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Volumn 6, Issue 2, 2015, Pages

The ferrous iron-responsive BqsRS two-component system activates genes that promote cationic stress tolerance

Author keywords

[No Author keywords available]

Indexed keywords

AMINOGLYCOSIDE; FERROUS ION; POLYMYXIN; POLYMYXIN B; SPERMIDINE; TOBRAMYCIN; ANTIINFECTIVE AGENT; BACTERIAL DNA; BACTERIAL PROTEIN; CATION; IRON;

EID: 84929995205     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.02549-14     Document Type: Article
Times cited : (35)

References (88)
  • 1
    • 0038352097 scopus 로고    scopus 로고
    • The role of Fe-S proteins in sensing and regulation in bacteria
    • Kiley PJ, Beinert H. 2003. The role of Fe-S proteins in sensing and regulation in bacteria. Curr Opin Microbiol 6:181–185.http://dx.doi.org/10.1016/S1369-5274(03)00039-0.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 181-185
    • Kiley, P.J.1    Beinert, H.2
  • 2
    • 33646368396 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Ever-expanding roles
    • Fontecave M. 2006. Iron-sulfur clusters: ever-expanding roles. Nat Chem Biol 2:171–174.http://dx.doi.org/10.1038/nchembio0406-171.
    • (2006) Nat Chem Biol , vol.2 , pp. 171-174
    • Fontecave, M.1
  • 3
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill R. 2009. Function and biogenesis of iron-sulphur proteins. Nature 460:831–838.http://dx.doi.org/10.1038/nature08301.
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 4
    • 84856621657 scopus 로고    scopus 로고
    • New insights on iron acquisition mechanisms in pathogenic Pseudomonas
    • In Ramos J-L, Levesque R, Springer, New York, NY
    • Schalk I. 2006. New insights on iron acquisition mechanisms in pathogenic Pseudomonas, p 1831–34. In Ramos J-L, Levesque R (ed), Pseudomonas. Springer, New York, NY.
    • (2006) Pseudomonas , pp. 1831-1834
    • Schalk, I.1
  • 5
    • 23344453820 scopus 로고    scopus 로고
    • Iron and Pseudomonas aeruginosa biofilm formation
    • Banin E, Vasil ML, Greenberg EP. 2005. Iron and Pseudomonas aeruginosa biofilm formation. Proc Natl Acad Sci U S A 102:11076–11081.http://dx.doi.org/10.1073/pnas.0504266102.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 11076-11081
    • Banin, E.1    Vasil, M.L.2    Greenberg, E.P.3
  • 6
    • 38749090228 scopus 로고    scopus 로고
    • Influence of quorum sensing and iron on twitching motility and biofilm formation in Pseudomonas aeruginosa
    • Patriquin GM, Banin E, Gilmour C, Tuchman R, Greenberg EP, Poole K. 2008. Influence of quorum sensing and iron on twitching motility and biofilm formation in Pseudomonas aeruginosa. J Bacteriol 190:662–671.http://dx.doi.org/10.1128/JB.01473-07.
    • (2008) J Bacteriol , vol.190 , pp. 662-671
    • Patriquin, G.M.1    Banin, E.2    Gilmour, C.3    Tuchman, R.4    Greenberg, E.P.5    Poole, K.6
  • 7
    • 0035014383 scopus 로고    scopus 로고
    • Mechanisms of biofilm resistance to antimicrobial agents
    • Mah TF, O’Toole GA. 2001. Mechanisms of biofilm resistance to antimicrobial agents. Trends Microbiol 9:34–39.http://dx.doi.org/10.1016/S0966-842X(00)01913-2.
    • (2001) Trends Microbiol , vol.9 , pp. 34-39
    • Mah, T.F.1    O’Toole, G.A.2
  • 8
    • 0001244969 scopus 로고
    • Oxygenation of ferrous iron
    • Stumm W, Lee GF. 1961. Oxygenation of ferrous iron. Ind Eng Chem 53:143–146.http://dx.doi.org/10.1021/ie50614a030.
    • (1961) Ind Eng Chem , vol.53 , pp. 143-146
    • Stumm, W.1    Lee, G.F.2
  • 9
    • 84857808700 scopus 로고    scopus 로고
    • BqsR/BqsS constitute a two-component system that senses extracellular Fe(II) in Pseudomonas aeruginosa
    • Kreamer NN, Wilks JC, Marlow JJ, Coleman ML, Newman DK. 2012. BqsR/BqsS constitute a two-component system that senses extracellular Fe(II) in Pseudomonas aeruginosa. J Bacteriol 194:1195–1204.http://dx.doi.org/10.1128/JB.05634-11.
    • (2012) J Bacteriol , vol.194 , pp. 1195-1204
    • Kreamer, N.N.1    Wilks, J.C.2    Marlow, J.J.3    Coleman, M.L.4    Newman, D.K.5
  • 10
    • 84869138518 scopus 로고    scopus 로고
    • Characterization of a ferrous iron-responsive two-component system in nontypeable Haemophilus influenzae
    • Steele KH, O’Connor LH, Burpo N, Kohler K, Johnston JW. 2012. Characterization of a ferrous iron-responsive two-component system in nontypeable Haemophilus influenzae. J Bacteriol 194:6162–6173.http://dx.doi.org/10.1128/JB.01465-12.
