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Volumn 8, Issue 9, 2013, Pages

The Transcriptional Regulator Np20 Is the Zinc Uptake Regulator in Pseudomonas aeruginosa

Author keywords

[No Author keywords available]

Indexed keywords

CHELATING AGENT; N,N'N TETRAKIS(2 PYRIDYLMETHYL)ETHYLENEDIAMINE; PROTEIN NP20; RECOMBINANT PROTEIN; RECOMBINANT ZURPA; REGULATOR PROTEIN; UNCLASSIFIED DRUG; ZINC;

EID: 84884519461     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0075389     Document Type: Article
Times cited : (48)

References (53)
  • 1
    • 30744471169 scopus 로고    scopus 로고
    • Counting the zinc-proteins encoded in the human genome
    • doi: 10.1021/pr050361j
    • Andreini C, Banci L, Bertini I, Rosato A, (2006) Counting the zinc-proteins encoded in the human genome. J Proteome Res 5: 196-201. doi:10.1021/pr050361j. PubMed: 16396512.
    • (2006) J Proteome Res , vol.5 , pp. 196-201
    • Andreini, C.1    Banci, L.2    Bertini, I.3    Rosato, A.4
  • 2
    • 0027203884 scopus 로고
    • Effect of zinc on superoxide-dependent hydroxyl radical production in vitro
    • doi: 10.1007/BF02785311
    • Coudray C, Rachidi S, Favier A, (1993) Effect of zinc on superoxide-dependent hydroxyl radical production in vitro. Biol Trace Elem Res 38: 273-287. doi:10.1007/BF02785311. PubMed: 7504944.
    • (1993) Biol Trace Elem Res , vol.38 , pp. 273-287
    • Coudray, C.1    Rachidi, S.2    Favier, A.3
  • 3
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • doi: 10.1126/science.1060331
    • Outten CE, O'Halloran TV, (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292: 2488-2492. doi:10.1126/science.1060331. PubMed: 11397910.
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 4
    • 0030574276 scopus 로고    scopus 로고
    • Bacterial resistances to toxic metal ions--a review
    • doi: 10.1016/S0378-1119(96)00323-X
    • Silver S, (1996) Bacterial resistances to toxic metal ions--a review. Gene 179: 9-19. doi:10.1016/S0378-1119(96)00323-X. PubMed: 8991852.
    • (1996) Gene , vol.179 , pp. 9-19
    • Silver, S.1
  • 5
    • 0025239795 scopus 로고
    • The physiological role of zinc as an antioxidant
    • doi: 10.1016/0891-5849(90)90076-U
    • Bray TM, Bettger WJ, (1990) The physiological role of zinc as an antioxidant. Free Radic Biol Med 8: 281-291. doi:10.1016/0891-5849(90)90076-U. PubMed: 2187766.
    • (1990) Free Radic Biol Med , vol.8 , pp. 281-291
    • Bray, T.M.1    Bettger, W.J.2
  • 6
    • 62649162905 scopus 로고    scopus 로고
    • Regulation and activity of a zinc uptake regulator, Zur, in Corynebacterium diphtheriae
    • doi: 10.1128/JB.01392-08
    • Smith KF, Bibb LA, Schmitt MP, Oram DM, (2009) Regulation and activity of a zinc uptake regulator, Zur, in Corynebacterium diphtheriae. J Bacteriol 191: 1595-1603. doi:10.1128/JB.01392-08. PubMed: 19074382.
    • (2009) J Bacteriol , vol.191 , pp. 1595-1603
    • Smith, K.F.1    Bibb, L.A.2    Schmitt, M.P.3    Oram, D.M.4
  • 8
    • 24944583149 scopus 로고    scopus 로고
    • Transcriptional response of Escherichia coli to external zinc
    • doi: 10.1128/JB.187.18.6333-6340.2005
    • Yamamoto K, Ishihama A, (2005) Transcriptional response of Escherichia coli to external zinc. J Bacteriol 187: 6333-6340. doi:10.1128/JB.187.18.6333-6340.2005. PubMed: 16159766.
