메뉴 건너뛰기




Volumn 20, Issue 3, 2011, Pages 621-629

MarR homologs with urate-binding signature

Author keywords

Ligand binding; MarR; PecS; Transcriptional regulation; Urate

Indexed keywords

BACTERIAL PROTEIN; PROTEIN MARR; PROTEIN PECS; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; URATE; URATE OXIDASE; XANTHINE OXIDASE;

EID: 79952155643     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.588     Document Type: Article
Times cited : (23)

References (45)
  • 1
    • 1642295733 scopus 로고    scopus 로고
    • Immune cells: Free radicals and antioxidants in sepsis
    • DOI 10.1016/j.intimp.2004.01.020, PII S1567576904000487
    • Victor VM, Rocha M, De la Fuente M (2004) Immune cells: free radicals and antioxidants in sepsis. Int Immunopharmacol 4:327-347. (Pubitemid 38375967)
    • (2004) International Immunopharmacology , vol.4 , Issue.3 , pp. 327-347
    • Victor, V.M.1    Rocha, M.2    De, L.F.M.3
  • 3
    • 3242715114 scopus 로고    scopus 로고
    • Reactive oxygen species: Metabolism, oxidative stress, and signal transduction
    • DOI 10.1146/annurev.arplant.55.031903.141701
    • Apel K, Hirt H (2004) Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Annu Rev Plant Biol 55:373-399. (Pubitemid 38940937)
    • (2004) Annual Review of Plant Biology , vol.55 , pp. 373-399
    • Apel, K.1    Hirt, H.2
  • 4
    • 28144449309 scopus 로고    scopus 로고
    • Deinococcus radiodurans: The consummate survivor
    • Cox MM, Battista JR (2005) Deinococcus radiodurans: the consummate survivor. Nat Rev Microbiol 3:882-892.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 882-892
    • Cox, M.M.1    Battista, J.R.2
  • 5
    • 10944240100 scopus 로고    scopus 로고
    • HucR, a novel uric acid-responsive member of the MarR family of transcriptional regulators from Deinococcus radiodurans
    • DOI 10.1074/jbc.M405586200
    • Wilkinson SP, Grove A (2004) HucR, a novel uric acid-responsive member of the MarR family of transcriptional regulators from Deinococcus radiodurans. J Biol Chem 279:51442-51450. (Pubitemid 40017892)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 51442-51450
    • Wilkinson, S.P.1    Grove, A.2
  • 6
    • 79951505770 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand-mediated attenuation of DNA binding by MarR family transcriptional regulators
    • Perera IC, Grove A (2010) Molecular mechanisms of ligand-mediated attenuation of DNA binding by MarR family transcriptional regulators. J Mol Cell Biol 2:243-254
    • (2010) J Mol Cell Biol , vol.2 , pp. 243-254
    • Perera, I.C.1    Grove, A.2
  • 7
    • 20544435632 scopus 로고    scopus 로고
    • Negative cooperativity of uric acid binding to the transcriptional regulator HucR from Deinococcus radiodurans
    • DOI 10.1016/j.jmb.2005.05.027, PII S002228360500570X
    • Wilkinson SP, Grove A (2005) Negative cooperativity of uric acid binding to the transcriptional regulator HucR from Deinococcus radiodurans. J Mol Biol 350:617-630. (Pubitemid 40848663)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.4 , pp. 617-630
    • Wilkinson, S.P.1    Grove, A.2
  • 8
    • 33745267050 scopus 로고    scopus 로고
    • The Crystal Structure of the Transcriptional Regulator HucR from Deinococcus radiodurans Reveals a Repressor Preconfigured for DNA Binding
    • DOI 10.1016/j.jmb.2006.05.005, PII S0022283606005717
    • Bordelon T, Wilkinson SP, Grove A, Newcomer ME (2006) The crystal structure of the transcriptional regulator HucR from Deinococcus radiodurans reveals a repressor preconfigured for DNA binding. J Mol Biol 360:168-177. (Pubitemid 43927819)
    • (2006) Journal of Molecular Biology , vol.360 , Issue.1 , pp. 168-177
    • Bordelon, T.1    Wilkinson, S.P.2    Grove, A.3    Newcomer, M.E.4
  • 9
    • 67649836823 scopus 로고    scopus 로고
    • Mechanism for attenuation of DNA binding by MarR family transcriptional regulators by small molecule ligands
    • Perera IC, Lee YH, Wilkinson SP, Grove A (2009) Mechanism for attenuation of DNA binding by MarR family transcriptional regulators by small molecule ligands. J Mol Biol 390:1019-1029.