    • (2012) J Bacteriol , vol.194 , pp. 6162-6173
    • Steele, K.H.1    O’Connor, L.H.2    Burpo, N.3    Kohler, K.4    Johnston, J.W.5
  • 11
    • 84883420466 scopus 로고    scopus 로고
    • Ferrous iron is a significant component of bioavailable iron in cystic fibrosis airways
    • Hunter RC, Asfour F, Dingemans J, Osuna BL, Samad T, Malfroot A, Cornelis P, Newman DK. 2013. Ferrous iron is a significant component of bioavailable iron in cystic fibrosis airways. MBio 4(4):pii: e00557-13.http://dx.doi.org/10.1128/mBio.00557-13.
    • (2013) Mbio , vol.4 , Issue.4
    • Hunter, R.C.1    Asfour, F.2    Dingemans, J.3    Osuna, B.L.4    Samad, T.5    Malfroot, A.6    Cornelis, P.7    Newman, D.K.8
  • 13
    • 33646521973 scopus 로고    scopus 로고
    • Pulmonary function is negatively correlated with sputum inflammatory markers and cough clearability in subjects with cystic fibrosis but not those with chronic bronchitis
    • Kim J-S, Okamoto K, Rubin BK. 2006. Pulmonary function is negatively correlated with sputum inflammatory markers and cough clearability in subjects with cystic fibrosis but not those with chronic bronchitis. Chest 129:1148–1154.http://dx.doi.org/10.1378/chest.129.5.1148.
    • (2006) Chest , vol.129 , pp. 1148-1154
    • Kim, J.-S.1    Okamoto, K.2    Rubin, B.K.3
  • 14
    • 1642409263 scopus 로고    scopus 로고
    • Iron availability, oxygen limitation, Pseudomonas aeruginosa and cystic fibrosis
    • Zeng A-, Kim E-J. 2004. Iron availability, oxygen limitation, Pseudomonas aeruginosa and cystic fibrosis. Microbiology 150:516–518.http://dx.doi.org/10.1099/mic.0.26933-0.
    • (2004) Microbiology , vol.150 , pp. 516-518
    • Zeng, A.1    Kim, E.-J.2
  • 18
    • 0001803997 scopus 로고
    • Transformation of iron in a waterlogged soil as influenced by redox potential and pH
    • Gotoh S, Patrick WH. 1974. Transformation of iron in a waterlogged soil as influenced by redox potential and pH. Soil Sci Soc Am J 38:66–71.http://dx.doi.org/10.2136/sssaj1974.03615995003800010024x.
    • (1974) Soil Sci Soc am J , vol.38 , pp. 66-71
    • Gotoh, S.1    Patrick, W.H.2
  • 19
    • 60149108120 scopus 로고    scopus 로고
    • Regulation of virulence and antibiotic resistance by two-component regulatory systems in Pseudomonas aeruginosa
    • Gooderham WJ, Hancock RE. 2009. Regulation of virulence and antibiotic resistance by two-component regulatory systems in Pseudomonas aeruginosa. FEMS Microbiol Rev 33:279–294.http://dx.doi.org/10.1111/j.1574-6976.2008.00135.x.
    • (2009) FEMS Microbiol Rev , vol.33 , pp. 279-294
    • Gooderham, W.J.1    Hancock, R.E.2
  • 20
    • 78650069076 scopus 로고    scopus 로고
    • A novel two-component system BqsS-BqsR modulates quorum sensingdependent biofilm decay in Pseudomonas aeruginosa
    • Dong Y-H, Zhang X-F, An S-W, Xu J-L, Zhang L-H. 2008. A novel two-component system BqsS-BqsR modulates quorum sensingdependent biofilm decay in Pseudomonas aeruginosa. Commun Integr Biol 1:88–96.http://dx.doi.org/10.4161/cib.1.1.6717.
    • (2008) Commun Integr Biol , vol.1 , pp. 88-96
    • Dong, Y.-H.1    Zhang, X.-F.2    An, S.-W.3    Xu, J.-L.4    Zhang, L.-H.5
  • 21
    • 79958046092 scopus 로고    scopus 로고
    • The sensor kinase KinB regulates virulence in acute Pseudomonas aeruginosa infection
    • Chand NS, Lee JS, Clatworthy AE, Golas AJ, Smith RS, Hung DT. 2011. The sensor kinase KinB regulates virulence in acute Pseudomonas aeruginosa infection. J Bacteriol 193:2989–2999.http://dx.doi.org/10.1128/JB.01546-10.
    • (2011) J Bacteriol , vol.193 , pp. 2989-2999
    • Chand, N.S.1    Lee, J.S.2    Clatworthy, A.E.3    Golas, A.J.4    Smith, R.S.5    Hung, D.T.6
  • 22
    • 0000207681 scopus 로고
    • TMbase—a database of membrane spanning proteins segments
    • Hofmann K, Stoffel, W. 1993. TMbase—a database of membrane spanning proteins segments. Biol Chem Hoppe Seyler 374:166.
    • (1993) Biol Chem Hoppe Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 23
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: The dense alignment surface method
    • Cserzö M, Wallin E, Simon I, von Heijne G, Elofsson A. 1997. Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method. Protein Eng 10:673–676.http://dx.doi.org/10.1093/protein/10.6.673.
