메뉴 건너뛰기




Volumn 158, Issue 2, 2012, Pages 547-559

Escherichia coli enterobactin synthesis and uptake mutants are hypersensitive to an antimicrobial peptide that limits the availability of iron in addition to blocking Holliday junction resolution

Author keywords

[No Author keywords available]

Indexed keywords

ENTEROCHELIN; FERRIC ION; POLYPEPTIDE ANTIBIOTIC AGENT; RNA; TOLC PROTEIN;

EID: 84856740569     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.054361-0     Document Type: Article
Times cited : (13)

References (52)
  • 2
    • 0023664923 scopus 로고
    • Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli
    • Bagg, A. & Neilands, J. B. (1987). Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli. Biochemistry 26, 5471-5477.
    • (1987) Biochemistry , vol.26 , pp. 5471-5477
    • Bagg, A.1    Neilands, J.B.2
  • 4
    • 20444411178 scopus 로고    scopus 로고
    • DNA-bound redox activity of DNA repair glycosylases containing [4Fe-4S] clusters
    • Boal, A. K., Yavin, E., Lukianova, O. A., O'Shea, V. L., David, S. S. & Barton, J. K. (2005). DNA-bound redox activity of DNA repair glycosylases containing [4Fe-4S] clusters. Biochemistry 44, 8397-8407.
    • (2005) Biochemistry , vol.44 , pp. 8397-8407
    • Boal, A.K.1    Yavin, E.2    Lukianova, O.A.3    O'Shea, V.L.4    David, S.S.5    Barton, J.K.6
  • 5
    • 0942276382 scopus 로고    scopus 로고
    • Reversible inhibitors of lambda integrase-mediated recombination efficiently trap Holliday junction intermediates and form the basis of a novel assay for junction resolution
    • Boldt, J. L., Pinilla, C. & Segall, A. M. (2004). Reversible inhibitors of lambda integrase-mediated recombination efficiently trap Holliday junction intermediates and form the basis of a novel assay for junction resolution. J Biol Chem 279, 3472-3483.
    • (2004) J Biol Chem , vol.279 , pp. 3472-3483
    • Boldt, J.L.1    Pinilla, C.2    Segall, A.M.3
  • 6
    • 0026724913 scopus 로고
    • Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex
    • Brickman, T. J. & McIntosh, M. A. (1992). Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex. J Biol Chem 267, 12350-12355.
    • (1992) J Biol Chem , vol.267 , pp. 12350-12355
    • Brickman, T.J.1    McIntosh, M.A.2
  • 8
    • 0036230974 scopus 로고    scopus 로고
    • Intracellular cyclic AMP concentration is decreased in Salmonella typhimurium fur mutants
    • Campoy, S., Jara, M., Busquets, N., de Rozas, A. M., Badiola, I. & Barbé, J. (2002). Intracellular cyclic AMP concentration is decreased in Salmonella typhimurium fur mutants. Microbiology 148, 1039-1048.
    • (2002) Microbiology , vol.148 , pp. 1039-1048
    • Campoy, S.1    Jara, M.2    Busquets, N.3    de Rozas, A.M.4    Badiola, I.5    Barbé, J.6
  • 9
    • 0029065955 scopus 로고
    • R cassettes with the option of Flpcatalyzed excision of the antibiotic-resistance determinant
    • R cassettes with the option of Flpcatalyzed excision of the antibiotic-resistance determinant. Gene 158, 9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 11
    • 0030200147 scopus 로고    scopus 로고
    • A new isochorismate synthase specifically involved in menaquinone (vitamin K2) biosynthesis encoded by the menF gene
    • Daruwala, R., Kwon, O., Meganathan, R. & Hudspeth, M. E. (1996). A new isochorismate synthase specifically involved in menaquinone (vitamin K2) biosynthesis encoded by the menF gene. FEMS Microbiol Lett 140, 159-163.
