메뉴 건너뛰기




Volumn 8, Issue 7, 2013, Pages

YjcC, a c-di-GMP Phosphodiesterase Protein, Regulates the Oxidative Stress Response and Virulence of Klebsiella pneumoniae CG43

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CYCLIC GMP PHOSPHODIESTERASE; GLUTAREDOXIN I; HEAT SHOCK PROTEIN; HYDROGEN PEROXIDE; MUTANT PROTEIN; PARAQUAT; PILIN; PILIN MRKA; POLYSACCHARIDE; PROTEIN MRKHI; REACTIVE OXYGEN METABOLITE; RECOMBINANT PROTEIN; SCAVENGER; THIOREDOXIN; TRANSCRIPTOME; UNCLASSIFIED DRUG; YJCC CYCLIC GMP PHOSPHODIESTERASE PROTEIN;

EID: 84880730755     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0066740     Document Type: Article
Times cited : (42)

References (71)
  • 1
    • 67349119442 scopus 로고    scopus 로고
    • Expression of the yggE gene protects Escherichia coli from potassium tellurite-generated oxidative stress
    • Acuna LG, Calderon IL, Elias AO, Castro ME, Vasquez CC, (2009) Expression of the yggE gene protects Escherichia coli from potassium tellurite-generated oxidative stress. Arch Microbiol 191: 473-476.
    • (2009) Arch Microbiol , vol.191 , pp. 473-476
    • Acuna, L.G.1    Calderon, I.L.2    Elias, A.O.3    Castro, M.E.4    Vasquez, C.C.5
  • 2
    • 43149093576 scopus 로고    scopus 로고
    • Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation-derived aldehydes
    • Perez JM, Arenas FA, Pradenas GA, Sandoval JM, Vasquez CC, (2008) Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation-derived aldehydes. J Biol Chem 283: 7346-7353.
    • (2008) J Biol Chem , vol.283 , pp. 7346-7353
    • Perez, J.M.1    Arenas, F.A.2    Pradenas, G.A.3    Sandoval, J.M.4    Vasquez, C.C.5
  • 4
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay JA, (2003) Pathways of oxidative damage. Annu Rev Microbiol 57: 395-418.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 5
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay JA, (2008) Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 77: 755-776.
    • (2008) Annu Rev Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 6
    • 0035324440 scopus 로고    scopus 로고
    • Oxidative stress and mechanisms of protection against it in bacteria
    • Lushchak VI, (2001) Oxidative stress and mechanisms of protection against it in bacteria. Biochemistry (Mosc) 66: 476-489.
    • (2001) Biochemistry (Mosc) , vol.66 , pp. 476-489
    • Lushchak, V.I.1
  • 7
    • 0025278585 scopus 로고
    • Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus
    • Niederhoffer EC, Naranjo CM, Bradley KL, Fee JA, (1990) Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus. J Bacteriol 172: 1930-1938.
    • (1990) J Bacteriol , vol.172 , pp. 1930-1938
    • Niederhoffer, E.C.1    Naranjo, C.M.2    Bradley, K.L.3    Fee, J.A.4
  • 8
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • Farr SB, Kogoma T, (1991) Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol Rev 55: 561-585.
    • (1991) Microbiol Rev , vol.55 , pp. 561-585
    • Farr, S.B.1    Kogoma, T.2
  • 9
    • 27844581259 scopus 로고    scopus 로고
    • Hydrogen peroxide increases the activities of soxRS regulon enzymes and the levels of oxidized proteins and lipids in Escherichia coli
    • Semchyshyn H, Bagnyukova T, Storey K, Lushchak V, (2005) Hydrogen peroxide increases the activities of soxRS regulon enzymes and the levels of oxidized proteins and lipids in Escherichia coli. Cell Biol Int 29: 898-902.
    • (2005) Cell Biol Int , vol.29 , pp. 898-902
    • Semchyshyn, H.1    Bagnyukova, T.2    Storey, K.3    Lushchak, V.4
  • 11
    • 0030835705 scopus 로고    scopus 로고
    • Involvement of Fnr and ArcA in anaerobic expression of the tdc operon of Escherichia coli
    • Chattopadhyay S, Wu Y, Datta P, (1997) Involvement of Fnr and ArcA in anaerobic expression of the tdc operon of Escherichia coli. J Bacteriol 179: 4868-4873.
    • (1997) J Bacteriol , vol.179 , pp. 4868-4873
    • Chattopadhyay, S.1    Wu, Y.2    Datta, P.3
  • 12
    • 22644438480 scopus 로고    scopus 로고
    • C-di-GMP: the dawning of a novel bacterial signalling system
    • Romling U, Gomelsky M, Galperin MY, (2005) C-di-GMP: the dawning of a novel bacterial signalling system. Mol Microbiol 57: 629-639.