    • (1997) Protein Eng , vol.10 , pp. 673-676
    • Cserzö, M.1    Wallin, E.2    Simon, I.3    Von Heijne, G.4    Elofsson, A.5
  • 24
    • 0034730333 scopus 로고    scopus 로고
    • A signal transduction system that responds to extracellular iron
    • Wösten MM, Kox LF, Chamnongpol S, Soncini FC, Groisman EA. 2000. A signal transduction system that responds to extracellular iron. Cell 103: 113–125.http://dx.doi.org/10.1016/S0092-8674(00)00092-1.
    • (2000) Cell , vol.103 , pp. 113-125
    • Wösten, M.M.1    Kox, L.F.2    Chamnongpol, S.3    Soncini, F.C.4    Groisman, E.A.5
  • 25
    • 0029921680 scopus 로고    scopus 로고
    • A permease-oxidase complex involved in high-affinity iron uptake in yeast
    • Stearman R, Yuan DS, Yamaguchi-Iwai Y, Klausner RD, Dancis A. 1996. A permease-oxidase complex involved in high-affinity iron uptake in yeast. Science 271:1552–1557.http://dx.doi.org/10.1126/science.271.5255.1552.
    • (1996) Science , vol.271 , pp. 1552-1557
    • Stearman, R.1    Yuan, D.S.2    Yamaguchi-Iwai, Y.3    Klausner, R.D.4    Dancis, A.5
  • 27
    • 77949911836 scopus 로고    scopus 로고
    • Diversity of structure and function of response regulator output domains
    • Galperin MY. 2010. Diversity of structure and function of response regulator output domains. Curr Opin Microbiol 13:150–159.http://dx.doi.org/10.1016/j.mib.2010.01.005.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 150-159
    • Galperin, M.Y.1
  • 28
    • 0024416995 scopus 로고
    • Characterization of OmpR binding sequences in the upstream region of the ompF promoter essential for transcriptional activation
    • Rampersaud A, Norioka S, Inouye M. 1989. Characterization of OmpR binding sequences in the upstream region of the ompF promoter essential for transcriptional activation. J Biol Chem 264:18693–18700.
    • (1989) J Biol Chem , vol.264 , pp. 18693-18700
    • Rampersaud, A.1    Norioka, S.2    Inouye, M.3
  • 29
    • 0036583638 scopus 로고    scopus 로고
    • Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator
    • Blanco AG, Sola M, Gomis-Rüth FX, Coll M. 2002. Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator. Structure 10:701–713.http://dx.doi.org/10.1016/S0969-2126(02)00761-X.
    • (2002) Structure , vol.10 , pp. 701-713
    • Blanco, A.G.1    Sola, M.2    Gomis-Rüth, F.X.3    Coll, M.4
  • 30
    • 34447522106 scopus 로고    scopus 로고
    • Target genes and DNA-binding sites of the response regulator PhoR from Corynebacterium glutamicum
    • Schaaf S, Bott M. 2007. Target genes and DNA-binding sites of the response regulator PhoR from Corynebacterium glutamicum. J Bacteriol 189: 5002–5011.http://dx.doi.org/10.1128/JB.00121-07.
    • (2007) J Bacteriol , vol.189 , pp. 5002-5011
    • Schaaf, S.1    Bott, M.2
  • 31
    • 77955128598 scopus 로고    scopus 로고
    • Mechanisms for activating bacterial RNA polymerase
    • Ghosh T, Bose D, Zhang X. 2010. Mechanisms for activating bacterial RNA polymerase. FEMS Microbiol Rev 34:611–627.http://dx.doi.org/10.1111/j.1574-6976.2010.00239.x.
    • (2010) FEMS Microbiol Rev , vol.34 , pp. 611-627
    • Ghosh, T.1    Bose, D.2    Zhang, X.3
  • 32
    • 0030811369 scopus 로고    scopus 로고
    • Isolation and characterization of rcsB mutations that affect colanic acid capsule synthesis in Escherichia coli K-12
    • Gupte G, Woodward C, Stout V. 1997. Isolation and characterization of rcsB mutations that affect colanic acid capsule synthesis in Escherichia coli K-12. J Bacteriol 179:4328–4335.
    • (1997) J Bacteriol , vol.179 , pp. 4328-4335
    • Gupte, G.1    Woodward, C.2    Stout, V.3
  • 33
    • 0031973725 scopus 로고    scopus 로고
    • Differential expression of the OmpF and OmpC porin proteins in Escherichia coli K-12 depends upon the level of active OmpR
    • Lan C-Y, Igo MM. 1998. Differential expression of the OmpF and OmpC porin proteins in Escherichia coli K-12 depends upon the level of active OmpR. J Bacteriol 180:171–174.
    • (1998) J Bacteriol , vol.180 , pp. 171-174
    • Lan, C.-Y.1    Igo, M.M.2
  • 34
    • 0027162310 scopus 로고
    • Glutamate at the site of phosphor- ylation of nitrogen-regulatory protein NTRC mimics aspartyl-phosphate and activates the protein
    • Klose KE, Weiss DS, Kustu S. 1993. Glutamate at the site of phosphor- ylation of nitrogen-regulatory protein NTRC mimics aspartyl-phosphate and activates the protein. J Mol Biol 232:67–78.http://dx.doi.org/10.1006/jmbi.1993.1370.
