메뉴 건너뛰기




Volumn 84, Issue 5-6, 2002, Pages 511-519

Focus on modified microcins: Structural features and mechanisms of action

Author keywords

Antimicrobial peptide; Bacteriocin; Mechanism of action; Microcin; Posttranslational modification

Indexed keywords

ANTIBIOTIC AGENT; BACTERIAL ENZYME; BACTERIAL PROTEIN; BACTERIOCIN; BACTERIUM ANTIBODY; MICROCIN B17; MICROCIN C7; MICROCIN J25; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; MICROCIN;

EID: 0036589245     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(02)01411-6     Document Type: Article
Times cited : (48)

References (62)
  • 1
    • 9444278428 scopus 로고    scopus 로고
    • Modular peptide synthetases involved in nonribosomal peptide synthesis
    • M.A. Marahiel, T. Stachelhaus, H.D. Mootz, Modular peptide synthetases involved in nonribosomal peptide synthesis, Chem. Rev. 97 (1997) 2651-2673.
    • (1997) Chem. Rev. , vol.97 , pp. 2651-2673
    • Marahiel, M.A.1    Stachelhaus, T.2    Mootz, H.D.3
  • 2
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • R.E. Hancock, Peptide antibiotics, Lancet 349 (1997) 418-422.
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.1
  • 3
    • 0033168860 scopus 로고    scopus 로고
    • Antibiotic peptides from higher eukaryotes: Biology and applications
    • T. Ganz, R.I. Lehrer, Antibiotic peptides from higher eukaryotes: biology and applications, Mol. Med. Today 5 (1999) 292-297.
    • (1999) Mol. Med. Today , vol.5 , pp. 292-297
    • Ganz, T.1    Lehrer, R.I.2
  • 4
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • M. Zasloff, Antimicrobial peptides of multicellular organisms, Nature 415 (2002) 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 5
    • 0033105191 scopus 로고    scopus 로고
    • The ecological role of bacteriocins in bacterial competition
    • M.A. Riley, D.M. Gordon, The ecological role of bacteriocins in bacterial competition, Trends Microbiol. 7 (1999) 129-133.
    • (1999) Trends Microbiol. , vol.7 , pp. 129-133
    • Riley, M.A.1    Gordon, D.M.2
  • 7
    • 0034540903 scopus 로고    scopus 로고
    • Isolation, purification and partial amino acid sequence of a highly hydrophobic new microcin named microcin L produced by Escherichia coli
    • S. Gaillard-Gendron, D. Vignon, G. Cottenceau, M. Grabe, N. Zorn, A. Van Dorsselaer, A.M. Pons, Isolation, purification and partial amino acid sequence of a highly hydrophobic new microcin named microcin L produced by Escherichia coli, FEMS Microbiol. Lett. 193 (2000) 95-98.
    • (2000) FEMS Microbiol. Lett. , vol.193 , pp. 95-98
    • Gaillard-Gendron, S.1    Vignon, D.2    Cottenceau, G.3    Grabe, M.4    Zorn, N.5    Van Dorsselaer, A.6    Pons, A.M.7
  • 8
    • 0027132575 scopus 로고
    • ABC transporter: Bacterial exporters
    • M.J. Fath, R. Kolter, ABC transporter: bacterial exporters, Microbiol. Rev. 57 (1993) 995-1017.
    • (1993) Microbiol. Rev. , vol.57 , pp. 995-1017
    • Fath, M.J.1    Kolter, R.2
  • 9
    • 0029905197 scopus 로고    scopus 로고
    • Processing of colicin V-1, a secretable marker protein of a bacterial ATP binding cassette export system, requires membrane integrity, energy, and cytosolic factors
    • X. Zhong, R. Kolter, P.C. Tai, Processing of colicin V-1, a secretable marker protein of a bacterial ATP binding cassette export system, requires membrane integrity, energy, and cytosolic factors, J. Biol. Chem. 271 (1996) 28057-28063.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28057-28063
    • Zhong, X.1    Kolter, R.2    Tai, P.C.3
  • 10
    • 0030858697 scopus 로고    scopus 로고
    • Interactions of dedicated export membrane proteins of the colicin V secretion system: CvaA, a member of the membrane fusion protein family, interacts with CvaB and Tolc
    • J. Hwang, X. Zhong,P.C. Tai, Interactions of dedicated export membrane proteins of the colicin V secretion system: CvaA, a member of the membrane fusion protein family, interacts with CvaB and Tolc, J. Bacteriol. 179 (1997) 6264-6270.