    • (2005) Mol Microbiol , vol.57 , pp. 629-639
    • Romling, U.1    Gomelsky, M.2    Galperin, M.Y.3
  • 13
    • 33845400857 scopus 로고    scopus 로고
    • Cyclic di-GMP signaling in bacteria: recent advances and new puzzles
    • Ryan RP, Fouhy Y, Lucey JF, Dow JM, (2006) Cyclic di-GMP signaling in bacteria: recent advances and new puzzles. J Bacteriol 188: 8327-8334.
    • (2006) J Bacteriol , vol.188 , pp. 8327-8334
    • Ryan, R.P.1    Fouhy, Y.2    Lucey, J.F.3    Dow, J.M.4
  • 14
    • 77956357900 scopus 로고    scopus 로고
    • Escherichia coli K-12 YfgF is an anaerobic cyclic di-GMP phosphodiesterase with roles in cell surface remodelling and the oxidative stress response
    • Lacey MM, Partridge JD, Green J, (2010) Escherichia coli K-12 YfgF is an anaerobic cyclic di-GMP phosphodiesterase with roles in cell surface remodelling and the oxidative stress response. Microbiology 156: 2873-2886.
    • (2010) Microbiology , vol.156 , pp. 2873-2886
    • Lacey, M.M.1    Partridge, J.D.2    Green, J.3
  • 15
    • 0031783181 scopus 로고    scopus 로고
    • Three cdg operons control cellular turnover of cyclic di-GMP in Acetobacter xylinum: genetic organization and occurrence of conserved domains in isoenzymes
    • Tal R, Wong HC, Calhoon R, Gelfand D, Fear AL, et al. (1998) Three cdg operons control cellular turnover of cyclic di-GMP in Acetobacter xylinum: genetic organization and occurrence of conserved domains in isoenzymes. J Bacteriol 180: 4416-4425.
    • (1998) J Bacteriol , vol.180 , pp. 4416-4425
    • Tal, R.1    Wong, H.C.2    Calhoon, R.3    Gelfand, D.4    Fear, A.L.5
  • 16
    • 77949325119 scopus 로고    scopus 로고
    • The cAMP receptor-like protein CLP is a novel c-di-GMP receptor linking cell-cell signaling to virulence gene expression in Xanthomonas campestris
    • Chin KH, Lee YC, Tu ZL, Chen CH, Tseng YH, et al. (2010) The cAMP receptor-like protein CLP is a novel c-di-GMP receptor linking cell-cell signaling to virulence gene expression in Xanthomonas campestris. J Mol Biol 396: 646-662.
    • (2010) J Mol Biol , vol.396 , pp. 646-662
    • Chin, K.H.1    Lee, Y.C.2    Tu, Z.L.3    Chen, C.H.4    Tseng, Y.H.5
  • 17
    • 33646397872 scopus 로고    scopus 로고
    • Analysis of FimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa
    • Kazmierczak BI, Lebron MB, Murray TS, (2006) Analysis of FimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa. Mol Microbiol 60: 1026-1043.
    • (2006) Mol Microbiol , vol.60 , pp. 1026-1043
    • Kazmierczak, B.I.1    Lebron, M.B.2    Murray, T.S.3
  • 18
    • 80052315142 scopus 로고    scopus 로고
    • MrkH, a novel c-di-GMP-dependent transcriptional activator, controls Klebsiella pneumoniae biofilm formation by regulating type 3 fimbriae expression
    • Wilksch JJ, Yang J, Clements A, Gabbe JL, Short KR, et al. (2011) MrkH, a novel c-di-GMP-dependent transcriptional activator, controls Klebsiella pneumoniae biofilm formation by regulating type 3 fimbriae expression. PLoS Pathog 7: e1002204.
    • (2011) PLoS Pathog , vol.7
    • Wilksch, J.J.1    Yang, J.2    Clements, A.3    Gabbe, J.L.4    Short, K.R.5
  • 19
    • 66149087307 scopus 로고    scopus 로고
    • XC1028 from Xanthomonas campestris adopts a PilZ domain-like structure without a c-di-GMP switch
    • Li TN, Chin KH, Liu JH, Wang AH, Chou SH, (2009) XC1028 from Xanthomonas campestris adopts a PilZ domain-like structure without a c-di-GMP switch. Proteins 75: 282-288.