    • (1993) J Mol Biol , vol.232 , pp. 67-78
    • Klose, K.E.1    Weiss, D.S.2    Kustu, S.3
  • 35
    • 33749531431 scopus 로고    scopus 로고
    • Mini-Tn7 insertion in bacteria with single attTn7 sites: Example Pseudomonas aeruginosa
    • Choi K-H, Schweizer HP. 2006. Mini-Tn7 insertion in bacteria with single attTn7 sites: example Pseudomonas aeruginosa. Nat Protoc 1:153–161.http://dx.doi.org/10.1038/nprot.2006.24.
    • (2006) Nat Protoc , vol.1 , pp. 153-161
    • Choi, K.-H.1    Schweizer, H.P.2
  • 36
    • 78651267246 scopus 로고    scopus 로고
    • Pseudomonas Genome Database: Improved comparative analysis and population genomics capability for Pseudomonas genomes
    • Winsor GL, Lam DK, Fleming L, Lo R, Whiteside MD, Yu NY, Hancock RE, Brinkman FS. 2011. Pseudomonas Genome Database: improved comparative analysis and population genomics capability for Pseudomonas genomes. Nucleic Acids Res 39:D596–D600.http://dx.doi.org/10.1093/nar/gkq869.
    • (2011) Nucleic Acids Res , vol.39 , pp. D596-D600
    • Winsor, G.L.1    Lam, D.K.2    Fleming, L.3    Lo, R.4    Whiteside, M.D.5    Yu, N.Y.6    Hancock, R.E.7    Brinkman, F.S.8
  • 37
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using David bioinformatics resources
    • da Huang W, Sherman BT, Lempicki RA. 2009. Systematic and integrative analysis of large gene lists using David bioinformatics resources. Nat Protoc 4:44–57.http://dx.doi.org/10.1038/nprot.2008.211.
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • Da Huang, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 38
    • 0032850479 scopus 로고    scopus 로고
    • PhoP–PhoQ homologues in Pseudomonas aeruginosa regulate expression of the outer-membrane protein OprH and polymyxin B resistance
    • Macfarlane EL, Kwasnicka A, Ochs MM, Hancock RE. 1999. PhoP–PhoQ homologues in Pseudomonas aeruginosa regulate expression of the outer-membrane protein OprH and polymyxin B resistance. Mol Microbiol 34:305–316.http://dx.doi.org/10.1046/j.1365-2958.1999.01600.x.
    • (1999) Mol Microbiol , vol.34 , pp. 305-316
    • Macfarlane, E.L.1    Kwasnicka, A.2    Ochs, M.M.3    Hancock, R.E.4
  • 39
    • 12944262276 scopus 로고    scopus 로고
    • Aminoglycoside resistance in Pseudomonas aeruginosa
    • Poole K. 2005. Aminoglycoside resistance in Pseudomonas aeruginosa. Antimicrob Agents Chemother 49:479–487.http://dx.doi.org/10.1128/AAC.49.2.479-487.2005.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 479-487
    • Poole, K.1
  • 40
    • 81555211920 scopus 로고    scopus 로고
    • PhoQ mutations promote lipid A modification and polymyxin resistance of Pseudomonas aeruginosa found in colistin-treated cystic fibrosis patients
    • Miller AK, Brannon MK, Stevens L, Johansen HK, Selgrade SE, Miller SI, Høiby N, Moskowitz SM. 2011. PhoQ mutations promote lipid A modification and polymyxin resistance of Pseudomonas aeruginosa found in colistin-treated cystic fibrosis patients. Antimicrob Agents Chemother 55:5761–5769.http://dx.doi.org/10.1128/AAC.05391-11.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 5761-5769
    • Miller, A.K.1    Brannon, M.K.2    Stevens, L.3    Johansen, H.K.4    Selgrade, S.E.5    Miller, S.I.6    Høiby, N.7    Moskowitz, S.M.8
  • 41
    • 40549096043 scopus 로고    scopus 로고
    • A multifaceted role for polyamines in bacterial pathogens
    • Shah P, Swiatlo E. 2008. A multifaceted role for polyamines in bacterial pathogens. Mol Microbiol 68:4–16.http://dx.doi.org/10.1111/j.1365-2958.2008.06126.x.
    • (2008) Mol Microbiol , vol.68 , pp. 4-16
    • Shah, P.1    Swiatlo, E.2
  • 42
    • 84857089163 scopus 로고    scopus 로고
    • Surfacelocalized spermidine protects the Pseudomonas aeruginosa outer membrane from antibiotic treatment and oxidative stress
    • Johnson L, Mulcahy H, Kanevets U, Shi Y, Lewenza S. 2012. Surfacelocalized spermidine protects the Pseudomonas aeruginosa outer membrane from antibiotic treatment and oxidative stress. J Bacteriol 194: 813–826.http://dx.doi.org/10.1128/JB.05230-11.
    • (2012) J Bacteriol , vol.194 , pp. 813-826
    • Johnson, L.1    Mulcahy, H.2    Kanevets, U.3    Shi, Y.4    Lewenza, S.5
  • 43
    • 0141484326 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides activate a two-component regulatory system, PmrA-PmrB, that regulates resistance to polymyxin B and cationic antimicrobial peptides in Pseudomonas aeruginosa
    • McPhee JB, Lewenza S, Hancock RE. 2003. Cationic antimicrobial peptides activate a two-component regulatory system, PmrA-PmrB, that regulates resistance to polymyxin B and cationic antimicrobial peptides in Pseudomonas aeruginosa. Mol Microbiol 50:205–217.http://dx.doi.org/10.1046/j.1365-2958.2003.03673.x.
