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Volumn 195, Issue 8, 2013, Pages 1815-1824

A rex family transcriptional repressor influences H2O2 accumulation by Enterococcus faecalis

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; HYDROGEN PEROXIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PROTEIN EF2638; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REX PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTOME; UNCLASSIFIED DRUG;

EID: 84876088340     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.02135-12     Document Type: Article
Times cited : (53)

References (43)
  • 1
    • 0032906898 scopus 로고    scopus 로고
    • The steady-state internal redox state (NADH/NAD) reflects the external redox state and is correlated with catabolic adaptation in Escherichia coli
    • de Graef MR, Alexeeva S, Snoep JL, Teixeira de Mattos MJ. 1999. The steady-state internal redox state (NADH/NAD) reflects the external redox state and is correlated with catabolic adaptation in Escherichia coli. J. Bacteriol. 181:2351-2357.
    • (1999) J. Bacteriol. , vol.181 , pp. 2351-2357
    • de Graef, M.R.1    Alexeeva, S.2    Snoep, J.L.3    Teixeira de Mattos, M.J.4
  • 7
    • 0141737064 scopus 로고    scopus 로고
    • + redox poise in Streptomyces coelicolor A3(2)
    • + redox poise in Streptomyces coelicolor A3(2). EMBO J. 22:4856-4865.
    • (2003) EMBO J. , vol.22 , pp. 4856-4865
    • Brekasis, D.1    Paget, M.S.2
  • 8
    • 33749588803 scopus 로고    scopus 로고
    • +) ratio by Rex (YdiH) and oxidation of NADH by NADH dehydrogenase Ndh in Bacillus subtilis
    • +) ratio by Rex (YdiH) and oxidation of NADH by NADH dehydrogenase Ndh in Bacillus subtilis. J. Bacteriol. 188:7062-7071.
    • (2006) J. Bacteriol. , vol.188 , pp. 7062-7071
    • Gyan, S.1    Shiohira, Y.2    Sato, I.3    Takeuchi, M.4    Sato, T.5
  • 9
    • 79958856251 scopus 로고    scopus 로고
    • Transcriptional repressor Rex is involved in regulation of oxidative stress response and biofilm formation by Streptococcus mutans
    • Bitoun JP, Nguyen AH, Fan Y, Burne RA, Wen ZT. 2011. Transcriptional repressor Rex is involved in regulation of oxidative stress response and biofilm formation by Streptococcus mutans. FEMS Microbiol. Lett. 320:110 -117.
    • (2011) FEMS Microbiol. Lett. , vol.320
    • Bitoun, J.P.1    Nguyen, A.H.2    Fan, Y.3    Burne, R.A.4    Wen, Z.T.5
  • 11
    • 0025100795 scopus 로고
    • The life and times of the Enterococcus
    • Murray BE. 1990. The life and times of the Enterococcus. Clin. Microbiol. Rev. 3:46-65.
    • (1990) Clin. Microbiol. Rev. , vol.3 , pp. 46-65
    • Murray, B.E.1
  • 12
    • 0003254539 scopus 로고    scopus 로고
    • Enterococci as members of the intestinal microflora of humans, p 101-132
    • Gilmore MS, Clewell DB, Courvalin P, Dunny GM, Murray BE, Rice LB (ed) American Society for Microbiology Press, Washington, DC
    • Tannock GW, Cook G. 2002. Enterococci as members of the intestinal microflora of humans, p 101-132. In Gilmore MS, Clewell DB, Courvalin P, Dunny GM, Murray BE, Rice LB (ed), The enterococci: pathogenesis, molecular biology, and antibiotic resistance. American Society for Microbiology Press, Washington, DC.
    • (2002) The enterococci: pathogenesis, molecular biology, and antibiotic resistance
    • Tannock, G.W.1    Cook, G.2
  • 13
    • 0037105297 scopus 로고    scopus 로고
    • In vivo production of hydroxyl radical by Enterococcus faecalis colonizing the intestinal tract using aromatic hydroxylation
    • Huycke MM, Moore DR. 2002. In vivo production of hydroxyl radical by Enterococcus faecalis colonizing the intestinal tract using aromatic hydroxylation. Free Radic. Biol. Med. 33:818-826.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 818-826
    • Huycke, M.M.1    Moore, D.R.2
  • 14
    • 0036209728 scopus 로고    scopus 로고
    • Enterococcus faecalis produces extracellular superoxide and hydrogen peroxide that damages colonic epithelial cell DNA
    • Huycke MM, Abrams V, Moore DR. 2002. Enterococcus faecalis produces extracellular superoxide and hydrogen peroxide that damages colonic epithelial cell DNA. Carcinogenesis 23:529 -536.