    • (1997) J. Bacteriol. , vol.179 , pp. 6264-6270
    • Hwang, J.1    Zhong, X.P.C.2    Tai3
  • 11
    • 0035150225 scopus 로고    scopus 로고
    • Type 1 secretion and multidrug efflux: Transport through the TolC channel-tunnel
    • S.K. Buchanan, Type 1 secretion and multidrug efflux: transport through the TolC channel-tunnel. Trends Biochem. Sci. 26 (2001) 3-6.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 3-6
    • Buchanan, S.K.1
  • 12
    • 0032991553 scopus 로고    scopus 로고
    • Escherichia coli outer membrane protein TolC is involved in production of the peptide antibiotic microcin J25
    • M.A. Delgado, J.O. Solbiati, M.J. Chiuchiolo, R.N. Faríias, R.A. Solomón, Escherichia coli outer membrane protein TolC is involved in production of the peptide antibiotic microcin J25, J. Bacteriol. 181 (1999) 1968-1970.
    • (1999) J. Bacteriol. , vol.181 , pp. 1968-1970
    • Delgado, M.A.1    Solbiati, J.O.2    Chiuchiolo, M.J.3    Faríias, R.N.4    Solomón, R.A.5
  • 13
    • 0035111967 scopus 로고    scopus 로고
    • The structure, function, and origin of the microcin H47 ATP-binding cassette exporter indicate its relatedness to that of colicin V
    • M.F. Azpiroz, E. Rodríguez, M. Laviña, The structure, function, and origin of the microcin H47 ATP-binding cassette exporter indicate its relatedness to that of colicin V, Antimicrob. Agents Chemother. 45 (2001) 969-972.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 969-972
    • Azpiroz, M.F.1    Rodríguez, E.2    Laviña, M.3
  • 14
    • 0035723807 scopus 로고    scopus 로고
    • Structure, organization and characterization of the gene cluster involved in the production of microcin E492, a channel-forming bacteriocin
    • R. Lagos, M. Baeza, G. Corsini, C. Hertz, E. Strahsburger, J.A. Castillo, C. Vergara, O. Monasterio, Structure, organization and characterization of the gene cluster involved in the production of microcin E492, a channel-forming bacteriocin, Mol. Microbiol. 42 (2001) 229-243.
    • (2001) Mol. Microbiol. , vol.42 , pp. 229-243
    • Lagos, R.1    Baeza, M.2    Corsini, G.3    Hertz, C.4    Strahsburger, E.5    Castillo, J.A.6    Vergara, C.7    Monasterio, O.8
  • 15
    • 0028271859 scopus 로고
    • Purification and characterization of colicin V from E. coli culture supernatants
    • M.J. Fath,L.H. Zhang, J. Rush, R. Kolter, Purification and characterization of colicin V from E. coli culture supernatants, Biochemistry 33 (1994) 6911-6917.
    • (1994) Biochemistry , vol.33 , pp. 6911-6917
    • Fath, M.J.1    Zhang, L.H.2    Rush, J.3    Kolter, R.4
  • 17
    • 0021342671 scopus 로고
    • Colicin V-treated Escherichia coli does not generate membrane potential
    • C.C. Yang, J. Konisky, Colicin V-treated Escherichia coli does not generate membrane potential, J. Bacteriol. 158 (1984) 757-759.
    • (1984) J. Bacteriol. , vol.158 , pp. 757-759
    • Yang, C.C.1    Konisky, J.2
  • 18
    • 0027533645 scopus 로고
    • Microcin E492 forms ion channels in phospholipid bilayer membrane
    • R. Lagos, M. Wilkens, C. Vergara, X. Cecchi, O. Monasterio, Microcin E492 forms ion channels in phospholipid bilayer membrane, FEBS Lett. 321 (1993) 145-148.
    • (1993) FEBS Lett. , vol.321 , pp. 145-148
    • Lagos, R.1    Wilkens, M.2    Vergara, C.3    Cecchi, X.4    Monasterio, O.5
  • 19
    • 0034695129 scopus 로고    scopus 로고
    • Effects of the antibiotic peptide microcin J25 on liposomes: Role of acyl chain length and negatively charged phosphiolipid
    • M.R. Rintoul, B.F. de Arcuri, R.D. Morero, Effects of the antibiotic peptide microcin J25 on liposomes: role of acyl chain length and negatively charged phosphiolipid, Biochim. Biophys Acta 1509 (2000) 65-72.
