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Volumn 362, Issue 3, 2015, Pages

DtxR, an iron-dependent transcriptional repressor that regulates the expression of siderophore gene clusters in Thermobifida fusca

Author keywords

DxtR like repressor; Gel shift assay; Thermobifida fusca

Indexed keywords

SIDEROPHORE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR DTXR; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; DNA BINDING PROTEIN; IRON; REPRESSOR PROTEIN;

EID: 84944149112     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1093/femsle/fnu053     Document Type: Article
Times cited : (11)

References (17)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 55749106422 scopus 로고    scopus 로고
    • Structure elucidation and biosynthesis of fuscachelins, peptide siderophores from the moderate thermophile Thermobifida fusca
    • Dimise EJ, Widboom PF, Bruner SD. Structure elucidation and biosynthesis of fuscachelins, peptide siderophores from the moderate thermophile Thermobifida fusca. P Natl Acad Sci USA 2008;105:15311-16.
    • (2008) P Natl Acad Sci USA , vol.105 , pp. 15311-15316
    • Dimise, E.J.1    Widboom, P.F.2    Bruner, S.D.3
  • 3
    • 0021054302 scopus 로고
    • Effect of cellobiose, glucose, ethanol, and metal ions on the cellulase enzyme complex of Thermomonospora fusca
    • Ferchak JD, Pye EK. Effect of cellobiose, glucose, ethanol, and metal ions on the cellulase enzyme complex of Thermomonospora fusca. Biotechnol Bioeng 1983;25:2865-72.
    • (1983) Biotechnol Bioeng , vol.25 , pp. 2865-2872
    • Ferchak, J.D.1    Pye, E.K.2
  • 4
    • 77950225539 scopus 로고    scopus 로고
    • Development and application of a PCRtargeted gene disruption method for studying CelR function in Thermobifida fusca
    • Fong SS, Deng Y. Development and application of a PCRtargeted gene disruption method for studying CelR function in Thermobifida fusca. Appl Environ Microb 2010;76: 2098-106.
    • (2010) Appl Environ Microb , vol.76 , pp. 2098-2106
    • Fong, S.S.1    Deng, Y.2
  • 5
    • 1442306069 scopus 로고    scopus 로고
    • Genetic and biophysical studies of diphtheria toxin repressor (DtxR) and the hyperactive mutant DtxR(E175K) support a multistep model of activation
    • Love JF, vanderSpek JC, Marin V, et al. Genetic and biophysical studies of diphtheria toxin repressor (DtxR) and the hyperactive mutant DtxR(E175K) support a multistep model of activation. P Natl Acad Sci USA 2004;101:2506-11.
    • (2004) P Natl Acad Sci USA , vol.101 , pp. 2506-2511
    • Love, J.F.1    vanderSpek, J.C.2    Marin, V.3
  • 6
    • 84891938922 scopus 로고    scopus 로고
    • A role for the DtxR family of metalloregulators in Gram-positive pathogenesis
    • Merchant AT, Spatafora GA. A role for the DtxR family of metalloregulators in Gram-positive pathogenesis. Mol Oral Microbiol 2014;29:1-10.
    • (2014) Mol Oral Microbiol , vol.29 , pp. 1-10
    • Merchant, A.T.1    Spatafora, G.A.2
  • 7
    • 84903831403 scopus 로고    scopus 로고
    • Production of butyric acid by a cellulolytic actinobacterium Thermobifida fusca on cellulose
    • Merklein K, Fong SS, Deng Y. Production of butyric acid by a cellulolytic actinobacterium Thermobifida fusca on cellulose. Biochem Eng J 2014;90:239-44.
    • (2014) Biochem Eng J , vol.90 , pp. 239-244
    • Merklein, K.1    Fong, S.S.2    Deng, Y.3
  • 8
    • 34548739613 scopus 로고    scopus 로고
    • Siderophore-based iron acquisition and pathogen control