    • (1996) FEMS Microbiol Lett , vol.140 , pp. 159-163
    • Daruwala, R.1    Kwon, O.2    Meganathan, R.3    Hudspeth, M.E.4
  • 13
    • 18544384019 scopus 로고
    • Oxidation of tartaric acid in presence of iron
    • Fenton, H. (1894). Oxidation of tartaric acid in presence of iron. J Chem Soc Trans 65, 899.
    • (1894) J Chem Soc Trans , vol.65 , pp. 899
    • Fenton, H.1
  • 14
    • 0035421993 scopus 로고    scopus 로고
    • Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions
    • Forbes, J. R. & Gros, P. (2001). Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions. Trends Microbiol 9, 397-403.
    • (2001) Trends Microbiol , vol.9 , pp. 397-403
    • Forbes, J.R.1    Gros, P.2
  • 15
    • 0036015639 scopus 로고    scopus 로고
    • Export of the siderophore enterobactin in Escherichia coli: Involvement of a 43 kDa membrane exporter
    • Furrer, J. L., Sanders, D. N., Hook-Barnard, I. G. & McIntosh, M. A. (2002). Export of the siderophore enterobactin in Escherichia coli: involvement of a 43 kDa membrane exporter. Mol Microbiol 44, 1225-1234.
    • (2002) Mol Microbiol , vol.44 , pp. 1225-1234
    • Furrer, J.L.1    Sanders, D.N.2    Hook-Barnard, I.G.3    McIntosh, M.A.4
  • 16
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N. & Strong, R. K. (2002). The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol Cell 10, 1033-1043.
    • (2002) Mol Cell , vol.10 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3    Bluhm, M.E.4    Raymond, K.N.5    Strong, R.K.6
  • 17
    • 79951789722 scopus 로고    scopus 로고
    • The SoxRS response of Escherichia coli is directly activated by redox-cycling drugs rather than by superoxide
    • Gu, M. & Imlay, J. A. (2011). The SoxRS response of Escherichia coli is directly activated by redox-cycling drugs rather than by superoxide. Mol Microbiol 79, 1136-1150.
    • (2011) Mol Microbiol , vol.79 , pp. 1136-1150
    • Gu, M.1    Imlay, J.A.2
  • 18
    • 0027945605 scopus 로고
    • Microbial iron transport
    • Guerinot, M. L. (1994). Microbial iron transport. Annu Rev Microbiol 48, 743-772.
    • (1994) Annu Rev Microbiol , vol.48 , pp. 743-772
    • Guerinot, M.L.1
  • 19
    • 33645051465 scopus 로고    scopus 로고
    • DNA repair, a novel antibacterial target: Holliday junction-trapping peptides induce DNA damage and chromosome segregation defects
    • Gunderson, C. W. & Segall, A. M. (2006). DNA repair, a novel antibacterial target: Holliday junction-trapping peptides induce DNA damage and chromosome segregation defects. Mol Microbiol 59, 1129-1148.
    • (2006) Mol Microbiol , vol.59 , pp. 1129-1148
    • Gunderson, C.W.1    Segall, A.M.2
  • 20
    • 64049098351 scopus 로고    scopus 로고
    • Peptide wrwycr inhibits the excision of several prophages and traps Holliday junctions inside bacteria
    • Gunderson, C. W., Boldt, J. L., Authement, R. N. & Segall, A. M. (2009). Peptide wrwycr inhibits the excision of several prophages and traps Holliday junctions inside bacteria. J Bacteriol 191, 2169-2176.
    • (2009) J Bacteriol , vol.191 , pp. 2169-2176
    • Gunderson, C.W.1    Boldt, J.L.2    Authement, R.N.3    Segall, A.M.4
  • 21
    • 34250942854 scopus 로고
    • Über die Katalyse des Hydroperoxydes
    • Haber, F. & Weiss, J. (1932). Über die Katalyse des Hydroperoxydes. Naturwiss 20, 948-950.
    • (1932) Naturwiss , vol.20 , pp. 948-950
    • Haber, F.1    Weiss, J.2
  • 22
    • 0000162325 scopus 로고
    • The catalytic decomposition of hydrogen peroxide by iron salts
    • Haber, F. & Weiss, J. (1934). The catalytic decomposition of hydrogen peroxide by iron salts. Proc R Soc Lond A Math Phys Sci 147, 332-351.