    • (2000) Biochim. Biophys. Acta , vol.1509 , pp. 65-72
    • Rintoul, M.R.1    De Arcuri, B.F.2    Morero, R.D.3
  • 20
    • 0017286529 scopus 로고
    • A new family of low molecular weight antibiotics from enterobacteria
    • C. Asensio, J.C. Pérez-Díaz, A new family of low molecular weight antibiotics from enterobacteria, Biochem. Biophys. Res. Commun. 69 (1976) 7-14.
    • (1976) Biochem. Biophys. Res. Commun. , vol.69 , pp. 7-14
    • Asensio, C.1    Pérez-Díaz, J.c.2
  • 23
    • 33748223344 scopus 로고
    • Post-translational backbone modifications in the ribosomal biosynthesis of the glycine-rich antibiotic microcin B17
    • A. Bayer, S. Freund, G. Nicholson, G. Jung, Post-translational backbone modifications in the ribosomal biosynthesis of the glycine-rich antibiotic microcin B17, Angew. Chem. Int. Ed. Engl. 32 (1993) 1336-1339.
    • (1993) Angew. Chem. Int. Ed. Engl. , vol.32 , pp. 1336-1339
    • Bayer, A.1    Freund, S.2    Nicholson, G.3    Jung, G.4
  • 24
    • 0029762864 scopus 로고    scopus 로고
    • Synthesis of the DNA gyrase inhibitor microcin B17, a 43-peptide antibiotic with eight aromatic heterocycles in its backbone
    • G.I. Videnov, D. Kaiser, M. Brooks, G. Jung, Synthesis of the DNA gyrase inhibitor microcin B17, a 43-peptide antibiotic with eight aromatic heterocycles in its backbone, Angew. Chem. Int. Ed. Engl. 35 (1996) 1506-1508.
    • (1996) Angew. Chem. Int. Ed. Engl. , vol.35 , pp. 1506-1508
    • Videnov, G.i.1    Kaiser, D.2    Brooks, M.3    Jung, G.4
  • 25
    • 0021858635 scopus 로고
    • Cloning and mapping of the genetic determinants for microcin B17 production and immunity
    • J.L. San Millán, C. Hernández-Chico, P. Pereda, F. Moreno, Cloning and mapping of the genetic determinants for microcin B17 production and immunity, J. Bacteriol. 163 (1985) 275-281.
    • (1985) J. Bacteriol. , vol.163 , pp. 275-281
    • San Millán, J.L.1    Hernández-Chico, C.2    Pereda, P.3    Moreno, F.4
  • 26
    • 0021926685 scopus 로고
    • Plasmid genes required for microcin B17 production
    • J.L. San Millán, R. Kolter, F. Moreno, Plasmid genes required for microcin B17 production, J. Bacteriol. 163 (1985) 1016-1020.
    • (1985) J. Bacteriol. , vol.163 , pp. 1016-1020
    • San Millán, J.L.1    Kolter, R.2    Moreno, F.3
  • 27
    • 0029923954 scopus 로고    scopus 로고
    • From peptide precursors to oxazole and thiazole-containing peptide antibiotics: Microcin B17 synthase
    • Y.M. Li, J.C. Milne, L.L. Madison, R. Kolter, C.T. Walsh, From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase, Science 274 (1996) 1188-1193.
    • (1996) Science , vol.274 , pp. 1188-1193
    • Li, Y.M.1    Milne, J.C.2    Madison, L.L.3    Kolter, R.4    Walsh, C.T.5
  • 28
    • 0039130745 scopus 로고    scopus 로고
    • Cofactor requirements and reconstitution of microcin B17 synthase: A multienzyme complex that catalyzes the formation of oxazoles and thiazoles in the antibiotic microcin B17
    • J.C. Milne, R.S. Roy, AC. Eliot, N.L. Kelleher, A. Wokhlu,B. Nickels, C.T. Walsh, Cofactor requirements and reconstitution of microcin B17 synthase: a multienzyme complex that catalyzes the formation of oxazoles and thiazoles in the antibiotic microcin B17, Biochemistry 38 (1999) 4768-4781.
