메뉴 건너뛰기




Volumn , Issue , 2006, Pages 115-123

Colicins: Bacterial/Antibiotic Peptides

Author keywords

[No Author keywords available]

Indexed keywords


EID: 33846232373     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012369442-3/50021-0     Document Type: Chapter
Times cited : (5)

References (45)
  • 1
    • 84882824803 scopus 로고    scopus 로고
    • Almendinger R, Hager, LP. Studies on the mechanism of action of colicin E2. 107-133. In "Chemistry and function of colicins" (Hager LP, ed.). Academic Press, New York.
    • Almendinger R, Hager, LP. Studies on the mechanism of action of colicin E2. 107-133. In "Chemistry and function of colicins" (Hager LP, ed.). Academic Press, New York.
  • 2
    • 0024789570 scopus 로고
    • Comparison of the uptake systems for the entry of various BtuB group colicins into Escherichia coli
    • Bénédetti H, Frenette M, Baty D, Lloublès R, Geli V, Lazdunski C Comparison of the uptake systems for the entry of various BtuB group colicins into Escherichia coli. J Gen Microbiol 1989, 135:3413-3420.
    • (1989) J Gen Microbiol , vol.135 , pp. 3413-3420
    • Bénédetti, H.1    Frenette, M.2    Baty, D.3    Lloublès, R.4    Geli, V.5    Lazdunski, C.6
  • 3
    • 0022409086 scopus 로고
    • Localization of the immunity protein-reactive domain in unmodified and chemically modified COOH-terminal peptides of colicin E1
    • Bishop LJ, Bjes ES, Davidson VL, Cramer WA Localization of the immunity protein-reactive domain in unmodified and chemically modified COOH-terminal peptides of colicin E1. J Bacteriol 1985, 164:237-244.
    • (1985) J Bacteriol , vol.164 , pp. 237-244
    • Bishop, L.J.1    Bjes, E.S.2    Davidson, V.L.3    Cramer, W.A.4
  • 4
    • 0031034934 scopus 로고    scopus 로고
    • The N-terminal domain of colicin E3 interacts with TolB which is involved in the colicin translocation step
    • Bouveret E, Rigal A, Lazdunski C, Bénédetti H The N-terminal domain of colicin E3 interacts with TolB which is involved in the colicin translocation step. Mol Microbiol 1997, 23:909-920.
    • (1997) Mol Microbiol , vol.23 , pp. 909-920
    • Bouveret, E.1    Rigal, A.2    Lazdunski, C.3    Bénédetti, H.4
  • 5
    • 0015188985 scopus 로고
    • Specific inactivation of ribosomes by colicin E3 in vitro and mechanism of immunity in colicinogenic cells
    • Bowman CM, Sidikaro J, Nomura M Specific inactivation of ribosomes by colicin E3 in vitro and mechanism of immunity in colicinogenic cells. Nat New Biol 1971, 234:133-137.
    • (1971) Nat New Biol , vol.234 , pp. 133-137
    • Bowman, C.M.1    Sidikaro, J.2    Nomura, M.3
  • 6
    • 0036589164 scopus 로고    scopus 로고
    • Ton-dependent colicins and microcins: modular design and evolution
    • Braun V, Patzer SI, Hantke K Ton-dependent colicins and microcins: modular design and evolution. Biochimie 2002, 84:365-380.
    • (2002) Biochimie , vol.84 , pp. 365-380
    • Braun, V.1    Patzer, S.I.2    Hantke, K.3
  • 7
    • 0016292598 scopus 로고
    • Isolation and characterization of an Escherichia coli mutant tolerant to colicins Ia and Ib
    • Cardelli J, Konisky J Isolation and characterization of an Escherichia coli mutant tolerant to colicins Ia and Ib. J Bacteriol 1974, 119:379-385.
    • (1974) J Bacteriol , vol.119 , pp. 379-385