    • (1934) Proc R Soc Lond a Math Phys Sci , vol.147 , pp. 332-351
    • Haber, F.1    Weiss, J.2
  • 23
    • 85163178998 scopus 로고
    • Unpaarigkeit und Radikalketten im Reaktionsmechanismus organischer und enzymatischer Vorgänge
    • Haber, F. & Willstätter, R. (1931). Unpaarigkeit und Radikalketten im Reaktionsmechanismus organischer und enzymatischer Vorgänge. Chem Ber 64, 2844-2856.
    • (1931) Chem Ber , vol.64 , pp. 2844-2856
    • Haber, F.1    Willstätter, R.2
  • 24
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell, B. & Gutteridge, J. M. (1984). Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J 219, 1-14.
    • (1984) Biochem J , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.2
  • 25
    • 0025707199 scopus 로고
    • Dihydroxybenzoylserine - a siderophore for
    • Hantke, K. (1990). Dihydroxybenzoylserine - a siderophore for E. coli. FEMS Microbiol Lett 55, 5-8.
    • (1990) E. Coli. FEMS Microbiol Lett , vol.55 , pp. 5-8
    • Hantke, K.1
  • 26
    • 0022919619 scopus 로고
    • Effects of iron-limitation of Escherichia coli on growth, the respiratory chains and gallium uptake
    • Hubbard, J. A., Lewandowska, K. B., Hughes, M. N. & Poole, R. K. (1986). Effects of iron-limitation of Escherichia coli on growth, the respiratory chains and gallium uptake. Arch Microbiol 146, 80-86.
    • (1986) Arch Microbiol , vol.146 , pp. 80-86
    • Hubbard, J.A.1    Lewandowska, K.B.2    Hughes, M.N.3    Poole, R.K.4
  • 27
    • 0023905646 scopus 로고
    • Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
    • Imlay, J. A., Chin, S. M. & Linn, S. (1988). Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 240, 640-642.
    • (1988) Science , vol.240 , pp. 640-642
    • Imlay, J.A.1    Chin, S.M.2    Linn, S.3
  • 28
    • 84856751993 scopus 로고    scopus 로고
    • The effects of antibacterial peptides on bacterial and membrane integrity and their mechanism of cellular entry.
    • San Diego, USA
    • Jonnalagadda, U. M. (2009). The effects of antibacterial peptides on bacterial and membrane integrity and their mechanism of cellular entry. Master's thesis, San Diego State University, San Diego, USA.
    • (2009) Master's thesis San Diego State University
    • Jonnalagadda, U.M.1
  • 29
    • 18744364456 scopus 로고    scopus 로고
    • Holliday junctionbinding peptides inhibit distinct junction-processing enzymes
    • Kepple, K. V., Boldt, J. L. & Segall, A. M. (2005). Holliday junctionbinding peptides inhibit distinct junction-processing enzymes. Proc Natl Acad Sci U S A 102, 6867-6872.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6867-6872
    • Kepple, K.V.1    Boldt, J.L.2    Segall, A.M.3
  • 30
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • Kohanski, M. A., Dwyer, D. J., Hayete, B., Lawrence, C. A. & Collins, J. J. (2007). A common mechanism of cellular death induced by bactericidal antibiotics. Cell 130, 797-810.
    • (2007) Cell , vol.130 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 31
    • 0242405531 scopus 로고    scopus 로고
    • TolC - the bacterial exit duct for proteins and drugs
    • Koronakis, V. (2003). TolC - the bacterial exit duct for proteins and drugs. FEBS Lett 555, 66-71.
    • (2003) FEBS Lett , vol.555 , pp. 66-71
    • Koronakis, V.1
  • 32
    • 3943108216 scopus 로고    scopus 로고
    • Structure and function of TolC: The bacterial exit duct for proteins and drugs
    • Koronakis, V., Eswaran, J. & Hughes, C. (2004). Structure and function of TolC: the bacterial exit duct for proteins and drugs. Annu Rev Biochem 73, 467-489.