    • (2002) Carcinogenesis , vol.23
    • Huycke, M.M.1    Abrams, V.2    Moore, D.R.3
  • 16
    • 0343990840 scopus 로고    scopus 로고
    • Evidence for regulation of the NADH peroxidase gene (npr) from Enterococcus faecalis by OxyR
    • Ross RP, Claiborne A. 1997. Evidence for regulation of the NADH peroxidase gene (npr) from Enterococcus faecalis by OxyR. FEMS Microbiol. Lett. 151:177-183.
    • (1997) FEMS Microbiol. Lett. , vol.151 , pp. 177-183
    • Ross, R.P.1    Claiborne, A.2
  • 17
    • 0026568406 scopus 로고
    • Flavin-linked peroxide reductases: protein-sulfenic acids and the oxidative stress response
    • Claiborne A, Ross RP, Parsonage D. 1992. Flavin-linked peroxide reductases: protein-sulfenic acids and the oxidative stress response. Trends Biochem. Sci. 17:183-186.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 183-186
    • Claiborne, A.1    Ross, R.P.2    Parsonage, D.3
  • 18
    • 0021024844 scopus 로고
    • Synthesis of catalase by Streptococcus faecalis subsp Zymogenes
    • Pugh SY, Knowles CJ. 1983. Synthesis of catalase by "Streptococcus faecalis subsp. Zymogenes." Arch. Microbiol. 136:60-63.
    • (1983) Arch. Microbiol. , vol.136 , pp. 60-63
    • Pugh, S.Y.1    Knowles, C.J.2
  • 20
    • 0017859596 scopus 로고
    • Superoxide dismutase and oxygen metabolism in Streptococcus faecalis and comparisons with other organisms
    • Britton L, Malinowski DP, Fridovich I. 1978. Superoxide dismutase and oxygen metabolism in Streptococcus faecalis and comparisons with other organisms. J. Bacteriol. 134:229 -236.
    • (1978) J. Bacteriol. , vol.134
    • Britton, L.1    Malinowski, D.P.2    Fridovich, I.3
  • 21
    • 0031656590 scopus 로고    scopus 로고
    • Enterococcus faecalis glutathione reductase: purification, characterization and expression under normal and hyperbaric O2 conditions
    • Patel MP, Marcinkeviciene J, Blanchard JS. 1998. Enterococcus faecalis glutathione reductase: purification, characterization and expression under normal and hyperbaric O2 conditions. FEMS Microbiol. Lett. 166: 155-163.
    • (1998) FEMS Microbiol. Lett. , vol.166 , pp. 155-163
    • Patel, M.P.1    Marcinkeviciene, J.2    Blanchard, J.S.3
  • 22
    • 0016747793 scopus 로고
    • The prevalence of enterococci in the human mouth and their pathogenicity in animal models
    • Gold OG, Jordan HV, van Houte J. 1975. The prevalence of enterococci in the human mouth and their pathogenicity in animal models. Arch. Oral Biol. 20:473- 477.
    • (1975) Arch. Oral Biol. , vol.20
    • Gold, O.G.1    Jordan, H.V.2    van Houte, J.3
  • 23
    • 84858689036 scopus 로고    scopus 로고
    • MurAA is required for intrinsic cephalosporin resistance of Enterococcus faecalis
    • Vesic D, Kristich CJ. 2012. MurAA is required for intrinsic cephalosporin resistance of Enterococcus faecalis. Antimicrob. Agents Chemother. 56: 2443-2451.
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 2443-2451
    • Vesic, D.1    Kristich, C.J.2
  • 24
  • 25
    • 33846993832 scopus 로고    scopus 로고
    • Development of a hostgenotype- independent counterselectable marker and a high-frequency conjugative delivery system and their use in genetic analysis of Enterococcus faecalis
    • Kristich CJ, Chandler JR, Dunny GM. 2007. Development of a hostgenotype- independent counterselectable marker and a high-frequency conjugative delivery system and their use in genetic analysis of Enterococcus faecalis. Plasmid 57:131-144.