    • (2009) J Mol Biol , vol.390 , pp. 1019-1029
    • Perera, I.C.1    Lee, Y.H.2    Wilkinson, S.P.3    Grove, A.4
  • 10
    • 77956930197 scopus 로고    scopus 로고
    • Urate is a ligand for the transcriptional regulator PecS
    • Perera IC, Grove A (2010) Urate is a ligand for the transcriptional regulator PecS. J Mol Biol 402:571-583.
    • (2010) J Mol Biol , vol.402 , pp. 571-583
    • Perera, I.C.1    Grove, A.2
  • 11
    • 77957900698 scopus 로고    scopus 로고
    • Urate-responsive MarR homologs from Burkholderia
    • Grove A (2010) Urate-responsive MarR homologs from Burkholderia. Mol BioSyst 6:2133-2142.
    • (2010) Mol BioSyst , vol.6 , pp. 2133-2142
    • Grove, A.1
  • 12
    • 26944455545 scopus 로고    scopus 로고
    • PecS and PecT coregulate the synthesis of HrpN and pectate lyases, two virulence determinants in Erwinia chrysanthemi 3937
    • DOI 10.1094/MPMI-18-1205
    • Nasser W, Reverchon S, Vedel R, Boccara M (2005) PecS and PecT coregulate the synthesis of HrpN and pectate lyases, two virulence determinants in Erwinia chrysanthemi 3937. Mol Plant Microbe Interact 18:1205-1214. (Pubitemid 41484243)
    • (2005) Molecular Plant-Microbe Interactions , vol.18 , Issue.11 , pp. 1205-1214
    • Nasser, W.1    Reverchon, S.2    Vedel, R.3    Boccara, M.4
  • 13
    • 0030917519 scopus 로고    scopus 로고
    • Mutual control of the PecS/PecM couple, two proteins regulating virulence-factor synthesis in Erwinia chrysanthemi
    • Praillet T, Reverchon S, Nasser W (1997) Mutual control of the PecS/PecM couple, two proteins regulating virulence-factor synthesis in Erwinia chrysanthemi. Mol Microbiol 24:803-814. (Pubitemid 27229725)
    • (1997) Molecular Microbiology , vol.24 , Issue.4 , pp. 803-814
    • Praillet, T.1    Reverchon, S.2    Nasser, W.3
  • 14
    • 0029930138 scopus 로고    scopus 로고
    • Purification and functional characterization of PecS, a regulator of virulence-factor synthesis in Erwinia chrysanthemi
    • Praillet T, Nasser W, Robert-Baudouy J, Reverchon S (1996) Purification and functional characterization of PecS, a regulator of virulence-factor synthesis in Erwinia chrysanthemi. Mol Microbiol 20:391-402.
    • (1996) Mol Microbiol , vol.20 , pp. 391-402
    • Praillet, T.1    Nasser, W.2    Robert-Baudouy, J.3    Reverchon, S.4
  • 15
    • 0028334118 scopus 로고
    • PecS: A locus controlling pectinase, cellulase and blue pigment production in Erwinia chrysanthemi
    • DOI 10.1111/j.1365-2958.1994.tb00389.x
    • Reverchon S, Nasser W, Robert-Baudouy J (1994) pecS: a locus controlling pectinase, cellulase and blue pigment production in Erwinia chrysanthemi. Mol Microbiol 11:1127-1139. (Pubitemid 24201628)
    • (1994) Molecular Microbiology , vol.11 , Issue.6 , pp. 1127-1139
    • Reverchon, S.1    Nasser, W.2    Robert-Baudouy, J.3
  • 16
    • 0036168701 scopus 로고    scopus 로고
    • Characterization of indigoidine biosynthetic genes in Erwinia chrysanthemi and role of this blue pigment in pathogenicity
    • Reverchon S, Rouanet C, Expert D, Nasser W (2002) Characterization of indigoidine biosynthetic genes in Erwinia chrysanthemi and role of this blue pigment in pathogenicity. J Bacteriol 184:654-665. (Pubitemid 34150211)
    • (2002) Journal of Bacteriology , vol.184 , Issue.3 , pp. 654-665