    • Cardelli, J.1    Konisky, J.2
  • 8
    • 0000331264 scopus 로고
    • General introduction to the secretion of bacteriocins
    • Springer-Verlag, Berlin, R. James, C. Lazdunski, F. Pattus (Eds.)
    • Cavard D, Oudega B General introduction to the secretion of bacteriocins. Bacteriocins, Microcins, and Lantibiotics 1992, 297-305. Springer-Verlag, Berlin. R. James, C. Lazdunski, F. Pattus (Eds.).
    • (1992) Bacteriocins, Microcins, and Lantibiotics , pp. 297-305
    • Cavard, D.1    Oudega, B.2
  • 9
    • 0034881923 scopus 로고    scopus 로고
    • Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase LepB
    • de Zamaroczy M, Mora L, Lecuyer A, Geli V, Buckingham RH Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase LepB. Mol Cell 2001, 8:159-168.
    • (2001) Mol Cell , vol.8 , pp. 159-168
    • de Zamaroczy, M.1    Mora, L.2    Lecuyer, A.3    Geli, V.4    Buckingham, R.H.5
  • 10
    • 0031569354 scopus 로고    scopus 로고
    • A mechanism for protein insertion into the membranes is suggested by the crystal structure of the channel-forming domain of colicin E1
    • Elkins P, Bunker A, Cramer WA, Stauffacher CV A mechanism for protein insertion into the membranes is suggested by the crystal structure of the channel-forming domain of colicin E1. Structure 1997, 5:443-458.
    • (1997) Structure , vol.5 , pp. 443-458
    • Elkins, P.1    Bunker, A.2    Cramer, W.A.3    Stauffacher, C.V.4
  • 11
    • 0024658176 scopus 로고
    • Topology and function of the integral membrane protein conferring immunity to colicin A
    • Géli V, Baty D, Pattus F, Lazdunski C Topology and function of the integral membrane protein conferring immunity to colicin A. Mol Microbiol 1989, 3:679-687.
    • (1989) Mol Microbiol , vol.3 , pp. 679-687
    • Géli, V.1    Baty, D.2    Pattus, F.3    Lazdunski, C.4
  • 12
    • 0017646422 scopus 로고
    • Studies on the depolarization of the Escherichia coli cell membrane by colicin E1
    • Gould JM, Cramer WA Studies on the depolarization of the Escherichia coli cell membrane by colicin E1. J Biol Chem 1977, 252:5491-5497.
    • (1977) J Biol Chem , vol.252 , pp. 5491-5497
    • Gould, J.M.1    Cramer, W.A.2
  • 13
    • 2342447390 scopus 로고    scopus 로고
    • Structural inhibition of the colicin D tRNase by the tRNA-mimicking immunity protein
    • Graille M, Mora L, Buckingham RH, van Tilbeurgh H, de Zamaroczy M Structural inhibition of the colicin D tRNase by the tRNA-mimicking immunity protein. EMBO J 2004, 23:1474-1482.
    • (2004) EMBO J , vol.23 , pp. 1474-1482
    • Graille, M.1    Mora, L.2    Buckingham, R.H.3    van Tilbeurgh, H.4    de Zamaroczy, M.5
  • 14
    • 1242297815 scopus 로고    scopus 로고
    • Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution
    • Hilsenbeck JL, Park H, Chen G, Youn B, Postle K, Kang C Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution. Mol Microbiol 2004, 51:711-720.
    • (2004) Mol Microbiol , vol.51 , pp. 711-720
    • Hilsenbeck, J.L.1    Park, H.2    Chen, G.3    Youn, B.4    Postle, K.5    Kang, C.6
  • 15
    • 0012852996 scopus 로고
    • Highly purified colicin E3 contains immunity protein
    • Jakes K, Zinder ND Highly purified colicin E3 contains immunity protein. Proc Natl Acad Sci USA 1974, 71:3380-3384.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 3380-3384