    • (2003) Mol Microbiol , vol.50 , pp. 205-217
    • McPhee, J.B.1    Lewenza, S.2    Hancock, R.E.3
  • 44
    • 0346655236 scopus 로고    scopus 로고
    • PmrAB, a two-component regulatory system of Pseudomonas aeruginosa that modulates resistance to cationic antimicrobial peptides and addition of aminoarabinose to lipid A
    • Moskowitz SM, Ernst RK, Miller SI. 2004. PmrAB, a two-component regulatory system of Pseudomonas aeruginosa that modulates resistance to cationic antimicrobial peptides and addition of aminoarabinose to lipid A. J Bacteriol 186:575–579.http://dx.doi.org/10.1128/JB.186.2.575-579.2004.
    • (2004) J Bacteriol , vol.186 , pp. 575-579
    • Moskowitz, S.M.1    Ernst, R.K.2    Miller, S.I.3
  • 45
    • 11444252559 scopus 로고    scopus 로고
    • Sociomicrobiology: The connections between quorum sensing and biofilms
    • Parsek MR, Greenberg EP. 2005. Sociomicrobiology: the connections between quorum sensing and biofilms. Trends Microbiol 13:27–33.http://dx.doi.org/10.1016/j.tim.2004.11.007.
    • (2005) Trends Microbiol , vol.13 , pp. 27-33
    • Parsek, M.R.1    Greenberg, E.P.2
  • 47
    • 84896735766 scopus 로고    scopus 로고
    • Voom: Precision weights unlock linear model analysis tools for RNA-seq read counts
    • Law CW, Chen Y, Shi W, Smyth GK. 2014. voom: precision weights unlock linear model analysis tools for RNA-seq read counts. Genome Biol 15:R29.http://dx.doi.org/10.1186/gb-2014-15-2-r29.
    • (2014) Genome Biol , vol.15 , pp. R29
    • Law, C.W.1    Chen, Y.2    Shi, W.3    Smyth, G.K.4
  • 48
    • 84902251807 scopus 로고    scopus 로고
    • Functional characterization of the potRABCD operon for spermine and spermidine uptake and regulation in Staphylococcus aureus
    • Yao X, Lu C-D. 2014. Functional characterization of the potRABCD operon for spermine and spermidine uptake and regulation in Staphylococcus aureus. Curr Microbiol 69:75–81.http://dx.doi.org/10.1007/s00284-014-0556-1.
    • (2014) Curr Microbiol , vol.69 , pp. 75-81
    • Yao, X.1    Lu, C.-D.2
  • 49
    • 0030660581 scopus 로고    scopus 로고
    • A genomic perspective on protein families
    • Tatusov RL, Koonin EV, Lipman DJ. 1997. A genomic perspective on protein families. Science 278:631–637.http://dx.doi.org/10.1126/science.278.5338.631.
    • (1997) Science , vol.278 , pp. 631-637
    • Tatusov, R.L.1    Koonin, E.V.2    Lipman, D.J.3
  • 50
    • 33646462432 scopus 로고    scopus 로고
    • Polyamines induce resistance to cationic peptide, aminoglycoside, and quinolone antibiotics in Pseudomonas aeruginosa PAO1
    • Kwon DH, Lu C-D. 2006. Polyamines induce resistance to cationic peptide, aminoglycoside, and quinolone antibiotics in Pseudomonas aeruginosa PAO1. Antimicrob Agents Chemother 50:1615–1622.http://dx.doi.org/10.1128/AAC.50.5.1615-1622.2006.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1615-1622
    • Kwon, D.H.1    Lu, C.-D.2
  • 52
    • 2142822839 scopus 로고    scopus 로고
    • Iron blocks the accumulation and activity of tetracyclines in bacteria
    • Avery AM, Goddard HJ, Sumner ER, Avery SV. 2004. Iron blocks the accumulation and activity of tetracyclines in bacteria. Antimicrob Agents Chemother 48:1892–1894.http://dx.doi.org/10.1128/AAC.48.5.1892-1894.2004.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 1892-1894
    • Avery, A.M.1    Goddard, H.J.2    Sumner, E.R.3    Avery, S.V.4
  • 53
    • 84883189863 scopus 로고    scopus 로고
    • Iron binding at specific sites within the octameric HbpS protects Streptomycetes from iron-mediated oxidative stress
    • Wedderhoff I, Kursula I, Groves MR, Ortiz de Orué Lucana D. 2013. Iron binding at specific sites within the octameric HbpS protects Streptomycetes from iron-mediated oxidative stress. PLoS One 8:e71579.http://dx.doi.org/10.1371/journal.pone.0071579.
    • (2013) Plos One , vol.8 , pp. e71579
    • Wedderhoff, I.1    Kursula, I.2    Groves, M.R.3    De Ortiz, D.4
  • 54
    • 44449112421 scopus 로고    scopus 로고
    • Specificity in two-component signal transduction pathways
    • Laub MT, Goulian M. 2007. Specificity in two-component signal transduction pathways. Annu Rev Genet 41:121–145.http://dx.doi.org/10.1146/annurev.genet.41.042007.170548.