    • Reverchon, S.1    Rouanet, C.2    Expert, D.3    Nasser, W.4
  • 17
    • 0035084902 scopus 로고    scopus 로고
    • The PecM protein of the phytopathogenic bacterium Erwinia chrysanthemi, membrane topology and possible involvement in the efflux of the blue pigment indigoidine
    • Rouanet C, Nasser W (2001) The PecM protein of the phytopathogenic bacterium Erwinia chrysanthemi, membrane topology and possible involvement in the efflux of the blue pigment indigoidine. J Mol Microbiol Biotechnol 3:309-318. (Pubitemid 32257918)
    • (2001) Journal of Molecular Microbiology and Biotechnology , vol.3 , Issue.2 , pp. 309-318
    • Rouanet, C.1    Nasser, W.2
  • 19
    • 0037097751 scopus 로고    scopus 로고
    • Bacteria-hemocyte interactions and phagocytosis in marine bivalves
    • DOI 10.1002/jemt.10100
    • Canesi L, Gallo G, Gavioli M, Pruzzo C (2002) Bacteria-hemocyte interactions and phagocytosis in marine bivalves. Microsc Res Tech 57:469-476. (Pubitemid 34701147)
    • (2002) Microscopy Research and Technique , vol.57 , Issue.6 , pp. 469-476
    • Canesi, L.1    Gallo, G.2    Gavioli, M.3    Pruzzo, C.4
  • 20
    • 0031600901 scopus 로고    scopus 로고
    • Specific Inhibition of Chemiluminescent Activity by Pathogenic Vibrios in Hemocytes of Two Marine Bivalves:Pecten maximus and Crassostrea gigas
    • DOI 10.1006/jipa.1997.4707, PII S0022201197947078
    • Lambert C, Nicolas JL (1998) Specific inhibition of chemiluminescent activity by pathogenic vibrios in hemocytes of two marine bivalves: Pecten maximus and Crassostrea gigas. J Invertebr Pathol 71:53-63. (Pubitemid 128352150)
    • (1998) Journal of Invertebrate Pathology , vol.71 , Issue.1 , pp. 53-63
    • Lambert, C.1    Nicolas, J.L.2
  • 21
    • 0034986539 scopus 로고    scopus 로고
    • Toxicity to bivalve hemocytes of pathogenic Vibrio cytoplasmic extract
    • DOI 10.1006/jipa.2001.5013
    • Lambert C, Nicolas JL, Bultel V (2001) Toxicity to bivalve hemocytes of pathogenic vibrio cytoplasmic extract. J Invertebr Pathol 77:165-172. (Pubitemid 32507615)
    • (2001) Journal of Invertebrate Pathology , vol.77 , Issue.3 , pp. 165-172
    • Lambert, C.1    Nicolas, J.-L.2    Bultel, V.3
  • 22
    • 0034117341 scopus 로고    scopus 로고
    • Xanthine oxidase contributes to host defense against Burkholderia cepacia in the p47(phox-/-) mouse model of chronic granulomatous disease
    • DOI 10.1128/IAI.68.4.2374-2378.2000
    • Segal BH, Sakamoto N, Patel M, Maemura K, Klein AS, Holland SM, Bulkley GB (2000) Xanthine oxidase contributes to host defense against Burkholderia cepacia in the p47(phox-/-) mouse model of chronic granulomatous disease. Infect Immun 68:2374-2378. (Pubitemid 30164882)
    • (2000) Infection and Immunity , vol.68 , Issue.4 , pp. 2374-2378
    • Segal, B.H.1    Sakamoto, N.2    Patel, M.3    Maemura, K.4    Klein, A.S.5    Holland, S.M.6    Bulkley, G.B.7
  • 23
    • 0029907839 scopus 로고    scopus 로고
    • Role of reactive oxygen metabolites in murine peritoneal macrophage phagocytosis and phagocytic killing
    • Takao S, Smith EH, Wang D, Chan CK, Bulkley GB, Klein AS (1996) Role of reactive oxygen metabolites in murine peritoneal macrophage phagocytosis and phagocytic killing. Am J Physiol 271:C1278-C1284.