    • (2007) Plasmid , vol.57 , pp. 131-144
    • Kristich, C.J.1    Chandler, J.R.2    Dunny, G.M.3
  • 26
    • 70350434311 scopus 로고    scopus 로고
    • Capsular polysaccharide production in Enterococcus faecalis and contribution of CpsF to capsule serospecificity
    • Thurlow LR, Thomas VC, Hancock LE. 2009. Capsular polysaccharide production in Enterococcus faecalis and contribution of CpsF to capsule serospecificity. J. Bacteriol. 191:6203- 6210.
    • (2009) J. Bacteriol. , vol.191
    • Thurlow, L.R.1    Thomas, V.C.2    Hancock, L.E.3
  • 28
    • 34249901823 scopus 로고    scopus 로고
    • New insights into the Enterococcus faecalis CroRS two-component system obtained using a differential- display random arbitrarily primed PCR approach
    • Le Breton Y, Muller C, Auffray Y, Rince A. 2007. New insights into the Enterococcus faecalis CroRS two-component system obtained using a differential- display random arbitrarily primed PCR approach. Appl. Environ. Microbiol. 73:3738 -3741.
    • (2007) Appl. Environ. Microbiol. , vol.73
    • Le Breton, Y.1    Muller, C.2    Auffray, Y.3    Rince, A.4
  • 29
    • 0027855511 scopus 로고
    • High- and low-copy-number Lactococcus shuttle cloning vectors with features for clone screening
    • O'Sullivan DJ, Klaenhammer TR. 1993. High- and low-copy-number Lactococcus shuttle cloning vectors with features for clone screening. Gene 137:227-231.
    • (1993) Gene , vol.137 , pp. 227-231
    • O'Sullivan, D.J.1    Klaenhammer, T.R.2
  • 30
    • 0030065558 scopus 로고    scopus 로고
    • Development of an expression strategy using a lytic phage to trigger explosive plasmid amplification and gene expression
    • O'Sullivan DJ, Walker SA, West SG, Klaenhammer TR. 1996. Development of an expression strategy using a lytic phage to trigger explosive plasmid amplification and gene expression. Biotechnology 14:82- 87.
    • (1996) Biotechnology , vol.14
    • O'Sullivan, D.J.1    Walker, S.A.2    West, S.G.3    Klaenhammer, T.R.4
  • 31
    • 26844580763 scopus 로고    scopus 로고
    • Development of a method for markerless genetic exchange in Enterococcus faecalis and its use in construction of a srtA mutant
    • Kristich CJ, Manias DA, Dunny GM. 2005. Development of a method for markerless genetic exchange in Enterococcus faecalis and its use in construction of a srtA mutant. Appl. Environ. Microbiol. 71:5837-5849.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 5837-5849
    • Kristich, C.J.1    Manias, D.A.2    Dunny, G.M.3
  • 32
    • 0029814919 scopus 로고    scopus 로고
    • Role of NAD in regulating the adhE gene of Escherichia coli
    • Leonardo MR, Dailly Y, Clark DP. 1996. Role of NAD in regulating the adhE gene of Escherichia coli. J. Bacteriol. 178:6013- 6018.
    • (1996) J. Bacteriol. , vol.178
    • Leonardo, M.R.1    Dailly, Y.2    Clark, D.P.3
  • 34
    • 84857161122 scopus 로고    scopus 로고
    • Use of recombinase-based in vivo expression technology to characterize Enterococcus faecalis gene expression during infection identifies in vivo-expressed antisense RNAs and implicates the protease Eep in pathogenesis
    • Frank KL, Barnes AM, Grindle SM, Manias DA, Schlievert PM, Dunny GM. 2012. Use of recombinase-based in vivo expression technology to characterize Enterococcus faecalis gene expression during infection identifies in vivo-expressed antisense RNAs and implicates the protease Eep in pathogenesis. Infect. Immun. 80:539 -549.