    • (2007) Annu Rev Genet , vol.41 , pp. 121-145
    • Laub, M.T.1    Goulian, M.2
  • 56
    • 0033050589 scopus 로고    scopus 로고
    • Effect of O-side-chain-lipopolysaccharide chemistry on metal binding
    • Langley S, Beveridge TJ. 1999. Effect of O-side-chain-lipopolysaccharide chemistry on metal binding. Appl Environ Microbiol 65:489–498.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 489-498
    • Langley, S.1    Beveridge, T.J.2
  • 57
    • 0018566710 scopus 로고
    • Effects of divalent metal cations in the growth medium upon sensitivity of batch-grown Pseudomonas aeruginosa to EDTA or polymyxin B
    • Boggis W, Kenward MA, Brown MR. 1979. Effects of divalent metal cations in the growth medium upon sensitivity of batch-grown Pseudomonas aeruginosa to EDTA or polymyxin B. J Appl Bacteriol 47:477–488.http://dx.doi.org/10.1111/j.1365-2672.1979.tb01209.x.
    • (1979) J Appl Bacteriol , vol.47 , pp. 477-488
    • Boggis, W.1    Kenward, M.A.2    Brown, M.R.3
  • 58
    • 84878594153 scopus 로고    scopus 로고
    • Iron and copper act synergistically to delay anaerobic growth of bacteria
    • Bird LJ, Coleman ML, Newman DK. 2013. Iron and copper act synergistically to delay anaerobic growth of bacteria. Appl Environ Microbiol 79: 3619–3627.http://dx.doi.org/10.1128/AEM.03944-12.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 3619-3627
    • Bird, L.J.1    Coleman, M.L.2    Newman, D.K.3
  • 59
    • 0031964968 scopus 로고    scopus 로고
    • Anaerobic killing of oral streptococci by reduced, transition metal cations
    • Dunning JC, Ma Y, Marquis RE. 1998. Anaerobic killing of oral streptococci by reduced, transition metal cations. Appl Environ Microbiol 64: 27–33.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 27-33
    • Dunning, J.C.1    Ma, Y.2    Marquis, R.E.3
  • 60
    • 70350491397 scopus 로고    scopus 로고
    • Rhodobacter capsulatus catalyzes lightdependent Fe(II) oxidation under anaerobic conditions as a potential detoxification mechanism
    • Poulain AJ, Newman DK. 2009. Rhodobacter capsulatus catalyzes lightdependent Fe(II) oxidation under anaerobic conditions as a potential detoxification mechanism. Appl Environ Microbiol 75:6639–6646.http://dx.doi.org/10.1128/AEM.00054-09.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 6639-6646
    • Poulain, A.J.1    Newman, D.K.2
  • 61
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido H, Vaara M. 1985. Molecular basis of bacterial outer membrane permeability. Microbiol Rev 49:1–32.
    • (1985) Microbiol Rev , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 62
    • 84855386928 scopus 로고    scopus 로고
    • Positive regulation of the Vibrio cholerae porin OmpT by iron and Fur
    • Craig SA, Carpenter CD, Mey AR, Wyckoff EE, Payne SM. 2011. Positive regulation of the Vibrio cholerae porin OmpT by iron and Fur. J Bacteriol 193:6505–6511.http://dx.doi.org/10.1128/JB.05681-11.
    • (2011) J Bacteriol , vol.193 , pp. 6505-6511
    • Craig, S.A.1    Carpenter, C.D.2    Mey, A.R.3    Wyckoff, E.E.4    Payne, S.M.5
  • 63
    • 0034460303 scopus 로고    scopus 로고
    • S-adenosylmethionine decarboxylase from the archaeon Methanococcus jannaschii: Identification of a novel family of pyruvoyl enzymes
    • Kim AD, Graham DE, Seeholzer SH, Markham GD. 2000. S-adenosylmethionine decarboxylase from the archaeon Methanococcus jannaschii: identification of a novel family of pyruvoyl enzymes. J Bacteriol 182:6667–6672.http://dx.doi.org/10.1128/JB.182.23.6667-6672.2000.
    • (2000) J Bacteriol , vol.182 , pp. 6667-6672
    • Kim, A.D.1    Graham, D.E.2    Seeholzer, S.H.3    Markham, G.D.4
  • 64
    • 34447303805 scopus 로고    scopus 로고
    • Metal ion activation of S-adenosylmethionine decarboxylase reflects cation charge density
    • Lu ZJ, Markham GD. 2007. Metal ion activation of S-adenosylmethionine decarboxylase reflects cation charge density. Biochemistry 46: 8172–8180.http://dx.doi.org/10.1021/bi6025962.
    • (2007) Biochemistry , vol.46 , pp. 8172-8180
    • Lu, Z.J.1    Markham, G.D.2
  • 65
    • 0141651685 scopus 로고    scopus 로고
    • Abnormal growth of polyamine-deficient Escherichia coli mutant is partially caused by oxidative stress-induced damage
    • Jung IL, Oh TJ, Kim IG. 2003. Abnormal growth of polyamine-deficient Escherichia coli mutant is partially caused by oxidative stress-induced damage. Arch Biochem Biophys 418:125–132.http://dx.doi.org/10.1016/j.abb.2003.08.003.