    • (1996) Am J Physiol , vol.271
    • Takao, S.1    Smith, E.H.2    Wang, D.3    Chan, C.K.4    Bulkley, G.B.5    Klein, A.S.6
  • 25
    • 17444369030 scopus 로고    scopus 로고
    • Melioidosis: Epidemiology, pathophysiology, and management
    • DOI 10.1128/CMR.18.2.383-416.2005
    • Cheng AC, Currie BJ (2005) Melioidosis: epidemiology, pathophysiology, and management. Clin Microbiol Rev 18:383-416. (Pubitemid 40548298)
    • (2005) Clinical Microbiology Reviews , vol.18 , Issue.2 , pp. 383-416
    • Cheng, A.C.1    Currie, B.J.2
  • 26
    • 0034824349 scopus 로고    scopus 로고
    • The drug/metabolite transporter superfamily
    • DOI 10.1046/j.1432-1327.2001.02265.x
    • Jack DL, Yang NM, Saier MH, Jr. (2001) The drug/metabolite transporter superfamily. Eur J Biochem 268:3620-3639. (Pubitemid 32862900)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.13 , pp. 3620-3639
    • Jack, D.L.1    Yang, N.M.2    Saier Jr., M.H.3
  • 27
    • 0028277913 scopus 로고
    • Crystal structures of aconitase with transaconitate and nitrocitrate bound
    • Lauble H, Kennedy MC, Beinert H, Stout CD (1994) Crystal structures of aconitase with transaconitate and nitrocitrate bound. J Mol Biol 237:4374-4351.
    • (1994) J Mol Biol , vol.237 , pp. 4374-14351
    • Lauble, H.1    Kennedy, M.C.2    Beinert, H.3    Stout, C.D.4
  • 29
    • 0036225829 scopus 로고    scopus 로고
    • Escherichia coli aconitases and oxidative stress: Post-transcriptional regulation of sodA expression
    • Tang Y, Quail MA, Artymiuk PJ, Guest JR, Green J (2002) Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression. Microbiology 148:1027-1037. (Pubitemid 34436778)
    • (2002) Microbiology , vol.148 , Issue.4 , pp. 1027-1037
    • Tang, Y.1    Quail, M.A.2    Artymiuk, P.J.3    Guest, J.R.4    Green, J.5
  • 30
    • 69049103173 scopus 로고    scopus 로고
    • ST1710-DNA complex crystal structure reveals the DNA binding mechanism of the MarR family of regulators
    • Kumarevel T, Tanaka T, Umehara T, Yokoyama S (2009) ST1710-DNA complex crystal structure reveals the DNA binding mechanism of the MarR family of regulators. Nucl Acids Res 37:4723-4735.
    • (2009) Nucl Acids Res , vol.37 , pp. 4723-4735
    • Kumarevel, T.1    Tanaka, T.2    Umehara, T.3    Yokoyama, S.4
  • 31
    • 0032826179 scopus 로고    scopus 로고
    • Identifying DNA and protein patterns with statistically significant alignments of multiple sequences
    • Hertz GZ, Stormo GD (1999) Identifying DNA and protein patterns with statistically significant alignments of multiple sequences. Bioinformatics 15:563-577. (Pubitemid 29462105)
    • (1999) Bioinformatics , vol.15 , Issue.7-8 , pp. 563-577
    • Hertz, G.Z.1    Stormo, G.D.2
  • 32
    • 0037040884 scopus 로고    scopus 로고
    • The oligogalacturonate-specific porin KdgM of Erwinia chrysanthemi belongs to a new porin family
    • DOI 10.1074/jbc.M109193200
    • Blot N, Berrier C, Hugouvieux-Cotte-Pattat N, Ghazi A, Condemine G (2002) The oligogalacturonate-specific porin KdgM of Erwinia chrysanthemi belongs to a new porin family. J Biol Chem 277:7936-7944. (Pubitemid 34968244)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.10 , pp. 7936-7944
    • Blot, N.1    Berrier, C.2    Hugouvieux-Cotte-Pattat, N.3    Ghazi, A.4    Condemine, G.5
  • 33
    • 0025109929 scopus 로고
    • Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous
    • Neidhart DJ, Kenyon GL, Gerlt JA, Petsko GA (1990) Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous. Nature 347:692-694.
    • (1990) Nature , vol.347 , pp. 692-694
    • Neidhart, D.J.1    Kenyon, G.L.2    Gerlt, J.A.3    Petsko, G.A.4
  • 34
    • 0037072888 scopus 로고    scopus 로고
    • Identification of two protein-binding and functional regions of curli, a surface organelle and virulence determinant of Escherichia coli
    • Olsen A, Herwald H, Wikstrom M, Persson K, Mattsson E, Bjorck L (2002) Identification of two protein-binding and functional regions of curli, a surface organelle and virulence determinant of Escherichia coli. J Biol Chem 277:34568-34572.