    • (2009) Proteins , vol.75 , pp. 282-288
    • Li, T.N.1    Chin, K.H.2    Liu, J.H.3    Wang, A.H.4    Chou, S.H.5
  • 20
    • 76749083886 scopus 로고    scopus 로고
    • Vibrio cholerae VpsT regulates matrix production and motility by directly sensing cyclic di-GMP
    • Krasteva PV, Fong JC, Shikuma NJ, Beyhan S, Navarro MV, et al. (2010) Vibrio cholerae VpsT regulates matrix production and motility by directly sensing cyclic di-GMP. Science 327: 866-868.
    • (2010) Science , vol.327 , pp. 866-868
    • Krasteva, P.V.1    Fong, J.C.2    Shikuma, N.J.3    Beyhan, S.4    Navarro, M.V.5
  • 21
    • 19944422767 scopus 로고    scopus 로고
    • A glutamate-alanine-leucine (EAL) domain protein of Salmonella controls bacterial survival in mice, antioxidant defence and killing of macrophages: role of cyclic diGMP
    • Hisert KB, MacCoss M, Shiloh MU, Darwin KH, Singh S, et al. (2005) A glutamate-alanine-leucine (EAL) domain protein of Salmonella controls bacterial survival in mice, antioxidant defence and killing of macrophages: role of cyclic diGMP. Mol Microbiol 56: 1234-1245.
    • (2005) Mol Microbiol , vol.56 , pp. 1234-1245
    • Hisert, K.B.1    MacCoss, M.2    Shiloh, M.U.3    Darwin, K.H.4    Singh, S.5
  • 22
    • 9244224674 scopus 로고    scopus 로고
    • Capsule polysaccharide mediates bacterial resistance to antimicrobial peptides
    • Campos MA, Vargas MA, Regueiro V, Llompart CM, Alberti S, et al. (2004) Capsule polysaccharide mediates bacterial resistance to antimicrobial peptides. Infect Immun 72: 7107-7114.
    • (2004) Infect Immun , vol.72 , pp. 7107-7114
    • Campos, M.A.1    Vargas, M.A.2    Regueiro, V.3    Llompart, C.M.4    Alberti, S.5
  • 23
    • 34548119197 scopus 로고    scopus 로고
    • Pyogenic liver abscess caused by hypermucoviscous Klebsiella pneumoniae
    • Keynan Y, Karlowsky JA, Walus T, Rubinstein E, (2007) Pyogenic liver abscess caused by hypermucoviscous Klebsiella pneumoniae. Scand J Infect Dis 39: 828-830.
    • (2007) Scand J Infect Dis , vol.39 , pp. 828-830
    • Keynan, Y.1    Karlowsky, J.A.2    Walus, T.3    Rubinstein, E.4
  • 24
    • 80051616335 scopus 로고    scopus 로고
    • Isolation of genes involved in biofilm formation of a Klebsiella pneumoniae strain causing pyogenic liver abscess
    • Wu MC, Lin TL, Hsieh PF, Yang HC, Wang JT, (2011) Isolation of genes involved in biofilm formation of a Klebsiella pneumoniae strain causing pyogenic liver abscess. PLoS One 6: e23500.
    • (2011) PLoS One , vol.6
    • Wu, M.C.1    Lin, T.L.2    Hsieh, P.F.3    Yang, H.C.4    Wang, J.T.5
  • 25
    • 0037310768 scopus 로고    scopus 로고
    • RmpA2, an activator of capsule biosynthesis in Klebsiella pneumoniae CG43, regulates K2 cps gene expression at the transcriptional level
    • Lai YC, Peng HL, Chang HY, (2003) RmpA2, an activator of capsule biosynthesis in Klebsiella pneumoniae CG43, regulates K2 cps gene expression at the transcriptional level. J Bacteriol 185: 788-800.
    • (2003) J Bacteriol , vol.185 , pp. 788-800
    • Lai, Y.C.1    Peng, H.L.2    Chang, H.Y.3
  • 26
    • 33750686621 scopus 로고    scopus 로고
    • Homologous response regulators KvgA, KvhA and KvhR regulate the synthesis of capsular polysaccharide in Klebsiella pneumoniae CG43 in a coordinated manner
    • Lin CT, Huang TY, Liang WC, Peng HL, (2006) Homologous response regulators KvgA, KvhA and KvhR regulate the synthesis of capsular polysaccharide in Klebsiella pneumoniae CG43 in a coordinated manner. J Biochem 140: 429-438.
