mot, R.6
  • 16
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J.H. (1972) Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 73:1976;248-254.
    • (1976) Anal. Biochem. , vol.73 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0030600478 scopus 로고    scopus 로고
    • The galE gene encoding the UDP-galactose 4-epimerase of Brevibacterium lactofermentum is coupled transcriptionally to the dmdR gene
    • Oguiza J.A., Marcos A.T., Malumbres M., Martin J.F. The galE gene encoding the UDP-galactose 4-epimerase of Brevibacterium lactofermentum is coupled transcriptionally to the dmdR gene. Gene. 177:1996;103-107.
    • (1996) Gene , vol.177 , pp. 103-107
    • Oguiza, J.A.1    Marcos, A.T.2    Malumbres, M.3    Martin, J.F.4
  • 19
    • 0028826149 scopus 로고
    • Structures of the apo- And the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae
    • Schiering N., Tao X., Zeng H., Murphy J.R., Petsko G.A., Ringe D. Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae. Proc. Natl. Acad. Sci. USA. 92:1995;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
  • 20
    • 0025300518 scopus 로고
    • Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae
    • Boyd J., Oza M.N., Murphy J.R. Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae. Proc. Natl. Acad. Sci. USA. 87:1990;5968-5972.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5968-5972
    • Boyd, J.1    Oza, M.N.2    Murphy, J.R.3
  • 21
    • 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., Holmes R.K. 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. 176:1994;1141-1149.
    • (1994) J. Bacteriol. , vol.176 , pp. 1141-1149
    • Schmitt, M.P.1    Holmes, R.K.2
  • 22
    • 0027968843 scopus 로고
    • Determination of the minimal essential nucleotide sequence for diphtheria tox repressor binding by in vitro affinity selection
    • Tao X., Murphy J.R. Determination of the minimal essential nucleotide sequence for diphtheria tox repressor binding by in vitro affinity selection. Proc. Natl. Acad. Sci. USA. 91:1994;9646-9650.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9646-9650
    • Tao, X.1    Murphy, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.