    • (2005) J Bacteriol , vol.187 , pp. 6333-6340
    • Yamamoto, K.1    Ishihama, A.2
  • 9
    • 84862513194 scopus 로고    scopus 로고
    • Zinc-induced envelope stress diminishes type III secretion in enteropathogenic Escherichia coli
    • doi: 10.1186/1471-2180-12-123
    • Mellies JL, Thomas K, Turvey M, Evans NR, Crane J, et al. (2012) Zinc-induced envelope stress diminishes type III secretion in enteropathogenic Escherichia coli. BMC Microbiol 12: 123. doi:10.1186/1471-2180-12-123. PubMed: 22727253.
    • (2012) BMC Microbiol , vol.12 , pp. 123
    • Mellies, J.L.1    Thomas, K.2    Turvey, M.3    Evans, N.R.4    Crane, J.5
  • 10
    • 0031798662 scopus 로고    scopus 로고
    • The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli
    • doi: 10.1046/j.1365-2958.1998.00883.x
    • Patzer SI, Hantke K, (1998) The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol Microbiol 28: 1199-1210. doi:10.1046/j.1365-2958.1998.00883.x. PubMed: 9680209.
    • (1998) Mol Microbiol , vol.28 , pp. 1199-1210
    • Patzer, S.I.1    Hantke, K.2
  • 11
    • 34248219997 scopus 로고    scopus 로고
    • Crystal structure and function of the zinc uptake regulator FurB from Mycobacterium tuberculosis
    • doi: 10.1074/jbc.M609974200
    • Lucarelli D, Russo S, Garman E, Milano A, Meyer-Klaucke W, et al. (2007) Crystal structure and function of the zinc uptake regulator FurB from Mycobacterium tuberculosis. J Biol Chem 282: 9914-9922. doi:10.1074/jbc.M609974200. PubMed: 17213192.
    • (2007) J Biol Chem , vol.282 , pp. 9914-9922
    • Lucarelli, D.1    Russo, S.2    Garman, E.3    Milano, A.4    Meyer-Klaucke, W.5
  • 12
    • 0035807029 scopus 로고    scopus 로고
    • Characterization of the metal receptor sites in Escherichia coli Zur, an ultrasensitive zinc(II) metalloregulatory protein
    • doi: 10.1021/bi0155448
    • Outten CE, Tobin DA, Penner-Hahn JE, O'Halloran TV, (2001) Characterization of the metal receptor sites in Escherichia coli Zur, an ultrasensitive zinc(II) metalloregulatory protein. Biochemistry 40: 10417-10423. doi:10.1021/bi0155448. PubMed: 11523983.
    • (2001) Biochemistry , vol.40 , pp. 10417-10423
    • Outten, C.E.1    Tobin, D.A.2    Penner-Hahn, J.E.3    O'Halloran, T.V.4
  • 13
    • 79953212617 scopus 로고    scopus 로고
    • Graded expression of zinc-responsive genes through two regulatory zinc-binding sites in Zur
    • doi: 10.1073/pnas.1017744108
    • Shin JH, Jung HJ, An YJ, Cho YB, Cha SS, et al. (2011) Graded expression of zinc-responsive genes through two regulatory zinc-binding sites in Zur. Proc Natl Acad Sci U S A 108: 5045-5050. doi:10.1073/pnas.1017744108. PubMed: 21383173.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 5045-5050
    • Shin, J.H.1    Jung, H.J.2    An, Y.J.3    Cho, Y.B.4    Cha, S.S.5
  • 14
    • 0034793386 scopus 로고    scopus 로고
    • Common mechanisms for pathogens of plants and animals
    • doi: 10.1146/annurev.phyto.39.1.259
    • Cao H, Baldini RL, Rahme LG, (2001) Common mechanisms for pathogens of plants and animals. Annu Rev Phytopathol 39: 259-284. doi:10.1146/annurev.phyto.39.1.259. PubMed: 11701866.
    • (2001) Annu Rev Phytopathol , vol.39 , pp. 259-284
    • Cao, H.1    Baldini, R.L.2    Rahme, L.G.3
  • 15
    • 0035685108 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa PAO1 kills Caenorhabditis elegans by cyanide poisoning
    • doi: 10.1128/JB.183.21.6207-6214.2001
    • Gallagher LA, Manoil C, (2001) Pseudomonas aeruginosa PAO1 kills Caenorhabditis elegans by cyanide poisoning. J Bacteriol 183: 6207-6214. doi:10.1128/JB.183.21.6207-6214.2001. PubMed: 11591663.