    • (1999) Biochemistry , vol.38 , pp. 4768-4781
    • Milne, J.C.1    Roy, R.S.2    Eliot, A.C.3    Kelleher, N.L.4    Wokhlu, A.5    Nickels, B.6    Walsh, C.T.7
  • 29
    • 0032558419 scopus 로고    scopus 로고
    • ATP/GTP hydrolysis is required for oxazole and thiazole biosynthesis in the peptide antibiotic microcin B17
    • J.C. Milne, AC. Eliot, N.L. Kelleher, C.T. Walsh, ATP/GTP hydrolysis is required for oxazole and thiazole biosynthesis in the peptide antibiotic microcin B17, Biochemistry 37 (1998) 13250-13261.
    • (1998) Biochemistry , vol.37 , pp. 13250-13261
    • Milne, J.C.1    Eliot, A.C.2    Kelleher, N.l.3    Walsh, C.T.4
  • 30
    • 0031023072 scopus 로고    scopus 로고
    • The leader peptide is essential for the post-translational modification of the DNA-gyrase inhibitor microcin B17
    • L.L. Madison, E.I. Vivas, Y.M. Li, C.T. Walsh, R. Kolter, The leader peptide is essential for the post-translational modification of the DNA-gyrase inhibitor microcin B17, Mol. Microbiol. 23 (1997) 161-168.
    • (1997) Mol. Microbiol. , vol.23 , pp. 161-168
    • Madison, L.L.1    Vivas, E.I.2    Li, Y.M.3    Walsh, C.t.4    Kolter, R.5
  • 31
    • 0033598801 scopus 로고    scopus 로고
    • Post-translational heterocyclization of cysteine and serine residues in theantibiotic microcin B17: Distributivity and directionality
    • N.L. Kelleher, C.L. Hendrickson, C.T. Walsh, Post-translational heterocyclization of cysteine and serine residues in theantibiotic microcin B17: distributivity and directionality, Biochemistry 38 (1999) 15623-1530.
    • (1999) Biochemistry , vol.38 , pp. 15623-15630
    • Kelleher, N.L.1    Hendrickson, C.L.2    Walsh, C.T.3
  • 32
    • 0024022450 scopus 로고
    • The export of the DNA replication inhibitor microcin B17 provides immunity for the host cell
    • M.C. Garrido, M. Herrero, R. Kolter, F. Moreno, The export of the DNA replication inhibitor microcin B17 provides immunity for the host cell. EMBO J. 7 (1988) 1853-1862.
    • (1988) EMBO J. , vol.7 , pp. 1853-1862
    • Garrido, M.C.1    Herrero, M.2    Kolter, R.3    Moreno, F.4
  • 33
    • 0022516452 scopus 로고
    • Identification, mapping, cloning and characterization of a gene (sbmA) required for microcin B17 action on Escherichia coli K12
    • M. Laviña,A.P. Pugsley, F. Moreno, Identification, mapping, cloning and characterization of a gene (sbmA) required for microcin B17 action on Escherichia coli K12, J. Gen. Microbiol. 132 (1986) 1685-1693.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 1685-1693
    • Laviña, M.1    Pugsley, A.P.2    Moreno, F.3
  • 34
    • 0022653084 scopus 로고
    • Microcin B17 blocks DNA replication and induces the SOS system in Escherichia coli
    • M. Herrero, F. Moreno, Microcin B17 blocks DNA replication and induces the SOS system in Escherichia coli, J. Gen. Microbiol. 132 (1986) 393-402.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 393-402
    • Herrero, M.1    Moreno, F.2
  • 35
    • 0035101015 scopus 로고    scopus 로고
    • Construction and characterization of mutations at codon 751 of the Escherichia coli gyrB gene that confer resistance to the antimicrobial peptide microcin B17 and alter the activity of DNA gyrase
    • F.J. del Castillo, I. del Castillo, F. Moreno, Construction and characterization of mutations at codon 751 of the Escherichia coli gyrB gene that confer resistance to the antimicrobial peptide microcin B17 and alter the activity of DNA gyrase, J. Bacteriol. 183 (2001) 2137-2140.
    • (2001) J. Bacteriol. , vol.183 , pp. 2137-2140
    • Del Castillo, F.J.1    Del Castillo, I.2    Moreno, F.3
  • 36
    • 0025964113 scopus 로고
    • The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. coli DNA gyrase
    • J.L. Vizán, C. Hernández-Chico, I. del Castillo, F. Moreno, The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. coli DNA gyrase, EMBO J. 10 (1991) 467-476.