    • (2012) Infect. Immun. , vol.80
    • Frank, K.L.1    Barnes, A.M.2    Grindle, S.M.3    Manias, D.A.4    Schlievert, P.M.5    Dunny, G.M.6
  • 35
    • 67349215276 scopus 로고    scopus 로고
    • Physiological proteomics and stress/starvation responses in Bacillus subtilis and Staphylococcus aureus
    • Hecker M, Reder A, Fuchs S, Pagels M, Engelmann S. 2009. Physiological proteomics and stress/starvation responses in Bacillus subtilis and Staphylococcus aureus. Res. Microbiol. 160:245-258.
    • (2009) Res. Microbiol. , vol.160 , pp. 245-258
    • Hecker, M.1    Reder, A.2    Fuchs, S.3    Pagels, M.4    Engelmann, S.5
  • 36
    • 27144540194 scopus 로고    scopus 로고
    • Coordinated patterns of cytochrome bd and lactate dehydrogenase expression in Bacillus subtilis
    • Larsson JT, Rogstam A, von Wachenfeldt C. 2005. Coordinated patterns of cytochrome bd and lactate dehydrogenase expression in Bacillus subtilis. Microbiology 151:3323-3335.
    • (2005) Microbiology , vol.151 , pp. 3323-3335
    • Larsson, J.T.1    Rogstam, A.2    von Wachenfeldt, C.3
  • 37
    • 79953273591 scopus 로고    scopus 로고
    • Transcriptome, proteome, and metabolite analyses of a lactate dehydrogenase- negative mutant of Enterococcus faecalis V583
    • Mehmeti I, Jonsson M, Fergestad EM, Mathiesen G, Nes IF, Holo H. 2011. Transcriptome, proteome, and metabolite analyses of a lactate dehydrogenase- negative mutant of Enterococcus faecalis V583. Appl. Environ. Microbiol. 77:2406 -2413.
    • (2011) Appl. Environ. Microbiol. , vol.77
    • Mehmeti, I.1    Jonsson, M.2    Fergestad, E.M.3    Mathiesen, G.4    Nes, I.F.5    Holo, H.6
  • 39
    • 0027229131 scopus 로고
    • Regulation of glycerol metabolism in Enterococcus faecalis by phosphoenolpyruvate-dependent phosphorylation of glycerol kinase catalyzed by enzyme I and HPr of the phosphotransferase system
    • Deutscher J, Bauer B, Sauerwald H. 1993. Regulation of glycerol metabolism in Enterococcus faecalis by phosphoenolpyruvate-dependent phosphorylation of glycerol kinase catalyzed by enzyme I and HPr of the phosphotransferase system. J. Bacteriol. 175:3730 -3733.
    • (1993) J. Bacteriol. , vol.175
    • Deutscher, J.1    Bauer, B.2    Sauerwald, H.3
  • 40
    • 0035212036 scopus 로고    scopus 로고
    • Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli
    • Seaver LC, Imlay JA. 2001. Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli. J. Bacteriol. 183:7182-7189.
    • (2001) J. Bacteriol. , vol.183 , pp. 7182-7189
    • Seaver, L.C.1    Imlay, J.A.2
  • 42
    • 0037044847 scopus 로고    scopus 로고
    • Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase
    • Messner KR, Imlay JA. 2002. Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase. J. Biol. Chem. 277:42563-42571.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42563-42571
    • Messner, K.R.1    Imlay, J.A.2
  • 43
    • 36148995456 scopus 로고    scopus 로고
    • Comparative study of the physiological roles of three peroxidases (NADH peroxidase, alkyl hydroperoxide reductase and thiol peroxidase) in oxidative stress response, survival inside macrophages and virulence of Enterococcus faecalis
    • La Carbona S, Sauvageot N, Giard JC, Benachour A, Posteraro B, Auffray Y, Sanguinetti M, Hartke A. 2007. Comparative study of the physiological roles of three peroxidases (NADH peroxidase, alkyl hydroperoxide reductase and thiol peroxidase) in oxidative stress response, survival inside macrophages and virulence of Enterococcus faecalis. Mol. Microbiol. 66:1148 -1163.
    • (2007) Mol. Microbiol. , vol.66 , pp. 1148-1163
    • La Carbona, S.1    Sauvageot, N.2    Giard, J.C.3    Benachour, A.4    Posteraro, B.5    Auffray, Y.6    Sanguinetti, M.7    Hartke, A.8


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