    • (2001) J Bacteriol , vol.183 , pp. 6207-6214
    • Gallagher, L.A.1    Manoil, C.2
  • 16
    • 3042550379 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa pyocyanin is critical for lung infection in mice
    • doi: 10.1128/IAI.72.7.4275-4278.2004
    • Lau GW, Ran H, Kong F, Hassett DJ, Mavrodi D, (2004) Pseudomonas aeruginosa pyocyanin is critical for lung infection in mice. Infect Immun 72: 4275-4278. doi:10.1128/IAI.72.7.4275-4278.2004. PubMed: 15213173.
    • (2004) Infect Immun , vol.72 , pp. 4275-4278
    • Lau, G.W.1    Ran, H.2    Kong, F.3    Hassett, D.J.4    Mavrodi, D.5
  • 17
    • 0033534534 scopus 로고    scopus 로고
    • Molecular mechanisms of bacterial virulence elucidated using a Pseudomonas aeruginosa-Caenorhabditis elegans pathogenesis model
    • doi: 10.1016/S0092-8674(00)80958-7
    • Mahajan-Miklos S, Tan MW, Rahme LG, Ausubel FM, (1999) Molecular mechanisms of bacterial virulence elucidated using a Pseudomonas aeruginosa-Caenorhabditis elegans pathogenesis model. Cell 96: 47-56. doi:10.1016/S0092-8674(00)80958-7. PubMed: 9989496.
    • (1999) Cell , vol.96 , pp. 47-56
    • Mahajan-Miklos, S.1    Tan, M.W.2    Rahme, L.G.3    Ausubel, F.M.4
  • 18
    • 0030725506 scopus 로고    scopus 로고
    • Use of model plant hosts to identify Pseudomonas aeruginosa virulence factors
    • doi: 10.1073/pnas.94.24.13245
    • Rahme LG, Tan MW, Le L, Wong SM, Tompkins RG, et al. (1997) Use of model plant hosts to identify Pseudomonas aeruginosa virulence factors. Proc Natl Acad Sci U S A 94: 13245-13250. doi:10.1073/pnas.94.24.13245. PubMed: 9371831.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 13245-13250
    • Rahme, L.G.1    Tan, M.W.2    Le, L.3    Wong, S.M.4    Tompkins, R.G.5
  • 19
    • 0028914085 scopus 로고
    • Early pulmonary inflammation in infants with cystic fibrosis
    • doi: 10.1164/ajrccm/151.4.1075
    • Khan TZ, Wagener JS, Bost T, Martinez J, Accurso FJ, et al. (1995) Early pulmonary inflammation in infants with cystic fibrosis. Am J Respir Crit Care Med 151: 1075-1082. doi:10.1164/ajrccm/151.4.1075. PubMed: 7697234.
    • (1995) Am J Respir Crit Care Med , vol.151 , pp. 1075-1082
    • Khan, T.Z.1    Wagener, J.S.2    Bost, T.3    Martinez, J.4    Accurso, F.J.5
  • 20
    • 67649523525 scopus 로고    scopus 로고
    • Characterization of Zur-dependent genes and direct Zur targets in Yersinia pestis
    • doi: 10.1186/1471-2180-9-128
    • Li Y, Qiu Y, Gao H, Guo Z, Han Y, et al. (2009) Characterization of Zur-dependent genes and direct Zur targets in Yersinia pestis. BMC Microbiol 9: 128. doi:10.1186/1471-2180-9-128. PubMed: 19552825.
    • (2009) BMC Microbiol , vol.9 , pp. 128
    • Li, Y.1    Qiu, Y.2    Gao, H.3    Guo, Z.4    Han, Y.5
  • 21
    • 0036889038 scopus 로고    scopus 로고
    • Functions required for extracellular quinolone signaling by Pseudomonas aeruginosa
    • doi: 10.1128/JB.184.23.6472-6480.2002
    • Gallagher LA, McKnight SL, Kuznetsova MS, Pesci EC, Manoil C, (2002) Functions required for extracellular quinolone signaling by Pseudomonas aeruginosa. J Bacteriol 184: 6472-6480. doi:10.1128/JB.184.23.6472-6480.2002. PubMed: 12426334.