    • (2003) Arch Biochem Biophys , vol.418 , pp. 125-132
    • Jung, I.L.1    Oh, T.J.2    Kim, I.G.3
  • 66
    • 0142116431 scopus 로고    scopus 로고
    • Polyamines as modulators of gene expression under oxidative stress in Escherichia coli
    • Tkachenko AG, Nesterova LY. 2003. Polyamines as modulators of gene expression under oxidative stress in Escherichia coli. Biochemistry 68: 850–856.http://dx.doi.org/10.1007/s002030100301.
    • (2003) Biochemistry , vol.68 , pp. 850-856
    • Tkachenko, A.G.1    Nesterova, L.Y.2
  • 67
    • 33744775995 scopus 로고    scopus 로고
    • Contribution of the PhoP-PhoQ and PmrA-PmrB two-component regulatory systems to Mg2+-induced gene regulation in Pseudomonas aeruginosa
    • McPhee JB, Bains M, Winsor G, Lewenza S, Kwasnicka A, Brazas MD, Brinkman FS, Hancock RE. 2006. Contribution of the PhoP-PhoQ and PmrA-PmrB two-component regulatory systems to Mg2+-induced gene regulation in Pseudomonas aeruginosa. J Bacteriol 188:3995–4006.http://dx.doi.org/10.1128/JB.00053-06.
    • (2006) J Bacteriol , vol.188 , pp. 3995-4006
    • McPhee, J.B.1    Bains, M.2    Winsor, G.3    Lewenza, S.4    Kwasnicka, A.5    Brazas, M.D.6    Brinkman, F.S.7    Hancock, R.E.8
  • 69
    • 84907690161 scopus 로고    scopus 로고
    • Insights into novel antimicrobial compounds and antibiotic resistance genes from soil metagenomes
    • de Castro AP, Fernandes Gda R, Franco OL. 2014. Insights into novel antimicrobial compounds and antibiotic resistance genes from soil metagenomes. Front Microbiol 5:489.http://dx.doi.org/10.3389/fmicb.2014.00489.
    • (2014) Front Microbiol , vol.5 , pp. 489
    • De Castro, A.P.1    Fernandes Gda, R.2    Franco, O.L.3
  • 70
    • 0037031882 scopus 로고    scopus 로고
    • DsbB catalyzes disulfide bond formation de novo
    • Regeimbal J, Bardwell JC. 2002. DsbB catalyzes disulfide bond formation de novo. J Biol Chem 277:32706–32713.http://dx.doi.org/10.1074/jbc.M205433200.
    • (2002) J Biol Chem , vol.277 , pp. 32706-32713
    • Regeimbal, J.1    Bardwell, J.C.2
  • 71
    • 33947182874 scopus 로고    scopus 로고
    • The HP0165- HP0166 two-component system (ArsRS) regulates acid-induced expression of HP1186 +-carbonic anhydrase in Helicobacter pylori by activating the pH-dependent promoter
    • Wen Y, Feng J, Scott DR, Marcus EA, Sachs G. 2007. The HP0165- HP0166 two-component system (ArsRS) regulates acid-induced expression of HP1186 +-carbonic anhydrase in Helicobacter pylori by activating the pH-dependent promoter. J Bacteriol 189:2426–2434.http://dx.doi.org/10.1128/JB.01492-06.
    • (2007) J Bacteriol , vol.189 , pp. 2426-2434
    • Wen, Y.1    Feng, J.2    Scott, D.R.3    Marcus, E.A.4    Sachs, G.5
  • 72
    • 0035169376 scopus 로고    scopus 로고
    • The clinical use of colistin in patients with cystic fibrosis
    • Beringer P. 2001. The clinical use of colistin in patients with cystic fibrosis. Curr Opin Pulm Med 7:434–440.http://dx.doi.org/10.1097/00063198-200111000-00013.
    • (2001) Curr Opin Pulm Med , vol.7 , pp. 434-440
    • Beringer, P.1
  • 73
    • 84875312524 scopus 로고    scopus 로고
    • Ligand-enhanced abiotic iron oxidation and the effects of chemical versus biological iron cycling in anoxic environments
    • Kopf SH, Henny C, Newman DK. 2013. Ligand-enhanced abiotic iron oxidation and the effects of chemical versus biological iron cycling in anoxic environments. Environ Sci Technol 47:2602–2611.http://dx.doi.org/10.1021/es3049459.
    • (2013) Environ Sci Technol , vol.47 , pp. 2602-2611
    • Kopf, S.H.1    Henny, C.2    Newman, D.K.3
  • 74
    • 33847670407 scopus 로고
    • Ferrozine---a new spectrophotometric reagent for iron
    • Stookey LL. 1970. Ferrozine---a new spectrophotometric reagent for iron. Anal Chem 42:779–781.http://dx.doi.org/10.1021/ac60289a016.
    • (1970) Anal Chem , vol.42 , pp. 779-781
    • Stookey, L.L.1
  • 75
    • 0026512864 scopus 로고
    • Phosphorylation of bacterial response regulator proteins by low molecular weight phosphodonors
    • Lukat GS, McCleary WR, Stock AM, Stock JB. 1992. Phosphorylation of bacterial response regulator proteins by low molecular weight phosphodonors. Proc Natl Acad Sci U S A 89:718–722.http://dx.doi.org/10.1073/pnas.89.2.718.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 718-722
    • Lukat, G.S.1    McCleary, W.R.2    Stock, A.M.3    Stock, J.B.4
  • 76
    • 78650239608 scopus 로고    scopus 로고
    • Regulation of the phototrophic iron oxidation (Pio) genes in Rhodopseudomonas palustris TIE-1 is mediated by the global regulator, FixK
    • Bose A, Newman DK. 2011. Regulation of the phototrophic iron oxidation (pio) genes in Rhodopseudomonas palustris TIE-1 is mediated by the global regulator, FixK. Mol Microbiol 79:63–75.http://dx.doi.org/10.1111/j.1365-2958.2010.07430.x.