    • (2006) J Biochem , vol.140 , pp. 429-438
    • Lin, C.T.1    Huang, T.Y.2    Liang, W.C.3    Peng, H.L.4
  • 27
    • 79951500673 scopus 로고    scopus 로고
    • Fur regulation of the capsular polysaccharide biosynthesis and iron-acquisition systems in Klebsiella pneumoniae CG43
    • Lin CT, Wu CC, Chen YS, Lai YC, Chi C, et al. (2011) Fur regulation of the capsular polysaccharide biosynthesis and iron-acquisition systems in Klebsiella pneumoniae CG43. Microbiology 157: 419-429.
    • (2011) Microbiology , vol.157 , pp. 419-429
    • Lin, C.T.1    Wu, C.C.2    Chen, Y.S.3    Lai, Y.C.4    Chi, C.5
  • 28
    • 5644285349 scopus 로고    scopus 로고
    • High prevalence of phagocytic-resistant capsular serotypes of Klebsiella pneumoniae in liver abscess
    • Lin JC, Chang FY, Fung CP, Xu JZ, Cheng HP, et al. (2004) High prevalence of phagocytic-resistant capsular serotypes of Klebsiella pneumoniae in liver abscess. Microbes Infect 6: 1191-1198.
    • (2004) Microbes Infect , vol.6 , pp. 1191-1198
    • Lin, J.C.1    Chang, F.Y.2    Fung, C.P.3    Xu, J.Z.4    Cheng, H.P.5
  • 29
    • 0034440538 scopus 로고    scopus 로고
    • Capsule impedes adhesion to and invasion of epithelial cells by Klebsiella pneumoniae
    • Sahly H, Podschun R, Oelschlaeger TA, Greiwe M, Parolis H, et al. (2000) Capsule impedes adhesion to and invasion of epithelial cells by Klebsiella pneumoniae. Infect Immun 68: 6744-6749.
    • (2000) Infect Immun , vol.68 , pp. 6744-6749
    • Sahly, H.1    Podschun, R.2    Oelschlaeger, T.A.3    Greiwe, M.4    Parolis, H.5
  • 30
    • 0034778454 scopus 로고    scopus 로고
    • Identification of genes induced in vivo during Klebsiella pneumoniae CG43 infection
    • Lai YC, Peng HL, Chang HY, (2001) Identification of genes induced in vivo during Klebsiella pneumoniae CG43 infection. Infect Immun 69: 7140-7145.
    • (2001) Infect Immun , vol.69 , pp. 7140-7145
    • Lai, Y.C.1    Peng, H.L.2    Chang, H.Y.3
  • 31
    • 84868372310 scopus 로고    scopus 로고
    • Enzymatically Active and Inactive Phosphodiesterases and Diguanylate Cyclases Are Involved in Regulation of Motility or Sessility in Escherichia coli CFT073
    • Spurbeck RR, Tarrien RJ, Mobley HL, (2012) Enzymatically Active and Inactive Phosphodiesterases and Diguanylate Cyclases Are Involved in Regulation of Motility or Sessility in Escherichia coli CFT073. MBio 3.
    • (2012) MBio , vol.3
    • Spurbeck, R.R.1    Tarrien, R.J.2    Mobley, H.L.3
  • 33
    • 77955303037 scopus 로고    scopus 로고
    • Role of MrkJ, a phosphodiesterase, in type 3 fimbrial expression and biofilm formation in Klebsiella pneumoniae
    • Johnson JG, Clegg S, (2011) Role of MrkJ, a phosphodiesterase, in type 3 fimbrial expression and biofilm formation in Klebsiella pneumoniae. J Bacteriol 192: 3944-3950.
    • (2011) J Bacteriol , vol.192 , pp. 3944-3950
    • Johnson, J.G.1    Clegg, S.2
  • 34
    • 0034046748 scopus 로고    scopus 로고
    • Fur positive regulation of iron superoxide dismutase in Escherichia coli: functional analysis of the sodB promoter
    • Dubrac S, Touati D, (2000) Fur positive regulation of iron superoxide dismutase in Escherichia coli: functional analysis of the sodB promoter. J Bacteriol 182: 3802-3808.
    • (2000) J Bacteriol , vol.182 , pp. 3802-3808
    • Dubrac, S.1    Touati, D.2
  • 35
    • 79952790894 scopus 로고    scopus 로고
    • Regulation of catalase-peroxidase KatG is OxyR dependent and Fur independent in Caulobacter crescentus
    • Italiani VC, da Silva Neto JF, Braz VS, Marques MV, (2011) Regulation of catalase-peroxidase KatG is OxyR dependent and Fur independent in Caulobacter crescentus. J Bacteriol 193: 1734-1744.