    • (2002) J Bacteriol , vol.184 , pp. 6472-6480
    • Gallagher, L.A.1    McKnight, S.L.2    Kuznetsova, M.S.3    Pesci, E.C.4    Manoil, C.5
  • 22
    • 33747082622 scopus 로고    scopus 로고
    • The phenazine pyocyanin is a terminal signalling factor in the quorum sensing network of Pseudomonas aeruginosa
    • doi: 10.1111/j.1365-2958.2006.05306.x
    • Dietrich LE, Price-Whelan A, Petersen A, Whiteley M, Newman DK, (2006) The phenazine pyocyanin is a terminal signalling factor in the quorum sensing network of Pseudomonas aeruginosa. Mol Microbiol 61: 1308-1321. doi:10.1111/j.1365-2958.2006.05306.x. PubMed: 16879411.
    • (2006) Mol Microbiol , vol.61 , pp. 1308-1321
    • Dietrich, L.E.1    Price-Whelan, A.2    Petersen, A.3    Whiteley, M.4    Newman, D.K.5
  • 23
    • 78751693014 scopus 로고    scopus 로고
    • Role of a Zn-independent DksA in Zn homeostasis and stringent response
    • doi: 10.1111/j.1365-2958.2010.07475.x
    • Blaby-Haas CE, Furman R, Rodionov DA, Artsimovitch I, de Crécy-Lagard V, (2011) Role of a Zn-independent DksA in Zn homeostasis and stringent response. Mol Microbiol 79: 700-715. doi:10.1111/j.1365-2958.2010.07475.x. PubMed: 21255113.
    • (2011) Mol Microbiol , vol.79 , pp. 700-715
    • Blaby-Haas, C.E.1    Furman, R.2    Rodionov, D.A.3    Artsimovitch, I.4    de Crécy-Lagard, V.5
  • 24
    • 63849313566 scopus 로고    scopus 로고
    • A P-type ATPase importer that discriminates between essential and toxic transition metals
    • doi: 10.1073/pnas.0900666106
    • Lewinson O, Lee AT, Rees DC, (2009) A P-type ATPase importer that discriminates between essential and toxic transition metals. Proc Natl Acad Sci U S A 106: 4677-4682. doi:10.1073/pnas.0900666106. PubMed: 19264958.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 4677-4682
    • Lewinson, O.1    Lee, A.T.2    Rees, D.C.3
  • 25
    • 0032884944 scopus 로고    scopus 로고
    • Identification of a gene cluster, czr, involved in cadmium and zinc resistance in Pseudomonas aeruginosa
    • doi: 10.1016/S0378-1119(99)00349-2
    • Hassan MT, van der Lelie D, Springael D, Römling U, Ahmed N, et al. (1999) Identification of a gene cluster, czr, involved in cadmium and zinc resistance in Pseudomonas aeruginosa. Gene 238: 417-425. doi:10.1016/S0378-1119(99)00349-2. PubMed: 10570969.
    • (1999) Gene , vol.238 , pp. 417-425
    • Hassan, M.T.1    van der Lelie, D.2    Springael, D.3    Römling, U.4    Ahmed, N.5
  • 26
    • 77949409266 scopus 로고    scopus 로고
    • The Zur-regulated ZinT protein is an auxiliary component of the high-affinity ZnuABC zinc transporter that facilitates metal recruitment during severe zinc shortage
    • doi: 10.1128/JB.01310-09
    • Petrarca P, Ammendola S, Pasquali P, Battistoni A, (2010) The Zur-regulated ZinT protein is an auxiliary component of the high-affinity ZnuABC zinc transporter that facilitates metal recruitment during severe zinc shortage. J Bacteriol 192: 1553-1564. doi:10.1128/JB.01310-09. PubMed: 20097857.
    • (2010) J Bacteriol , vol.192 , pp. 1553-1564
    • Petrarca, P.1    Ammendola, S.2    Pasquali, P.3    Battistoni, A.4
  • 27
    • 77957684250 scopus 로고    scopus 로고
    • An outer membrane receptor of Neisseria meningitidis involved in zinc acquisition with vaccine potential
    • PubMed: 20617164
    • Stork M, Bos MP, Jongerius I, de Kok N, Schilders I, et al. (2010) An outer membrane receptor of Neisseria meningitidis involved in zinc acquisition with vaccine potential. PLOS Pathog 6: e1000969. PubMed: 20617164.