    • (2002) J Biol Chem , vol.277 , pp. 34568-34572
    • Olsen, A.1    Herwald, H.2    Wikstrom, M.3    Persson, K.4    Mattsson, E.5    Bjorck, L.6
  • 35
    • 0030762287 scopus 로고    scopus 로고
    • Availability of the fibre subunit CsgA and the nucleator protein CsgB during assembly of fibronectin-binding curli is limited by the intracellular concentration of the novel lipoprotein CsgG
    • Loferer H, Hammar M, Normark S (1997) Availability of the fibre subunit CsgA and the nucleator protein CsgB during assembly of fibronectin-binding curli is limited by the intracellular concentration of the novel lipoprotein CsgG. Mol Microbiol 26:11-23. (Pubitemid 27438234)
    • (1997) Molecular Microbiology , vol.26 , Issue.1 , pp. 11-23
    • Loferer, H.1    Hammar, M.2    Normark, S.3
  • 36
    • 0037469629 scopus 로고    scopus 로고
    • The FliS chaperone selectively binds the disordered flagellin C-terminal D0 domain central to polymerisation
    • DOI 10.1016/S0378-1097(02)01208-9
    • Ozin AJ, Claret L, Auvray F, Hughes C (2003) The FliS chaperone selectively binds the disordered flagellin C-terminal D0 domain central to polymerisation. FEMS Microbiol Lett 219:219-224. (Pubitemid 36302601)
    • (2003) FEMS Microbiology Letters , vol.219 , Issue.2 , pp. 219-224
    • Ozin, A.J.1    Claret, L.2    Auvray, F.3    Hughes, C.4
  • 37
    • 0035957518 scopus 로고    scopus 로고
    • Flagellin polymerisation control by a cytosolic export chaperone
    • DOI 10.1006/jmbi.2001.4597
    • Auvray F, Thomas J, Fraser GM, Hughes C (2001) Flagellin polymerisation control by a cytosolic export chaperone. J Mol Biol 308:221-229. (Pubitemid 33043566)
    • (2001) Journal of Molecular Biology , vol.308 , Issue.2 , pp. 221-229
    • Auvray, F.1    Thomas, J.2    Fraser, G.M.3    Hughes, C.4
  • 38
    • 0031015566 scopus 로고    scopus 로고
    • Characterization of flagella genes of Agrobacterium tumefaciens, and the effect of a bald strain on virulence
    • Chesnokova O, Coutinho JB, Khan IH, Mikhail MS, Kado CI (1997) Characterization of flagella genes of Agrobacterium tumefaciens, and the effect of a bald strain on virulence. Mol Microbiol 23:579-590. (Pubitemid 27051387)
    • (1997) Molecular Microbiology , vol.23 , Issue.3 , pp. 579-590
    • Chesnokova, O.1    Coutinho, J.B.2    Khan, I.H.3    Mikhail, M.S.4    Kado, C.I.5
  • 39
    • 3142750481 scopus 로고    scopus 로고
    • Definition of a consensus DNA-binding site for PecS, a global regulator of virulence gene expression in Erwinia chrysanthemi and identification of new members of the PecS regulon
    • DOI 10.1074/jbc.M403343200
    • Rouanet C, Reverchon S, Rodionov DA, Nasser W (2004) Definition of a consensus DNA-binding site for PecS, a global regulator of virulence gene expression in Erwinia chrysanthemi and identification of new members of the PecS regulon. J Biol Chem 279:30158-30167. (Pubitemid 38937939)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.29 , pp. 30158-30167
    • Rouanet, C.1    Reverchon, S.2    Rodionov, D.A.3    Nasser, W.4
  • 40
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 41
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4:406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 42
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • Tamura K, Dudley J, Nei M, Kumar S (2007) MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24:1596-1599. (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 43
    • 0001895697 scopus 로고
    • Evolutionary divergence and convergence in proteins
    • Bryson V, Vogel HJ, Eds. New York: Academic Press
    • Zuckerkandl E, Pauling L, Evolutionary divergence and convergence in proteins. In: Bryson V, Vogel HJ, Eds. (1965) Evolving genes and proteins. New York: Academic Press, pp 97-166.
    • (1965) Evolving Genes and Proteins , pp. 97-166
    • Zuckerkandl, E.1    Pauling, L.2
  • 44
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein J (1985) Confidence limits on phylogenies: an approach using the bootstrap. Evolution 39:783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.