    • (2011) J Bacteriol , vol.193 , pp. 1734-1744
    • Italiani, V.C.1    da Silva Neto, J.F.2    Braz, V.S.3    Marques, M.V.4
  • 36
    • 0030900804 scopus 로고    scopus 로고
    • Identification and analysis of the rpoS-dependent promoter of katE, encoding catalase HPII in Escherichia coli
    • Tanaka K, Handel K, Loewen PC, Takahashi H, (1997) Identification and analysis of the rpoS-dependent promoter of katE, encoding catalase HPII in Escherichia coli. Biochim Biophys Acta 1352: 161-166.
    • (1997) Biochim Biophys Acta , vol.1352 , pp. 161-166
    • Tanaka, K.1    Handel, K.2    Loewen, P.C.3    Takahashi, H.4
  • 37
    • 0030840083 scopus 로고    scopus 로고
    • RpoS- and OxyR-independent induction of HPI catalase at stationary phase in Escherichia coli and identification of rpoS mutations in common laboratory strains
    • Visick JE, Clarke S, (1997) RpoS- and OxyR-independent induction of HPI catalase at stationary phase in Escherichia coli and identification of rpoS mutations in common laboratory strains. J Bacteriol 179: 4158-4163.
    • (1997) J Bacteriol , vol.179 , pp. 4158-4163
    • Visick, J.E.1    Clarke, S.2
  • 38
    • 0034877746 scopus 로고    scopus 로고
    • Type 3 fimbrial shaft (MrkA) of Klebsiella pneumoniae, but not the fimbrial adhesin (MrkD), facilitates biofilm formation
    • Langstraat J, Bohse M, Clegg S, (2001) Type 3 fimbrial shaft (MrkA) of Klebsiella pneumoniae, but not the fimbrial adhesin (MrkD), facilitates biofilm formation. Infect Immun 69: 5805-5812.
    • (2001) Infect Immun , vol.69 , pp. 5805-5812
    • Langstraat, J.1    Bohse, M.2    Clegg, S.3
  • 39
    • 67650324665 scopus 로고    scopus 로고
    • Genome sequencing and comparative analysis of Klebsiella pneumoniae NTUH-K2044, a strain causing liver abscess and meningitis
    • Wu KM, Li LH, Yan JJ, Tsao N, Liao TL, et al. (2009) Genome sequencing and comparative analysis of Klebsiella pneumoniae NTUH-K2044, a strain causing liver abscess and meningitis. J Bacteriol 191: 4492-4501.
    • (2009) J Bacteriol , vol.191 , pp. 4492-4501
    • Wu, K.M.1    Li, L.H.2    Yan, J.J.3    Tsao, N.4    Liao, T.L.5
  • 40
    • 0038957365 scopus 로고    scopus 로고
    • Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress
    • Prieto-Alamo MJ, Jurado J, Gallardo-Madueno R, Monje-Casas F, Holmgren A, et al. (2000) Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress. J Biol Chem 275: 13398-13405.
    • (2000) J Biol Chem , vol.275 , pp. 13398-13405
    • Prieto-Alamo, M.J.1    Jurado, J.2    Gallardo-Madueno, R.3    Monje-Casas, F.4    Holmgren, A.5
  • 41
    • 33845689742 scopus 로고    scopus 로고
    • DinI and RecX modulate RecA-DNA structures in Escherichia coli K-12
    • Renzette N, Gumlaw N, Sandler SJ, (2007) DinI and RecX modulate RecA-DNA structures in Escherichia coli K-12. Mol Microbiol 63: 103-115.
    • (2007) Mol Microbiol , vol.63 , pp. 103-115
    • Renzette, N.1    Gumlaw, N.2    Sandler, S.J.3
  • 42
    • 0034653760 scopus 로고    scopus 로고
    • Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in Escherichia coli
    • Kitagawa M, Matsumura Y, Tsuchido T, (2000) Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in Escherichia coli. FEMS Microbiol Lett 184: 165-171.
    • (2000) FEMS Microbiol Lett , vol.184 , pp. 165-171
    • Kitagawa, M.1    Matsumura, Y.2    Tsuchido, T.3
  • 43
    • 77949329710 scopus 로고    scopus 로고
    • Synergistic cooperation between two ClpB isoforms in aggregate reactivation
    • Nagy M, Guenther I, Akoyev V, Barnett ME, Zavodszky MI, et al. (2010) Synergistic cooperation between two ClpB isoforms in aggregate reactivation. J Mol Biol 396: 697-707.