    • Jakes, K.1    Zinder, N.D.2
  • 17
    • 0034283147 scopus 로고    scopus 로고
    • Specificity in protein-protein interactions: the structural basis for dual recognition in endonuclease colicin-immunity protein complexes
    • Kühlmann UC, Pommer AJ, Moore GR, James R, Kleanthous C Specificity in protein-protein interactions: the structural basis for dual recognition in endonuclease colicin-immunity protein complexes. J Mol Bio 2000, 301:1163-1178.
    • (2000) J Mol Bio , vol.301 , pp. 1163-1178
    • Kühlmann, U.C.1    Pommer, A.J.2    Moore, G.R.3    James, R.4    Kleanthous, C.5
  • 20
    • 0036589166 scopus 로고    scopus 로고
    • The Tol proteins of Escherichia coli and their involvement in the translocation of group A colicins
    • Lazzaroni J-C, Dubuisson J-F, Vianney A The Tol proteins of Escherichia coli and their involvement in the translocation of group A colicins. Biochimie 2002, 84:391-397.
    • (2002) Biochimie , vol.84 , pp. 391-397
    • Lazzaroni, J.-C.1    Dubuisson, J.-F.2    Vianney, A.3
  • 21
    • 0034695404 scopus 로고    scopus 로고
    • Unfolding pathway of the colicin E1 channel protein on a membrane surface
    • Lindeberg M, Zakharov SD, Cramer WA Unfolding pathway of the colicin E1 channel protein on a membrane surface. J Mol Biol 2000, 295:679-692.
    • (2000) J Mol Biol , vol.295 , pp. 679-692
    • Lindeberg, M.1    Zakharov, S.D.2    Cramer, W.A.3
  • 22
    • 33947427320 scopus 로고
    • On the mechanisms of action of colicins
    • Luria SE On the mechanisms of action of colicins. Annales de L'Institut Pasteur 1964, 107:67-73.
    • (1964) Annales de L'Institut Pasteur , vol.107 , pp. 67-73
    • Luria, S.E.1
  • 23
    • 23544463912 scopus 로고
    • Mechanism of action of colicins
    • Nomura M Mechanism of action of colicins. Proc Natl Acad Sci USA 1964, 52:1514-1521.
    • (1964) Proc Natl Acad Sci USA , vol.52 , pp. 1514-1521
    • Nomura, M.1
  • 24
    • 0018883387 scopus 로고
    • Assignment of the functional loci in colicin E2 and E3 molecules by the characterization of their proteolytic fragments
    • Ohno-Iwashita Y, Imahori K Assignment of the functional loci in colicin E2 and E3 molecules by the characterization of their proteolytic fragments. Biochemistry 1980, 19:652-659.
    • (1980) Biochemistry , vol.19 , pp. 652-659
    • Ohno-Iwashita, Y.1    Imahori, K.2
  • 26
    • 0015922107 scopus 로고
    • Properties of the fluorescence probe response associated with the transmission mechanism of colicin E1
    • Phillips SK, Cramer WA Properties of the fluorescence probe response associated with the transmission mechanism of colicin E1. Biochemistry 1973, 12:1170-1176.
    • (1973) Biochemistry , vol.12 , pp. 1170-1176
    • Phillips, S.K.1    Cramer, W.A.2
  • 27
    • 0042065285 scopus 로고    scopus 로고
    • Touch and go: tying TonB to transport
    • Postle K, Kadner RJ Touch and go: tying TonB to transport. Mol Microbiol 2003, 49:869-882.
    • (2003) Mol Microbiol , vol.49 , pp. 869-882
    • Postle, K.1    Kadner, R.J.2
  • 28
    • 84882826950 scopus 로고
    • Springer-Verlag, New York, P. Reeves (Ed.)
    • The Bacteriocins, Chapter 1 1972, Springer-Verlag, New York. P. Reeves (Ed.).