    • (1991) EMBO J. , vol.10 , pp. 467-476
    • Vizán, J.L.1    Hernández-Chico, C.2    Del Castillo, I.3    Moreno, F.4
  • 38
    • 0034946779 scopus 로고    scopus 로고
    • In vitro characterization of DNA gyrase inhibition by microcin B17 analogs with altered bisheterocyclic sites
    • D.B. Zamble, D.A. Miller, J.G. Heddle, A. Maxwell, C.T. Walsh, F. Hollfelder, In vitro characterization of DNA gyrase inhibition by microcin B17 analogs with altered bisheterocyclic sites, Proc. Natl. Acad. Sci. USA 98 (2001) 7712-7717.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7712-7717
    • Zamble, D.B.1    Miller, D.A.2    Heddle, J.G.3    Maxwell, A.4    Walsh, C.T.5    Hollfelder, F.6
  • 39
    • 0033133846 scopus 로고    scopus 로고
    • In vivo processing and antibiotic activity of microcin B17 analogs with varying ring content and altered bisheterocyclic sites
    • R.S. Roy, N.L. Kelleher, J.C. Milne, C.T. Walsh, In vivo processing and antibiotic activity of microcin B17 analogs with varying ring content and altered bisheterocyclic sites, Chem. Biol. 6 (1999) 305-318.
    • (1999) Chem. Biol. , vol.6 , pp. 305-318
    • Roy, R.S.1    Kelleher, N.L.2    Milne, J.C.3    Walsh, C.t.4
  • 42
    • 0021945764 scopus 로고
    • Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli
    • J.F. Garcia-Bustos, N. Pezzi, E. Mendez, Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli, Antimicrob. Agents Chemother. 27 (1985) 791-797.
    • (1985) Antimicrob. Agents Chemother. , vol.27 , pp. 791-797
    • Garcia-Bustos, J.F.1    Pezzi, N.2    Mendez, E.3
  • 44
    • 0028868830 scopus 로고
    • Structure and organization of plasmid genes required to produce the translation inhibitor microcin C7
    • J.E. González-Pastor, J.L. San Millán, M.A. Castilla, F. Moreno, Structure and organization of plasmid genes required to produce the translation inhibitor microcin C7, J. Bacteriol. 177 (1995) 7131-7140.
    • (1995) J. Bacteriol. , vol.177 , pp. 7131-7140
    • González-Pastor, J.E.1    San Millán, J.L.2    Castilla, M.A.3    Moreno, F.4
  • 47
    • 0027136035 scopus 로고
    • Cloning and mapping of the genetic determinants for microcin C51 production and immunity
    • N.E. Kurepina, E.I. Basyuk, A.Z. Metlitskaya, D.A. Zaitsev, I.A. Khmel, Cloning and mapping of the genetic determinants for microcin C51 production and immunity, Mol. Gen. Genet. 241 (1993) 700-706.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 700-706
    • Kurepina, N.E.1    Basyuk, E.I.2    Metlitskaya, A.Z.3    Zaitsev, D.A.4    Khmel, I.A.5
  • 51
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins
    • Y.Q. Tang, J. Yuan, G. Osapay, K. Osapay, D. Tran, C.J. Miller, A.J. Ouellette, M.E. Selsted, A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins, Science 286 (1999) 498-502.
    • (1999) Science , vol.286 , pp. 498-502
    • Tang, Y.Q.1    Yuan, J.2    Osapay, G.3    Osapay, K.4    Tran, D.5    Miller, C.J.6    Ouellette, A.J.7    Selsted, M.E.8
  • 53
    • 0034793341 scopus 로고    scopus 로고
    • Plant cyclotides: Circular, knotted peptide toxins
    • D.J. Craik, Plant cyclotides: circular, knotted peptide toxins, Toxicon 39 (2001) 1809-1813.
    • (2001) Toxicon , vol.39 , pp. 1809-1813
    • Craik, D.J.1
  • 54
    • 0030006825 scopus 로고    scopus 로고
    • Genetic analysis of plasmid determinants for microcin J25 production and immunity
    • J.O. Solbiati, M. Ciaccio, R.N. Farías, R.A. Salomón, Genetic analysis of plasmid determinants for microcin J25 production and immunity, J. Bacteriol. 178 (1996) 3661-3663.