    • (2010) J Mol Biol , vol.396 , pp. 697-707
    • Nagy, M.1    Guenther, I.2    Akoyev, V.3    Barnett, M.E.4    Zavodszky, M.I.5
  • 44
    • 77957882515 scopus 로고    scopus 로고
    • Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli
    • Jovanovic G, Engl C, Mayhew AJ, Burrows PC, Buck M, (2010) Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli. Microbiology 156: 2920-2932.
    • (2010) Microbiology , vol.156 , pp. 2920-2932
    • Jovanovic, G.1    Engl, C.2    Mayhew, A.J.3    Burrows, P.C.4    Buck, M.5
  • 45
    • 0028856397 scopus 로고
    • Oxygen, iron, carbon, and superoxide control of the fumarase fumA and fumC genes of Escherichia coli: role of the arcA, fnr, and soxR gene products
    • Park SJ, Gunsalus RP, (1995) Oxygen, iron, carbon, and superoxide control of the fumarase fumA and fumC genes of Escherichia coli: role of the arcA, fnr, and soxR gene products. J Bacteriol 177: 6255-6262.
    • (1995) J Bacteriol , vol.177 , pp. 6255-6262
    • Park, S.J.1    Gunsalus, R.P.2
  • 46
    • 0039963175 scopus 로고    scopus 로고
    • Paraquat regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12 is SoxRS independent but modulated by sigma S
    • Membrillo-Hernandez J, Kim SO, Cook GM, Poole RK, (1997) Paraquat regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12 is SoxRS independent but modulated by sigma S. J Bacteriol 179: 3164-3170.
    • (1997) J Bacteriol , vol.179 , pp. 3164-3170
    • Membrillo-Hernandez, J.1    Kim, S.O.2    Cook, G.M.3    Poole, R.K.4
  • 47
    • 0029012855 scopus 로고
    • Isolation of a novel paraquat-inducible (pqi) gene regulated by the soxRS locus in Escherichia coli
    • Koh YS, Roe JH, (1995) Isolation of a novel paraquat-inducible (pqi) gene regulated by the soxRS locus in Escherichia coli. J Bacteriol 177: 2673-2678.
    • (1995) J Bacteriol , vol.177 , pp. 2673-2678
    • Koh, Y.S.1    Roe, J.H.2
  • 48
    • 0028140477 scopus 로고
    • NADPH: ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon
    • Liochev SI, Hausladen A, Beyer WF Jr, Fridovich I, (1994) NADPH: ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon. Proc Natl Acad Sci U S A 91: 1328-1331.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1328-1331
    • Liochev, S.I.1    Hausladen, A.2    Beyer Jr., W.F.3    Fridovich, I.4
  • 49
    • 61449200221 scopus 로고    scopus 로고
    • Gene expression patterns and differential input into curli fimbriae regulation of all GGDEF/EAL domain proteins in Escherichia coli
    • Sommerfeldt N, Possling A, Becker G, Pesavento C, Tschowri N, et al. (2009) Gene expression patterns and differential input into curli fimbriae regulation of all GGDEF/EAL domain proteins in Escherichia coli. Microbiology 155: 1318-1331.
    • (2009) Microbiology , vol.155 , pp. 1318-1331
    • Sommerfeldt, N.1    Possling, A.2    Becker, G.3    Pesavento, C.4    Tschowri, N.5
  • 50
    • 77950021681 scopus 로고    scopus 로고
    • Regulation of aerobic-to-anaerobic transitions by the FNR cycle in Escherichia coli
    • Tolla DA, Savageau MA, (2010) Regulation of aerobic-to-anaerobic transitions by the FNR cycle in Escherichia coli. J Mol Biol 397: 893-905.
    • (2010) J Mol Biol , vol.397 , pp. 893-905
    • Tolla, D.A.1    Savageau, M.A.2
  • 51
    • 84863515120 scopus 로고    scopus 로고
    • Comparative analysis of diguanylate cyclase and phosphodiesterase genes in Klebsiella pneumoniae
    • Cruz DP, Huertas MG, Lozano M, Zarate L, Zambrano MM, (2012) Comparative analysis of diguanylate cyclase and phosphodiesterase genes in Klebsiella pneumoniae. BMC Microbiol 12: 139.
    • (2012) BMC Microbiol , vol.12 , pp. 139
    • Cruz, D.P.1    Huertas, M.G.2    Lozano, M.3    Zarate, L.4    Zambrano, M.M.5
  • 52
    • 0037215715 scopus 로고    scopus 로고
    • Common extracellular sensory domains in transmembrane receptors for diverse signal transduction pathways in bacteria and archaea
    • Zhulin IB, Nikolskaya AN, Galperin MY, (2003) Common extracellular sensory domains in transmembrane receptors for diverse signal transduction pathways in bacteria and archaea. J Bacteriol 185: 285-294.
