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Volumn 148, Issue 8, 2002, Pages 2449-2456

The ferric uptake regulator of Pseudomonas aeruginosa has no essential cysteine residues and does not contain a structural zinc ion

Author keywords

Fur; Iron regulation

Indexed keywords

ALANINE; APOPROTEIN; ASPARTIC ACID; BACTERIAL PROTEIN; CYSTEINE; EDETIC ACID; FERRIC ION; HISTIDINE; HYBRID PROTEIN; LIGAND; MALTOSE BINDING PROTEIN; MONOMER; REGULATOR PROTEIN; ZINC ION; CARRIER PROTEIN; IRON UPTAKE REGULATION PROTEIN, BACTERIA; IRON-UPTAKE REGULATION PROTEIN, BACTERIA; MALTOSE-BINDING PROTEIN; REPRESSOR PROTEIN; ZINC;

EID: 0036667431     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-148-8-2449     Document Type: Article
Times cited : (39)

References (39)
  • 4
    • 0032811011 scopus 로고    scopus 로고
    • Interaction of Bacillus subtilis Fur (ferric uptake repressor) with the dhb operator in vitro and in vivo
    • (1999) J. Bacteriol , vol.181 , pp. 4299-4307
    • Bsat, N.1    Helmann, J.D.2
  • 5
    • 0032561133 scopus 로고    scopus 로고
    • NasR, a novel RNA-binding protein, mediates nitrate-responsive transcription antitermination of the Klebsiella oxytoca M5al nasF operon leader in vitro
    • (1998) J. Mol. Biol , vol.283 , pp. 339-351
    • Chai, W.1    Stewart, V.2
  • 14
    • 0029818614 scopus 로고    scopus 로고
    • The role of Fur in the acid tolerance response of Salmonella typhimurium is physiologically and genetically separable from its role in iron acquisition
    • (1996) J. Bacteriol , vol.178 , pp. 5683-5691
    • Hall, H.K.1    Foster, J.W.2
  • 15
    • 0023443062 scopus 로고
    • Selection procedure for deregulated iron transport mutants (fur) in Escherichia coli K12: Fur not only affects iron metabolism
    • (1987) Mol. Gen. Genet , vol.210 , pp. 135-139
    • Hantke, K.1
  • 19
    • 0027524866 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator. Over-expression, purification, and characterization of wild type and delta F508 mutant forms of the first nucleotide binding fold in fusion with the maltose-binding protein
    • (1993) J. Biol. Chem , vol.268 , pp. 24330-24338
    • Ko, Y.H.1    Thomas, P.J.2    Delannoy, M.R.3    Pedersen, P.L.4
  • 20
    • 0004040064 scopus 로고
    • Principles of Fluorescence Spectroscopy
    • New York: Plenum Press
    • (1983)
    • Lakowicz, J.R.1
  • 23
    • 0028023092 scopus 로고
    • In vitro interaction of nitrate-responsive regulatory protein NarL with DNA target sequences in the fdnG, narG, narK and frdA operon control regions of Escherichia coli K-12
    • (1994) J. Mol. Biol , vol.241 , pp. 150-165
    • Li, J.1    Kustu, S.2    Stewart, V.3
  • 27
    • 0003842951 scopus 로고
    • A Short Course in Bacterial Genetics
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • (1992)
    • Miller, J.H.1
  • 28
    • 0028789238 scopus 로고
    • Role of the ferric uptake regulator of Pseudomonas aeruginosa in the regulation of siderophores and exotoxin A expression: Purification and activity on iron-regulated promoters
    • (1995) J. Bacteriol , vol.177 , pp. 7194-7201
    • Ochsner, U.A.1    Vasil, A.I.2    Vasil, M.L.3
  • 31
    • 0027251630 scopus 로고
    • Coordinate regulation of siderophore and exotoxin A production: Molecular cloning and sequencing of the Pseudomonas aeruginosa fur gene
    • (1993) J. Bacteriol , vol.175 , pp. 2589-2598
    • Prince, R.W.1    Cox, C.D.2    Vasil, M.L.3
  • 33
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.