    • (2011) Mol Microbiol , vol.79 , pp. 63-75
    • Bose, A.1    Newman, D.K.2
  • 77
    • 0033956060 scopus 로고    scopus 로고
    • The COG database: A tool for genome-scale analysis of protein functions and evolution
    • Tatusov RL, Galperin MY, Natale DA, Koonin EV. 2000. The COG database: a tool for genome-scale analysis of protein functions and evolution. Nucleic Acids Res 28:33–36.http://dx.doi.org/10.1093/nar/28.1.33.
    • (2000) Nucleic Acids Res , vol.28 , pp. 33-36
    • Tatusov, R.L.1    Galperin, M.Y.2    Natale, D.A.3    Koonin, E.V.4
  • 78
    • 0037249633 scopus 로고    scopus 로고
    • The TIGRFAMs database of protein families
    • Haft DH, Selengut JD, White O. 2003. The TIGRFAMs database of protein families. Nucleic Acids Res 31:371–373.http://dx.doi.org/10.1093/nar/gkg128.
    • (2003) Nucleic Acids Res , vol.31 , pp. 371-373
    • Haft, D.H.1    Selengut, J.D.2    White, O.3
  • 82
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz J, Milpetz F, Bork P, Ponting CP. 1998. SMART, a simple modular architecture research tool: identification of signaling domains. Proc Natl Acad Sci U S A 95:5857–5864.http://dx.doi.org/10.1073/pnas.95.11.5857.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 83
    • 84905049901 scopus 로고    scopus 로고
    • Trimmomatic: A flexible trimmer for Illumina sequence data
    • Bolger AM, Lohse M, Usadel B. 2014. Trimmomatic: a flexible trimmer for Illumina sequence data. Bioinformatics 30:2114–2120.http://dx.doi.org/10.1093/bioinformatics/btu170.
    • (2014) Bioinformatics , vol.30 , pp. 2114-2120
    • Bolger, A.M.1    Lohse, M.2    Usadel, B.3
  • 84
    • 62349130698 scopus 로고    scopus 로고
    • Ultrafast and memory-efficient alignment of short DNA sequences to the human genome
    • Langmead B, Trapnell C, Pop M, Salzberg SL. 2009. Ultrafast and memory-efficient alignment of short DNA sequences to the human genome. Genome Biol 10:R25.http://dx.doi.org/10.1186/gb-2009-10-3-r25.
    • (2009) Genome Biol , vol.10 , pp. R25
    • Langmead, B.1    Trapnell, C.2    Pop, M.3    Salzberg, S.L.4
  • 85
    • 68549104404 scopus 로고    scopus 로고
    • The sequence alignment/map format and SAMtools
    • 1000 Genome Project Data Processing Subgroup
    • Li H, Handsaker B, Wysoker A, Fennell T, Ruan J, Homer N, Marth G, Abecasis G, Durbin R, 1000 Genome Project Data Processing Subgroup. 2009. The sequence alignment/map format and SAMtools. Bioinformatics 25:2078–2079.http://dx.doi.org/10.1093/bioinformatics/btp352.
    • (2009) Bioinformatics , vol.25 , pp. 2078-2079
    • Li, H.1    Handsaker, B.2    Wysoker, A.3    Fennell, T.4    Ruan, J.5    Homer, N.6    Marth, G.7    Abecasis, G.8    Durbin, R.9
  • 86
    • 84867318866 scopus 로고    scopus 로고
    • Easyrnaseq: A bioconductor package for processing RNA-Seq data
    • Delhomme N, Padioleau I, Furlong EE, Steinmetz LM. 2012. easyrnaseq: a bioconductor package for processing RNA-Seq data. Bioinformatics 28:2532–2533.http://dx.doi.org/10.1093/bioinformatics/bts477.
    • (2012) Bioinformatics , vol.28 , pp. 2532-2533
    • Delhomme, N.1    Padioleau, I.2    Furlong, E.E.3    Steinmetz, L.M.4
  • 87
    • 33747082622 scopus 로고    scopus 로고
    • The phenazine pyocyanin is a terminal signalling factor in the quorum sensing network of Pseudomonas aeruginosa
    • 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.http://dx.doi.org/10.1111/j.1365-2958.2006.05306.x.
    • (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
  • 88
    • 0023369404 scopus 로고
    • Analysis of polyamines as their dabsyl derivatives by reversed-phase high-performance liquid chromatography
    • Koski P, Helander IM, Sarvas M, Vaara M. 1987. Analysis of polyamines as their dabsyl derivatives by reversed-phase high-performance liquid chromatography. Anal Biochem 164:261–266.http://dx.doi.org/10.1016/0003-2697(87)90395-2.
    • (1987) Anal Biochem , vol.164 , pp. 261-266
    • Koski, P.1    Helander, I.M.2    Sarvas, M.3    Vaara, M.4


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