    • (2010) PLOS Pathog , vol.6
    • Stork, M.1    Bos, M.P.2    Jongerius, I.3    de Kok, N.4    Schilders, I.5
  • 28
    • 48349136542 scopus 로고    scopus 로고
    • The Zur of Xanthomonas campestris functions as a repressor and an activator of putative zinc homeostasis genes via recognizing two distinct sequences within its target promoters
    • doi: 10.1093/nar/gkn328
    • Huang DL, Tang DJ, Liao Q, Li HC, Chen Q, et al. (2008) The Zur of Xanthomonas campestris functions as a repressor and an activator of putative zinc homeostasis genes via recognizing two distinct sequences within its target promoters. Nucleic Acids Res 36: 4295-4309. doi:10.1093/nar/gkn328. PubMed: 18586823.
    • (2008) Nucleic Acids Res , vol.36 , pp. 4295-4309
    • Huang, D.L.1    Tang, D.J.2    Liao, Q.3    Li, H.C.4    Chen, Q.5
  • 29
    • 61349122680 scopus 로고    scopus 로고
    • The Zur of Xanthomonas campestris is involved in hypersensitive response and positively regulates the expression of the hrp cluster via hrpX but not hrpG
    • doi: 10.1094/MPMI-22-3-0321
    • Huang DL, Tang DJ, Liao Q, Li XQ, He YQ, et al. (2009) The Zur of Xanthomonas campestris is involved in hypersensitive response and positively regulates the expression of the hrp cluster via hrpX but not hrpG. Mol Plant Microbe Interact 22: 321-329. doi:10.1094/MPMI-22-3-0321. PubMed: 19245326.
    • (2009) Mol Plant Microbe Interact , vol.22 , pp. 321-329
    • Huang, D.L.1    Tang, D.J.2    Liao, Q.3    Li, X.Q.4    He, Y.Q.5
  • 30
    • 33846640080 scopus 로고    scopus 로고
    • Global analysis of the Mycobacterium tuberculosis Zur (FurB) regulon
    • doi: 10.1128/JB.01190-06
    • Maciag A, Dainese E, Rodriguez GM, Milano A, Provvedi R, et al. (2007) Global analysis of the Mycobacterium tuberculosis Zur (FurB) regulon. J Bacteriol 189: 730-740. doi:10.1128/JB.01190-06. PubMed: 17098899.
    • (2007) J Bacteriol , vol.189 , pp. 730-740
    • Maciag, A.1    Dainese, E.2    Rodriguez, G.M.3    Milano, A.4    Provvedi, R.5
  • 31
    • 73649136810 scopus 로고    scopus 로고
    • The zinc-responsive regulator Zur controls expression of the coelibactin gene cluster in Streptomyces coelicolor
    • doi: 10.1128/JB.01022-09
    • Kallifidas D, Pascoe B, Owen GA, Strain-Damerell CM, Hong HJ, et al. (2010) The zinc-responsive regulator Zur controls expression of the coelibactin gene cluster in Streptomyces coelicolor. J Bacteriol 192: 608-611. doi:10.1128/JB.01022-09. PubMed: 19915027.
    • (2010) J Bacteriol , vol.192 , pp. 608-611
    • Kallifidas, D.1    Pascoe, B.2    Owen, G.A.3    Strain-Damerell, C.M.4    Hong, H.J.5
  • 32
    • 70349125919 scopus 로고    scopus 로고
    • Contributions of Zur-controlled ribosomal proteins to growth under zinc starvation conditions
    • doi: 10.1128/JB.00802-09
    • Gabriel SE, Helmann JD, (2009) Contributions of Zur-controlled ribosomal proteins to growth under zinc starvation conditions. J Bacteriol 191: 6116-6122. doi:10.1128/JB.00802-09. PubMed: 19648245.