    • (2004) Annu Rev Biochem , vol.73 , pp. 467-489
    • Koronakis, V.1    Eswaran, J.2    Hughes, C.3
  • 33
    • 36049037827 scopus 로고    scopus 로고
    • Rapid kinetic microassay for catalase activity
    • Li, Y. & Schellhorn, H. E. (2007). Rapid kinetic microassay for catalase activity. J Biomol Tech 18, 185-187.
    • (2007) J Biomol Tech , vol.18 , pp. 185-187
    • Li, Y.1    Schellhorn, H.E.2
  • 34
    • 79958115232 scopus 로고    scopus 로고
    • A novel antimicrobial peptide significantly enhances acid-induced killing of Shiga toxinproducing Escherichia coli O157 and non-O157 serotypes
    • Lino, M., Kus, J. V., Tran, S. L., Naqvi, Z., Binnington, B., Goodman, S. D., Segall, A. M. & Foster, D. B. (2011). A novel antimicrobial peptide significantly enhances acid-induced killing of Shiga toxinproducing Escherichia coli O157 and non-O157 serotypes. Microbiology 157, 1768-1775.
    • (2011) Microbiology , vol.157 , pp. 1768-1775
    • Lino, M.1    Kus, J.V.2    Tran, S.L.3    Naqvi, Z.4    Binnington, B.5    Goodman, S.D.6    Segall, A.M.7    Foster, D.B.8
  • 35
    • 16344377473 scopus 로고    scopus 로고
    • A role for iron-sulfur clusters in DNA repair
    • Lukianova, O. A. & David, S. S. (2005). A role for iron-sulfur clusters in DNA repair. Curr Opin Chem Biol 9, 145-151.
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 145-151
    • Lukianova, O.A.1    David, S.S.2
  • 36
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • Massé, E. & Gottesman, S. (2002). A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc Natl Acad Sci U S A 99, 4620-4625.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 4620-4625
    • Massé, E.1    Gottesman, S.2
  • 37
    • 0141860088 scopus 로고    scopus 로고
    • Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli
    • Massé, E., Escorcia, F. E. & Gottesman, S. (2003). Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli. Genes Dev 17, 2374-2383.
    • (2003) Genes Dev , vol.17 , pp. 2374-2383
    • Massé, E.1    Escorcia, F.E.2    Gottesman, S.3
  • 38
    • 26444505976 scopus 로고    scopus 로고
    • Effect of RyhB small RNA on global iron use in Escherichia coli
    • Massé, E., Vanderpool, C. K. & Gottesman, S. (2005). Effect of RyhB small RNA on global iron use in Escherichia coli. J Bacteriol 187, 6962-6971.
    • (2005) J Bacteriol , vol.187 , pp. 6962-6971
    • Massé, E.1    Vanderpool, C.K.2    Gottesman, S.3
  • 39
  • 40
    • 34547863499 scopus 로고    scopus 로고
    • The co-ordinated regulation of iron homeostasis in murine macrophages limits the availability of iron for intracellular Salmonella typhimurium
    • Nairz, M., Theurl, I., Ludwiczek, S., Theurl, M., Mair, S. M., Fritsche, G. & Weiss, G. (2007). The co-ordinated regulation of iron homeostasis in murine macrophages limits the availability of iron for intracellular Salmonella typhimurium. Cell Microbiol 9, 2126-2140.
    • (2007) Cell Microbiol , vol.9 , pp. 2126-2140
    • Nairz, M.1    Theurl, I.2    Ludwiczek, S.3    Theurl, M.4    Mair, S.M.5    Fritsche, G.6    Weiss, G.7
  • 41
  • 42
    • 0019759560 scopus 로고
    • Iron absorption and transport in microorganisms
    • Neilands, J. B. (1981). Iron absorption and transport in microorganisms. Annu Rev Nutr 1, 27-46.
    • (1981) Annu Rev Nutr , vol.1 , pp. 27-46
    • Neilands, J.B.1
  • 43
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • Outten, F. W., Djaman, O. & Storz, G. (2004). A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol Microbiol 52, 861-872.