    • (1996) J. Bacteriol. , vol.178 , pp. 3661-3663
    • Solbiati, J.O.1    Ciaccio, M.2    Farías, R.N.3    Salomón, R.A.4
  • 55
    • 0032962962 scopus 로고    scopus 로고
    • Sequence analysis of the four plasmid genes required to produce the circular peptide antibiotic microcin J25
    • J.O. Solbiati, M. Ciaccio, R.N. Farías, J.E. González-Pastor, F. Moreno, R.A. Salomón, Sequence analysis of the four plasmid genes required to produce the circular peptide antibiotic microcin J25, J. Bacteriol. 181 (1999) 2659-2662.
    • (1999) J. Bacteriol. , vol.181 , pp. 2659-2662
    • Solbiati, J.O.1    Ciaccio, M.2    Farías, R.N.3    González-Pastor, J.E.4    Moreno, F.5    Salomón, R.A.6
  • 56
    • 0035856589 scopus 로고    scopus 로고
    • The antibacterial action of microcin J25: Evidence for disruption of cytoplasmic membrane energization in Salmonella newport
    • M.R. Rintoul, B.F. de Arcuri, R.A. Salomón, R.N. Farías, R.D. Moreno, The antibacterial action of microcin J25: evidence for disruption of cytoplasmic membrane energization in Salmonella newport,, FEMS Microbiol. Lett. 204 (2001) 265-270.
    • (2001) FEMS Microbiol. Lett. , vol.204 , pp. 265-270
    • Rintoul, M.R.1    De Arcuri, B.F.2    Salomón, R.A.3    Farías, R.N.4    Moreno, R.D.5
  • 57
    • 0027369822 scopus 로고
    • The FhuA protein is involved in microcin 25 uptake
    • R.A. Salomón, R.N. Farías, The FhuA protein is involved in microcin 25 uptake, J. Bacteriol. 175 (1993) 7741-7742.
    • (1993) J. Bacteriol. , vol.175 , pp. 7741-7742
    • Salomón, R.A.1    Farías, R.N.2
  • 58
    • 0029045349 scopus 로고
    • The peptide antibiotic microcin 25 is imported through the TonB pathway and the SbmA protein
    • R.A. Salomón, R.N. Farías, The peptide antibiotic microcin 25 is imported through the TonB pathway and the SbmA protein, J. Bacteriol. 177 (1995) 3323-3325.
    • (1995) J. Bacteriol. , vol.177 , pp. 3322-3325
    • Salomón, R.A.1    Farías, R.N.2
  • 59
    • 0032073710 scopus 로고    scopus 로고
    • FhuA, an Escherichia coli outer membrane protein with a dual function of transporter and channel which mediates the transport of phage DNA
    • M. Bonhivers, L. Plancon, A. Ghazi, P. Boulanger, M. le Maire, O. Lambert, J.L. Rigaud, L. Letellier, FhuA, an Escherichia coli outer membrane protein with a dual function of transporter and channel which mediates the transport of phage DNA, Biochimie 80 (1998) 363-369.
    • (1998) Biochimie , vol.80 , pp. 363-369
    • Bonhivers, M.1    Plancon, L.2    Ghazi, A.3    Boulanger, P.4    Le Maire, M.5    Lambert, O.6    Rigaud, J.L.7    Letellier, L.8
  • 60
    • 0017722421 scopus 로고
    • Genetics of sensitivity of Salmonella species to colicin M and bacteriophages T5, T1, and ES18
    • A.C. Graham, B.A. Stocker, Genetics of sensitivity of Salmonella species to colicin M and bacteriophages T5, T1, and ES18, J. Bacteriol. 130 (1977) 1214-1223.
    • (1977) J. Bacteriol. , vol.130 , pp. 1214-1223
    • Graham, A.C.1    Stocker, B.A.2
  • 61
    • 0034932730 scopus 로고    scopus 로고
    • Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25
    • M.A. Delgado, M.R. Rintoul, R.N. Farías, R.A. Salomón, Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25, J. Bacteriol. 183 (2001) 4543-4550.
    • (2001) J. Bacteriol. , vol.183 , pp. 4543-4550
    • Delgado, M.A.1    Rintoul, M.R.2    Farías, R.N.3    Salomón, R.A.4
  • 62
    • 0026526445 scopus 로고
    • Microcin 25, a novel antimicrobial peptide produced by Escherichia coli
    • R.A. Salomón, R.N. Farías, Microcin 25, a novel antimicrobial peptide produced by Escherichia coli, J. Bacteriol. 174 (1992) 7428-7435.
    • (1992) J. Bacteriol. , vol.174 , pp. 7428-7435
    • Salomón, R.A.1    Farías, R.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.