    • (2009) J Bacteriol , vol.191 , pp. 6116-6122
    • Gabriel, S.E.1    Helmann, J.D.2
  • 33
    • 47049087429 scopus 로고    scopus 로고
    • Regulation of the Bacillus subtilis yciC gene and insights into the DNA-binding specificity of the zinc-sensing metalloregulator Zur
    • doi: 10.1128/JB.01978-07
    • Gabriel SE, Miyagi F, Gaballa A, Helmann JD, (2008) Regulation of the Bacillus subtilis yciC gene and insights into the DNA-binding specificity of the zinc-sensing metalloregulator Zur. J Bacteriol 190: 3482-3488. doi:10.1128/JB.01978-07. PubMed: 18344368.
    • (2008) J Bacteriol , vol.190 , pp. 3482-3488
    • Gabriel, S.E.1    Miyagi, F.2    Gaballa, A.3    Helmann, J.D.4
  • 34
    • 0035225012 scopus 로고    scopus 로고
    • Two C or not two C: recurrent disruption of Zn-ribbons, gene duplication, lineage-specific gene loss, and horizontal gene transfer in evolution of bacterial ribosomal proteins
    • RESEARCH 0033
    • Makarova KS, Ponomarev VA, Koonin EV, (2001) Two C or not two C: recurrent disruption of Zn-ribbons, gene duplication, lineage-specific gene loss, and horizontal gene transfer in evolution of bacterial ribosomal proteins. Genome Biol 2RESEARCH 0033.
    • (2001) Genome Biol , vol.2
    • Makarova, K.S.1    Ponomarev, V.A.2    Koonin, E.V.3
  • 35
    • 0043193943 scopus 로고    scopus 로고
    • Comparative genomics of bacterial zinc regulons: enhanced ion transport, pathogenesis, and rearrangement of ribosomal proteins
    • doi: 10.1073/pnas.1733691100
    • Panina EM, Mironov AA, Gelfand MS, (2003) Comparative genomics of bacterial zinc regulons: enhanced ion transport, pathogenesis, and rearrangement of ribosomal proteins. Proc Natl Acad Sci U S A 100: 9912-9917. doi:10.1073/pnas.1733691100. PubMed: 12904577.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 9912-9917
    • Panina, E.M.1    Mironov, A.A.2    Gelfand, M.S.3
  • 36
    • 0000640710 scopus 로고    scopus 로고
    • Modulation of chemical composition and other parameters of the cell by growth rate
    • FC Neidhardt; Rci JL.Ingraham ECC, Lin KB, Low B, Magasanik WS, Rezinkoff M et al., Editors, 2nd ed. Washington, D.C.: ASM Press
    • Bremer H, Dennis PP, (1996) Modulation of chemical composition and other parameters of the cell by growth rate. In: FC Neidhardt; Rci JL.Ingraham ECC, Lin KB, Low B, Magasanik WS, Rezinkoff M et al., Editors. Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. Washington, D.C.: ASM Press. pp. 1553-1569.
    • (1996) Escherichia coli and Salmonella: Cellular and molecular biology , pp. 1553-1569
    • Bremer, H.1    Dennis, P.P.2
  • 37
    • 36749092727 scopus 로고    scopus 로고
    • High-affinity Zn2+ uptake system ZnuABC is required for bacterial zinc homeostasis in intracellular environments and contributes to the virulence of Salmonella enterica
    • doi: 10.1128/IAI.00559-07
    • Ammendola S, Pasquali P, Pistoia C, Petrucci P, Petrarca P, et al. (2007) High-affinity Zn2+ uptake system ZnuABC is required for bacterial zinc homeostasis in intracellular environments and contributes to the virulence of Salmonella enterica. Infect Immun 75: 5867-5876. doi:10.1128/IAI.00559-07. PubMed: 17923515.
    • (2007) Infect Immun , vol.75 , pp. 5867-5876
    • Ammendola, S.1    Pasquali, P.2    Pistoia, C.3    Petrucci, P.4    Petrarca, P.5
  • 38
    • 0036073696 scopus 로고    scopus 로고
    • Role of the high-affinity zinc uptake znuABC system in Salmonella enterica serovar typhimurium virulence
    • doi: 10.1128/IAI.70.8.4721-4725.2002
    • Campoy S, Jara M, Busquets N, Pérez De Rozas AM, Badiola I, et al. (2002) Role of the high-affinity zinc uptake znuABC system in Salmonella enterica serovar typhimurium virulence. Infect Immun 70: 4721-4725. doi:10.1128/IAI.70.8.4721-4725.2002. PubMed: 12117991.
