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Volumn 261, Issue 2, 2006, Pages 211-217

The Bacteroides fragilis P20 scavengase homolog is important in the oxidative stress response but is not controlled by OxyR

Author keywords

Bacteroides fragilis; Oxidative stress; Scavengase; Thiol peroxidase

Indexed keywords

BACTERIAL ENZYME; HYDROGEN PEROXIDE; MEMBRANE PROTEIN; MESSENGER RNA; MUTANT PROTEIN; OXYGEN; REGULATOR PROTEIN; REGULATOR PROTEIN OXYR; TERT BUTYL HYDROPEROXIDE; THIOL PEROXIDASE SCAVENGASE; UNCLASSIFIED DRUG;

EID: 33746555444     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2006.00353.x     Document Type: Article
Times cited : (14)

References (29)
  • 1
    • 0037646517 scopus 로고    scopus 로고
    • Catalytic mechanism of thiol peroxidase from Escherichia coli: Sulfenic acid formation and overoxidation of essential CYS61
    • Baker LM & Poole LB (2003) Catalytic mechanism of thiol peroxidase from Escherichia coli: sulfenic acid formation and overoxidation of essential CYS61. J Biol Chem 278: 9203-9211.
    • (2003) J Biol Chem , vol.278 , pp. 9203-9211
    • Baker, L.M.1    Poole, L.B.2
  • 2
    • 0037007024 scopus 로고    scopus 로고
    • A mitochondrial-like aconitase in the bacterium Bacteroides fragilis: Implications for the evolution of the mitochondrial Krebs cycle
    • Baughn AD & Malamy MH (2002) A mitochondrial-like aconitase in the bacterium Bacteroides fragilis: implications for the evolution of the mitochondrial Krebs cycle. Proc Natl Acad Sci USA 99: 4662-4667.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4662-4667
    • Baughn, A.D.1    Malamy, M.H.2
  • 3
    • 0842264185 scopus 로고    scopus 로고
    • The strict anaerobe Bacteroides fragilis grows in and benefits from nanomolar concentrations of oxygen
    • Baughn AD & Malamy MH (2004) The strict anaerobe Bacteroides fragilis grows in and benefits from nanomolar concentrations of oxygen. Nature 427: 441-444.
    • (2004) Nature , vol.427 , pp. 441-444
    • Baughn, A.D.1    Malamy, M.H.2
  • 4
    • 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 (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 1542335652 scopus 로고    scopus 로고
    • Escherichia coli periplasmic thiol peroxidase acts as lipid hydroperoxide peroxidase and the principal antioxidative function during anaerobic growth
    • Cha MK, Kim WC, Lim CJ, Kim K & Kim IH (2004) Escherichia coli periplasmic thiol peroxidase acts as lipid hydroperoxide peroxidase and the principal antioxidative function during anaerobic growth. J Biol Chem 279: 8769-8778.
    • (2004) J Biol Chem , vol.279 , pp. 8769-8778
    • Cha, M.K.1    Kim, W.C.2    Lim, C.J.3    Kim, K.4    Kim, I.H.5
  • 6
    • 0027526941 scopus 로고
    • A role for Bacteroides fragilis neuraminidase in bacterial growth in two model systems
    • Godoy VG, Dallas MM, Russo TA & Malamy MH (1993) A role for Bacteroides fragilis neuraminidase in bacterial growth in two model systems. Infect Immun 61: 4415-4426.
    • (1993) Infect Immun , vol.61 , pp. 4415-4426
    • Godoy, V.G.1    Dallas, M.M.2    Russo, T.A.3    Malamy, M.H.4
  • 7
    • 0022273807 scopus 로고
    • 2-induced manganese-containing superoxide dismutase from Bacteroides fragilis
    • 2-induced manganese-containing superoxide dismutase from Bacteroides fragilis. Arch Biochem Biophys 238: 83-89.
    • (1985) Arch Biochem Biophys , vol.238 , pp. 83-89
    • Gregory, E.M.1
  • 8
    • 0014310082 scopus 로고
    • Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis
    • Hedrick JL & Smith AJ (1968) Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis. Arch Biochem Biophys 126: 155-164.
    • (1968) Arch Biochem Biophys , vol.126 , pp. 155-164
    • Hedrick, J.L.1    Smith, A.J.2
  • 9
    • 0141887670 scopus 로고    scopus 로고
    • Genetic analysis of an important oxidative stress locus in the anaerobe Bacteroides fragilis
    • Herren CD, Rocha ER & Smith CJ (2003) Genetic analysis of an important oxidative stress locus in the anaerobe Bacteroides fragilis. Gene 316: 167-175.
    • (2003) Gene , vol.316 , pp. 167-175
    • Herren, C.D.1    Rocha, E.R.2    Smith, C.J.3
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl MW (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29: e45.
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1
  • 12
    • 0029019571 scopus 로고
    • Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilis
    • Rocha ER & Smith CJ (1995) Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilis. J Bacteriol 177: 3111-3119.
    • (1995) J Bacteriol , vol.177 , pp. 3111-3119
    • Rocha, E.R.1    Smith, C.J.2
  • 13
    • 0030613766 scopus 로고    scopus 로고
    • Regulation of Bacteriodes fragilis katB mRNA by oxidative stress and carbon limitation
    • Rocha ER & Smith CJ (1997) Regulation of Bacteriodes fragilis katB mRNA by oxidative stress and carbon limitation. J Bacteriol 179: 7033-7039.