    • (2003) J Bacteriol , vol.185 , pp. 285-294
    • Zhulin, I.B.1    Nikolskaya, A.N.2    Galperin, M.Y.3
  • 53
    • 0345097587 scopus 로고    scopus 로고
    • FimX, a multidomain protein connecting environmental signals to twitching motility in Pseudomonas aeruginosa
    • Huang B, Whitchurch CB, Mattick JS, (2003) FimX, a multidomain protein connecting environmental signals to twitching motility in Pseudomonas aeruginosa. J Bacteriol 185: 7068-7076.
    • (2003) J Bacteriol , vol.185 , pp. 7068-7076
    • Huang, B.1    Whitchurch, C.B.2    Mattick, J.S.3
  • 54
    • 73349133007 scopus 로고    scopus 로고
    • Thioredoxins and glutaredoxins: unifying elements in redox biology
    • Meyer Y, Buchanan BB, Vignols F, Reichheld JP, (2009) Thioredoxins and glutaredoxins: unifying elements in redox biology. Annu Rev Genet 43: 335-367.
    • (2009) Annu Rev Genet , vol.43 , pp. 335-367
    • Meyer, Y.1    Buchanan, B.B.2    Vignols, F.3    Reichheld, J.P.4
  • 55
    • 33645951646 scopus 로고    scopus 로고
    • The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase
    • Caldas T, Malki A, Kern R, Abdallah J, Richarme G, (2006) The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase. Biochem Biophys Res Commun 343: 780-786.
    • (2006) Biochem Biophys Res Commun , vol.343 , pp. 780-786
    • Caldas, T.1    Malki, A.2    Kern, R.3    Abdallah, J.4    Richarme, G.5
  • 56
    • 0033933125 scopus 로고    scopus 로고
    • ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells
    • Thomas JG, Baneyx F, (2000) ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells. Mol Microbiol 36: 1360-1370.
    • (2000) Mol Microbiol , vol.36 , pp. 1360-1370
    • Thomas, J.G.1    Baneyx, F.2
  • 57
    • 0031426190 scopus 로고    scopus 로고
    • Regulation of fumarase (fumB) gene expression in Escherichia coli in response to oxygen, iron and heme availability: role of the arcA, fur, and hemA gene products
    • Tseng CP, (1997) Regulation of fumarase (fumB) gene expression in Escherichia coli in response to oxygen, iron and heme availability: role of the arcA, fur, and hemA gene products. FEMS Microbiol Lett 157: 67-72.
    • (1997) FEMS Microbiol Lett , vol.157 , pp. 67-72
    • Tseng, C.P.1
  • 58
    • 0035152663 scopus 로고    scopus 로고
    • Oxygen- and growth rate-dependent regulation of Escherichia coli fumarase (FumA, FumB, and FumC) activity
    • Tseng CP, Yu CC, Lin HH, Chang CY, Kuo JT, (2001) Oxygen- and growth rate-dependent regulation of Escherichia coli fumarase (FumA, FumB, and FumC) activity. J Bacteriol 183: 461-467.
    • (2001) J Bacteriol , vol.183 , pp. 461-467
    • Tseng, C.P.1    Yu, C.C.2    Lin, H.H.3    Chang, C.Y.4    Kuo, J.T.5
  • 59
    • 79251615811 scopus 로고    scopus 로고
    • Efficient enzymatic production of the bacterial second messenger c-di-GMP by the diguanylate cyclase YdeH from E. coli
    • Zahringer F, Massa C, Schirmer T, (2011) Efficient enzymatic production of the bacterial second messenger c-di-GMP by the diguanylate cyclase YdeH from E. coli. Appl Biochem Biotechnol 163: 71-79.
    • (2011) Appl Biochem Biotechnol , vol.163 , pp. 71-79
    • Zahringer, F.1    Massa, C.2    Schirmer, T.3
  • 60
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak KJ, Schmittgen TD, (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 61
    • 0028923873 scopus 로고
    • An enhanced broad-host-range vector for gram-negative bacteria: avoiding tetracycline phototoxicity during the growth of photosynthetic bacteria
    • Mather MW, McReynolds LM, Yu CA, (1995) An enhanced broad-host-range vector for gram-negative bacteria: avoiding tetracycline phototoxicity during the growth of photosynthetic bacteria. Gene 156: 85-88.