    • (2002) Infect Immun , vol.70 , pp. 4721-4725
    • Campoy, S.1    Jara, M.2    Busquets, N.3    Pérez De Rozas, A.M.4    Badiola, I.5
  • 39
    • 62649160554 scopus 로고    scopus 로고
    • A Campylobacter jejuni znuA orthologue is essential for growth in low-zinc environments and chick colonization
    • doi: 10.1128/JB.01394-08
    • Davis LM, Kakuda T, DiRita VJ, (2009) A Campylobacter jejuni znuA orthologue is essential for growth in low-zinc environments and chick colonization. J Bacteriol 191: 1631-1640. doi:10.1128/JB.01394-08. PubMed: 19103921.
    • (2009) J Bacteriol , vol.191 , pp. 1631-1640
    • Davis, L.M.1    Kakuda, T.2    DiRita, V.J.3
  • 40
    • 16544379238 scopus 로고    scopus 로고
    • Zinc uptake system (znuA locus) of Brucella abortus is essential for intracellular survival and virulence in mice
    • doi: 10.1292/jvms.66.1059
    • Kim S, Watanabe K, Shirahata T, Watarai M, (2004) Zinc uptake system (znuA locus) of Brucella abortus is essential for intracellular survival and virulence in mice. J Vet Med Sci 66: 1059-1063. doi:10.1292/jvms.66.1059. PubMed: 15472468.
    • (2004) J Vet Med Sci , vol.66 , pp. 1059-1063
    • Kim, S.1    Watanabe, K.2    Shirahata, T.3    Watarai, M.4
  • 41
    • 0032858031 scopus 로고    scopus 로고
    • Identification of the znuA-encoded periplasmic zinc transport protein of Haemophilus ducreyi
    • doi: 10496878
    • Lewis DA, Klesney-Tait J, Lumbley SR, Ward CK, Latimer JL, et al. (1999) Identification of the znuA-encoded periplasmic zinc transport protein of Haemophilus ducreyi. Infect Immun 67: 5060-5068. PubMed: 10496878.
    • (1999) Infect Immun , vol.67 , pp. 5060-5068
    • Lewis, D.A.1    Klesney-Tait, J.2    Lumbley, S.R.3    Ward, C.K.4    Latimer, J.L.5
  • 42
    • 62449171768 scopus 로고    scopus 로고
    • Roles of the extraintestinal pathogenic Escherichia coli ZnuACB and ZupT zinc transporters during urinary tract infection
    • doi: 10.1128/IAI.01082-08
    • Sabri M, Houle S, Dozois CM, (2009) Roles of the extraintestinal pathogenic Escherichia coli ZnuACB and ZupT zinc transporters during urinary tract infection. Infect Immun 77: 1155-1164. doi:10.1128/IAI.01082-08. PubMed: 19103764.
    • (2009) Infect Immun , vol.77 , pp. 1155-1164
    • Sabri, M.1    Houle, S.2    Dozois, C.M.3
  • 43
    • 67650084636 scopus 로고    scopus 로고
    • The metal homeostasis protein, Lsp, of Streptococcus pyogenes is necessary for acquisition of zinc and virulence
    • doi: 10.1128/IAI.01299-08
    • Weston BF, Brenot A, Caparon MG, (2009) The metal homeostasis protein, Lsp, of Streptococcus pyogenes is necessary for acquisition of zinc and virulence. Infect Immun 77: 2840-2848. doi:10.1128/IAI.01299-08. PubMed: 19398546.
    • (2009) Infect Immun , vol.77 , pp. 2840-2848
    • Weston, B.F.1    Brenot, A.2    Caparon, M.G.3
  • 44
    • 78649931834 scopus 로고    scopus 로고
    • Znu is the predominant zinc importer in Yersinia pestis during in vitro growth but is not essential for virulence
    • doi: 10.1128/IAI.00732-10
    • Desrosiers DC, Bearden SW, Mier I Jr., Abney J, Paulley JT, et al. (2010) Znu is the predominant zinc importer in Yersinia pestis during in vitro growth but is not essential for virulence. Infect Immun 78: 5163-5177. doi:10.1128/IAI.00732-10. PubMed: 20855510.