    • (1997) J Bacteriol , vol.179 , pp. 7033-7039
    • Rocha, E.R.1    Smith, C.J.2
  • 14
    • 0031734418 scopus 로고    scopus 로고
    • Characterization of a peroxide-resistant mutant of the anaerobic bacterium Bacteroides fragilis
    • Rocha ER & Smith CJ (1998) Characterization of a peroxide-resistant mutant of the anaerobic bacterium Bacteroides fragilis. J Bacteriol 180: 5906-5912.
    • (1998) J Bacteriol , vol.180 , pp. 5906-5912
    • Rocha, E.R.1    Smith, C.J.2
  • 15
    • 0032851571 scopus 로고    scopus 로고
    • Role of the alkyl hydroperoxide reductase (ahpCF) gene in oxidative stress defense of the obligate anaerobe Bacteroides fragilis
    • Rocha ER & Smith CJ (1999) Role of the alkyl hydroperoxide reductase (ahpCF) gene in oxidative stress defense of the obligate anaerobe Bacteroides fragilis. J Bacteriol 181: 5701-5710.
    • (1999) J Bacteriol , vol.181 , pp. 5701-5710
    • Rocha, E.R.1    Smith, C.J.2
  • 16
    • 4344664059 scopus 로고    scopus 로고
    • Transcriptional regulation of the Bacteroides fragilis ferritin gene (ftnA) by redox stress
    • Rocha ER & Smith CJ (2004) Transcriptional regulation of the Bacteroides fragilis ferritin gene (ftnA) by redox stress. Microbiology 150: 2125-2134.
    • (2004) Microbiology , vol.150 , pp. 2125-2134
    • Rocha, E.R.1    Smith, C.J.2
  • 17
    • 0029848194 scopus 로고    scopus 로고
    • Oxidative stress response in an anaerobe, Bacteroides fragilis: A role for catalase in protection against hydrogen peroxide
    • Rocha ER, Selby T, Coleman JP & Smith CJ (1996) Oxidative stress response in an anaerobe, Bacteroides fragilis: a role for catalase in protection against hydrogen peroxide. J Bacteriol 178: 6895-6903.
    • (1996) J Bacteriol , vol.178 , pp. 6895-6903
    • Rocha, E.R.1    Selby, T.2    Coleman, J.P.3    Smith, C.J.4
  • 18
    • 0033816764 scopus 로고    scopus 로고
    • The redox-sensitive transcriptional activator OxyR regulates the peroxide response regulon in the obligate anaerobe Bacteroides fragilis
    • Rocha ER, Owens G Jr & Smith CJ (2000) The redox-sensitive transcriptional activator OxyR regulates the peroxide response regulon in the obligate anaerobe Bacteroides fragilis. J Bacteriol 182: 5059-5069.
    • (2000) J Bacteriol , vol.182 , pp. 5059-5069
    • Rocha, E.R.1    Owens Jr., G.2    Smith, C.J.3
  • 19
    • 0141788349 scopus 로고    scopus 로고
    • The complex oxidative stress response of Bacteroides fragilis: The role of OxyR in control of gene expression
    • Rocha ER, Herren CD, Smalley DJ & Smith CJ (2003) The complex oxidative stress response of Bacteroides fragilis: the role of OxyR in control of gene expression. Anaerobe 9: 165-173.
    • (2003) Anaerobe , vol.9 , pp. 165-173
    • Rocha, E.R.1    Herren, C.D.2    Smalley, D.J.3    Smith, C.J.4
  • 20
    • 0028176653 scopus 로고
    • Insertional activation of cepA leads to high-level beta-lactamase expression in Bacteroides fragilis clinical isolates
    • Rogers MB, Bennett TK, Payne CM & Smith CJ (1994) Insertional activation of cepA leads to high-level beta-lactamase expression in Bacteroides fragilis clinical isolates. J Bacteriol 176: 4376-4384.
    • (1994) J Bacteriol , vol.176 , pp. 4376-4384
    • Rogers, M.B.1    Bennett, T.K.2    Payne, C.M.3    Smith, C.J.4
  • 21
    • 0036155121 scopus 로고    scopus 로고
    • Aerobic-type ribonucleotide reductase in the anaerobe Bacteroides fragilis
    • Smalley D, Rocha ER & Smith CJ (2002) Aerobic-type ribonucleotide reductase in the anaerobe Bacteroides fragilis. J Bacteriol 184: 895-903.
    • (2002) J Bacteriol , vol.184 , pp. 895-903
    • Smalley, D.1    Rocha, E.R.2    Smith, C.J.3
  • 22
    • 0021978480 scopus 로고
    • Characterization of Bacteroides ovatus plasmid pBI136 and structure of its clindamycin resistance region
    • Smith CJ (1985) Characterization of Bacteroides ovatus plasmid pBI136 and structure of its clindamycin resistance region. J Bacteriol 161: 1069-1073.
    • (1985) J Bacteriol , vol.161 , pp. 1069-1073
    • Smith, C.J.1
  • 23
    • 0029589940 scopus 로고
    • Nucleotide sequence determination and genetic analysis of the Bacteroides plasmid, pBI143
    • Smith CJ, Rollins LA & Parker AC (1995) Nucleotide sequence determination and genetic analysis of the Bacteroides plasmid, pBI143. Plasmid 34: 211-222.
    • (1995) Plasmid , vol.34 , pp. 211-222
    • Smith, C.J.1    Rollins, L.A.2    Parker, A.C.3
  • 25
  • 27
    • 0028306066 scopus 로고
    • Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides
    • Wolff SP (1994) Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides. Methods Enzymol 233: 182-189.
    • (1994) Methods Enzymol , vol.233 , pp. 182-189
    • Wolff, S.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.