    • (2004) Mol Microbiol , vol.52 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 44
    • 34249777280 scopus 로고    scopus 로고
    • The small RNA RyhB activates the translation of shiA mRNA encoding a permease of shikimate, a compound involved in siderophore synthesis
    • Prévost, K., Salvail, H., Desnoyers, G., Jacques, J. F., Phaneuf, E. & Massé, E. (2007). The small RNA RyhB activates the translation of shiA mRNA encoding a permease of shikimate, a compound involved in siderophore synthesis. Mol Microbiol 64, 1260-1273.
    • (2007) Mol Microbiol , vol.64 , pp. 1260-1273
    • Prévost, K.1    Salvail, H.2    Desnoyers, G.3    Jacques, J.F.4    Phaneuf, E.5    Massé, E.6
  • 45
    • 0037389797 scopus 로고    scopus 로고
    • Enterobactin: An archetype for microbial iron transport
    • Raymond, K. N., Dertz, E. A. & Kim, S. S. (2003). Enterobactin: an archetype for microbial iron transport. Proc Natl Acad Sci U S A 100, 3584-3588.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 3584-3588
    • Raymond, K.N.1    Dertz, E.A.2    Kim, S.S.3
  • 46
    • 64149092801 scopus 로고    scopus 로고
    • Redox control of the DNA damage-inducible protein DinG helicase activity via its iron-sulfur cluster
    • Ren, B., Duan, X. & Ding, H. (2009). Redox control of the DNA damage-inducible protein DinG helicase activity via its iron-sulfur cluster. J Biol Chem 284, 4829-4835.
    • (2009) J Biol Chem , vol.284 , pp. 4829-4835
    • Ren, B.1    Duan, X.2    Ding, H.3
  • 47
    • 0023127806 scopus 로고
    • Universal chemical assay for the detection and determination of siderophores
    • Schwyn, B. & Neilands, J. B. (1987). Universal chemical assay for the detection and determination of siderophores. Anal Biochem 160, 47-56.
    • (1987) Anal Biochem , vol.160 , pp. 47-56
    • Schwyn, B.1    Neilands, J.B.2
  • 48
    • 77951224521 scopus 로고    scopus 로고
    • An antimicrobial peptide that targets DNA repair intermediates in vitro inhibits Salmonella growth within murine macrophages
    • Su, L. Y., Willner, D. L. & Segall, A. M. (2010). An antimicrobial peptide that targets DNA repair intermediates in vitro inhibits Salmonella growth within murine macrophages. Antimicrob Agents Chemother 54, 1888-1899.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 1888-1899
    • Su, L.Y.1    Willner, D.L.2    Segall, A.M.3
  • 49
    • 0034532850 scopus 로고    scopus 로고
    • A method for direct cloning of Fur-regulated genes: Identification of seven new Fur-regulated loci in Escherichia coli
    • Vassinova, N. & Kozyrev, D. (2000). A method for direct cloning of Fur-regulated genes: identification of seven new Fur-regulated loci in Escherichia coli. Microbiology 146, 3171-3182.
    • (2000) Microbiology , vol.146 , pp. 3171-3182
    • Vassinova, N.1    Kozyrev, D.2
  • 50
    • 0036125229 scopus 로고    scopus 로고
    • Quantitation of intracellular free iron by electron paramagnetic resonance spectroscopy
    • Woodmansee, A. N. & Imlay, J. A. (2002). Quantitation of intracellular free iron by electron paramagnetic resonance spectroscopy. Methods Enzymol 349, 3-9.
    • (2002) Methods Enzymol , vol.349 , pp. 3-9
    • Woodmansee, A.N.1    Imlay, J.A.2
  • 51
    • 33745187803 scopus 로고    scopus 로고
    • IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins
    • Yeo, W. S., Lee, J. H., Lee, K. C. & Roe, J. H. (2006). IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins. Mol Microbiol 61, 206-218.
    • (2006) Mol Microbiol , vol.61 , pp. 206-218
    • Yeo, W.S.1    Lee, J.H.2    Lee, K.C.3    Roe, J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.