    • (1995) Gene , vol.156 , pp. 85-88
    • Mather, M.W.1    McReynolds, L.M.2    Yu, C.A.3
  • 62
    • 20444385050 scopus 로고    scopus 로고
    • The phosphodiesterase activity of the HmsP EAL domain is required for negative regulation of biofilm formation in Yersinia pestis
    • Bobrov AG, Kirillina O, Perry RD, (2005) The phosphodiesterase activity of the HmsP EAL domain is required for negative regulation of biofilm formation in Yersinia pestis. FEMS Microbiol Lett 247: 123-130.
    • (2005) FEMS Microbiol Lett , vol.247 , pp. 123-130
    • Bobrov, A.G.1    Kirillina, O.2    Perry, R.D.3
  • 63
    • 36549021125 scopus 로고    scopus 로고
    • BifA, a cyclic-Di-GMP phosphodiesterase, inversely regulates biofilm formation and swarming motility by Pseudomonas aeruginosa PA14
    • Kuchma SL, Brothers KM, Merritt JH, Liberati NT, Ausubel FM, et al. (2007) BifA, a cyclic-Di-GMP phosphodiesterase, inversely regulates biofilm formation and swarming motility by Pseudomonas aeruginosa PA14. J Bacteriol 189: 8165-8178.
    • (2007) J Bacteriol , vol.189 , pp. 8165-8178
    • Kuchma, S.L.1    Brothers, K.M.2    Merritt, J.H.3    Liberati, N.T.4    Ausubel, F.M.5
  • 64
    • 21844451590 scopus 로고    scopus 로고
    • The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains
    • Schmidt AJ, Ryjenkov DA, Gomelsky M, (2005) The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains. J Bacteriol 187: 4774-4781.
    • (2005) J Bacteriol , vol.187 , pp. 4774-4781
    • Schmidt, A.J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 65
    • 16344384874 scopus 로고    scopus 로고
    • Antioxidant activity of commercial soft and hard wheat (Triticum aestivum L.) as affected by gastric pH conditions
    • Liyana-Pathirana CM, Shahidi F, (2005) Antioxidant activity of commercial soft and hard wheat (Triticum aestivum L.) as affected by gastric pH conditions. J Agric Food Chem 53: 2433-2440.
    • (2005) J Agric Food Chem , vol.53 , pp. 2433-2440
    • Liyana-Pathirana, C.M.1    Shahidi, F.2
  • 66
    • 53249125530 scopus 로고    scopus 로고
    • Antibacterial and antioxidant properties of the methanol extracts of the leaves and stems of Calpurnia aurea
    • Adedapo AA, Jimoh FO, Koduru S, Afolayan AJ, Masika PJ, (2008) Antibacterial and antioxidant properties of the methanol extracts of the leaves and stems of Calpurnia aurea. BMC Complement Altern Med 8: 53.
    • (2008) BMC Complement Altern Med , vol.8 , pp. 53
    • Adedapo, A.A.1    Jimoh, F.O.2    Koduru, S.3    Afolayan, A.J.4    Masika, P.J.5
  • 67
    • 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
  • 68
    • 0015153416 scopus 로고
    • Superoxide dismutase: improved assays and an assay applicable to acrylamide gels
    • Beauchamp C, Fridovich I, (1971) Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem 44: 276-287.
    • (1971) Anal Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 69
    • 0015152970 scopus 로고
    • An improved procedure using ferricyanide for detecting catalase isozymes
    • Woodbury W, Spencer AK, Stahman MA, (1971) An improved procedure using ferricyanide for detecting catalase isozymes. Anal Biochem 44: 301-305.
    • (1971) Anal Biochem , vol.44 , pp. 301-305
    • Woodbury, W.1    Spencer, A.K.2    Stahman, M.A.3
  • 70
    • 33745158157 scopus 로고
    • A Simple Method Of Estimating Fifty Percent Endpoints l ' 2
    • Mnench Ljrah
    • Mnench Ljrah (1937) A Simple Method Of Estimating Fifty Percent Endpoints l ' 2. The Amerian Journal Of Hygiene 27: 493-497.
    • (1937) The Amerian Journal Of Hygiene , vol.27 , pp. 493-497
  • 71
    • 77954009646 scopus 로고    scopus 로고
    • RmpA regulation of capsular polysaccharide biosynthesis in Klebsiella pneumoniae CG43
    • Cheng HY, Chen YS, Wu CY, Chang HY, Lai YC, et al. (2010) RmpA regulation of capsular polysaccharide biosynthesis in Klebsiella pneumoniae CG43. J Bacteriol 192: 3144-3158.
    • (2010) J Bacteriol , vol.192 , pp. 3144-3158
    • Cheng, H.Y.1    Chen, Y.S.2    Wu, C.Y.3    Chang, H.Y.4    Lai, Y.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.