    • (2010) Infect Immun , vol.78 , pp. 5163-5177
    • Desrosiers, D.C.1    Bearden, S.W.2    Mier Jr., I.3    Abney, J.4    Paulley, J.T.5
  • 47
    • 55749096264 scopus 로고    scopus 로고
    • PqsE functions independently of PqsR-Pseudomonas quinolone signal and enhances the rhl quorum-sensing system
    • doi: 10.1128/JB.00753-08
    • Farrow JM 3rd, Sund ZM, Ellison ML, Wade DS, Coleman JP, et al. (2008) PqsE functions independently of PqsR-Pseudomonas quinolone signal and enhances the rhl quorum-sensing system. J Bacteriol 190: 7043-7051. doi:10.1128/JB.00753-08. PubMed: 18776012.
    • (2008) J Bacteriol , vol.190 , pp. 7043-7051
    • Farrow 3rd, J.M.1    Sund, Z.M.2    Ellison, M.L.3    Wade, D.S.4    Coleman, J.P.5
  • 48
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension
    • doi: 10.1016/0378-1119(89)90359-4
    • Horton RM, Hunt HD, Ho SN, Pullen JK, Pease LR, (1989) Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77: 61-68. doi:10.1016/0378-1119(89)90359-4. PubMed: 2744488.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 49
    • 32244448730 scopus 로고    scopus 로고
    • A 10-min method for preparation of highly electrocompetent Pseudomonas aeruginosa cells: application for DNA fragment transfer between chromosomes and plasmid transformation
    • doi: 10.1016/j.mimet.2005.06.001
    • Choi KH, Kumar A, Schweizer HP, (2006) A 10-min method for preparation of highly electrocompetent Pseudomonas aeruginosa cells: application for DNA fragment transfer between chromosomes and plasmid transformation. J Microbiol Methods 64: 391-397. doi:10.1016/j.mimet.2005.06.001. PubMed: 15987659.
    • (2006) J Microbiol Methods , vol.64 , pp. 391-397
    • Choi, K.H.1    Kumar, A.2    Schweizer, H.P.3
  • 50
    • 33749531431 scopus 로고    scopus 로고
    • mini-Tn7 insertion in bacteria with single attTn7 sites: example Pseudomonas aeruginosa
    • doi: 10.1038/nprot.2006.24
    • Choi KH, Schweizer HP, (2006) mini-Tn7 insertion in bacteria with single attTn7 sites: example Pseudomonas aeruginosa. Nat Protoc 1: 153-161. doi:10.1038/nprot.2006.24. PubMed: 17406227.
    • (2006) Nat Protoc , vol.1 , pp. 153-161
    • Choi, K.H.1    Schweizer, H.P.2
  • 51
    • 0042121237 scopus 로고    scopus 로고
    • Multiple sequence alignment with the Clustal series of programs
    • doi: 10.1093/nar/gkg500
    • Chenna R, Sugawara H, Koike T, Lopez R, Gibson TJ, et al. (2003) Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Res 31: 3497-3500. doi:10.1093/nar/gkg500. PubMed: 12824352.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3497-3500
    • Chenna, R.1    Sugawara, H.2    Koike, T.3    Lopez, R.4    Gibson, T.J.5
  • 52
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • doi: 10.1093/nar/29.9.e45
    • Pfaffl MW, (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29: e45. doi:10.1093/nar/29.9.e45. PubMed: 11328886.
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1
  • 53
    • 84855395229 scopus 로고    scopus 로고
    • KynR, a Lrp/AsnC-type transcriptional regulator, directly controls the kynurenine pathway in Pseudomonas aeruginosa
    • doi: 10.1128/JB.05803-11
    • Knoten CA, Hudson LL, Coleman JP, Farrow JM 3rd, Pesci EC, (2011) KynR, a Lrp/AsnC-type transcriptional regulator, directly controls the kynurenine pathway in Pseudomonas aeruginosa. J Bacteriol 193: 6567-6575. doi:10.1128/JB.05803-11. PubMed: 21965577.
    • (2011) J Bacteriol , vol.193 , pp. 6567-6575
    • Knoten, C.A.1    Hudson, L.L.2    Coleman, J.P.3    Farrow 3rd, J.M.4    Pesci, E.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.