    • Miethke M, Marahiel MA. Siderophore-based iron acquisition and pathogen control. Microbiol Mol Biol R 2007;71: 413-51.
    • (2007) Microbiol Mol Biol R , vol.71 , pp. 413-451
    • Miethke, M.1    Marahiel, M.A.2
  • 9
    • 70350643410 scopus 로고    scopus 로고
    • The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis.
    • Oves-Costales D, Kadi N, Challis GL. The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis. Chem Commun (Cambridge) 2009;6530-41.
    • (2009) Chem Commun (Cambridge) , pp. 6530-6541
    • Oves-Costales, D.1    Kadi, N.2    Challis, G.L.3
  • 10
    • 18144400399 scopus 로고    scopus 로고
    • Programmable DNA self-assemblies for nanoscale organization of ligands and proteins
    • Park SH, Yin P, Liu Y, et al. Programmable DNA self-assemblies for nanoscale organization of ligands and proteins. Nano Lett 2005;5:729-33.
    • (2005) Nano Lett , vol.5 , pp. 729-733
    • Park, S.H.1    Yin, P.2    Liu, Y.3
  • 11
    • 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 MP, Holmes RK. 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 1991;59:3903-8.
    • (1991) Infect Immun , vol.59 , pp. 3903-3908
    • Schmitt, M.P.1    Holmes, R.K.2
  • 12
    • 0033988339 scopus 로고    scopus 로고
    • A celR mutation affecting transcription of cellulase genes in Thermobifida fusca
    • Spiridonov NA, Wilson DB. A celR mutation affecting transcription of cellulase genes in Thermobifida fusca. J Bacteriol 2000;182:252-5.
    • (2000) J Bacteriol , vol.182 , pp. 252-255
    • Spiridonov, N.A.1    Wilson, D.B.2
  • 13
    • 0027968843 scopus 로고
    • Determination of the minimal essential nucleotide sequence for diphtheria tox repressor binding by in vitro affinity selection
    • Tao X, Murphy JR. Determination of the minimal essential nucleotide sequence for diphtheria tox repressor binding by in vitro affinity selection. P Natl Acad Sci USA 1994;91: 9646-50.
    • (1994) P Natl Acad Sci USA , vol.91 , pp. 9646-9650
    • Tao, X.1    Murphy, J.R.2
  • 14
    • 0026782429 scopus 로고
    • Metal regulation of siderophore synthesis in Pseudomonas aeruginosa and functional effects of siderophore-metal complexes
    • Visca P, Colotti G, Serino L, et al. Metal regulation of siderophore synthesis in Pseudomonas aeruginosa and functional effects of siderophore-metal complexes. Appl Environ Microb 1992;58:2886-93.
    • (1992) Appl Environ Microb , vol.58 , pp. 2886-2893
    • Visca, P.1    Colotti, G.2    Serino, L.3
  • 15
    • 33645983933 scopus 로고    scopus 로고
    • The DtxR regulon of Corynebacterium glutamicum
    • Wennerhold J, Bott M. The DtxR regulon of Corynebacterium glutamicum. J Bacteriol 2006;188:2907-18.
    • (2006) J Bacteriol , vol.188 , pp. 2907-2918
    • Wennerhold, J.1    Bott, M.2
  • 16
    • 4143090473 scopus 로고    scopus 로고
    • Studies of Thermobifida fusca plant cellwall degrading enzymes
    • Wilson DB. Studies of Thermobifida fusca plant cellwall degrading enzymes. Chem Rec 2004;4:72-82.
    • (2004) Chem Rec , vol.4 , pp. 72-82
    • Wilson, D.B.1
  • 17
    • 84861894459 scopus 로고    scopus 로고
    • Functional self-assembled DNA nanostructures for molecular recognition
    • Zhang XJ, Yadavalli VK. Functional self-assembled DNA nanostructures for molecular recognition. Nanoscale 2012;4: 2439-46.
    • (2012) Nanoscale , vol.4 , pp. 2439-2446
    • Zhang, X.J.1    Yadavalli, V.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.