    • (1972) The Bacteriocins, Chapter 1
  • 29
    • 0018236743 scopus 로고
    • Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranes
    • Schein SJ, Kagan BL, Finkelstein A Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranes. Nature 1978, 276:159-163.
    • (1978) Nature , vol.276 , pp. 159-163
    • Schein, S.J.1    Kagan, B.L.2    Finkelstein, A.3
  • 30
    • 0030754709 scopus 로고    scopus 로고
    • Identification of residues in the putative TolA box which are essential for the toxicity of the endonuclease toxin colicin E9
    • Schneider CG, Penfold CN, Moore GR, Kleanthous C, James R Identification of residues in the putative TolA box which are essential for the toxicity of the endonuclease toxin colicin E9. Microbiology 1997, 143:2931-2938.
    • (1997) Microbiology , vol.143 , pp. 2931-2938
    • Schneider, C.G.1    Penfold, C.N.2    Moore, G.R.3    Kleanthous, C.4    James, R.5
  • 31
    • 0023218137 scopus 로고
    • Nucleotide sequence of the colicin B activity gene cba: Consensus pentapeptide among TonB-dependent colicins and receptors
    • Schramm E, Mende J, Braun V, Kamp RM Nucleotide sequence of the colicin B activity gene cba: Consensus pentapeptide among TonB-dependent colicins and receptors. J Bacteriol 1987, 169:3350-3357.
    • (1987) J Bacteriol , vol.169 , pp. 3350-3357
    • Schramm, E.1    Mende, J.2    Braun, V.3    Kamp, R.M.4
  • 32
    • 21644453615 scopus 로고    scopus 로고
    • Identification of an essential cleavage site in ColE7 required for import and killing of cells
    • Shi Z, Chak KF, Yuan HS Identification of an essential cleavage site in ColE7 required for import and killing of cells. J Biol Chem 2005, 280:24663-24668.
    • (2005) J Biol Chem , vol.280 , pp. 24663-24668
    • Shi, Z.1    Chak, K.F.2    Yuan, H.S.3
  • 33
    • 0028100898 scopus 로고
    • Identification of a translocated protein segment in a voltage-dependent channel
    • Slatin SL, Qiu X-Q, Jakes KS, Finkelstein A Identification of a translocated protein segment in a voltage-dependent channel. Nature 1994, 371:158-161.
    • (1994) Nature , vol.371 , pp. 158-161
    • Slatin, S.L.1    Qiu, X.-Q.2    Jakes, K.S.3    Finkelstein, A.4
  • 35
    • 0035930345 scopus 로고    scopus 로고
    • Crystal structure of colicin E3: Implications for cell entry and ribosome inactivation
    • Soelaiman S, Jakes K, Wu N, Li CM, Shoham M Crystal structure of colicin E3: Implications for cell entry and ribosome inactivation. Mol Cell 2001, 8:1053-1062.
    • (2001) Mol Cell , vol.8 , pp. 1053-1062
    • Soelaiman, S.1    Jakes, K.2    Wu, N.3    Li, C.M.4    Shoham, M.5
  • 36
    • 0036891689 scopus 로고    scopus 로고
    • Metal ions and phosphate binding in the H-N-H motif: crystal structures of the nuclease domain of Cole7/Im7 in complex with a phosphate ion and different divalent metal ions
    • Sui MJ, Tsai LC, Hsia KC, Doudeva LG, Ku WY, Han GW, Yuan HS Metal ions and phosphate binding in the H-N-H motif: crystal structures of the nuclease domain of Cole7/Im7 in complex with a phosphate ion and different divalent metal ions. Prot Sci 2002, 11:2947-2957.
    • (2002) Prot Sci , vol.11 , pp. 2947-2957
    • Sui, M.J.1    Tsai, L.C.2    Hsia, K.C.3    Doudeva, L.G.4    Ku, W.Y.5    Han, G.W.6    Yuan, H.S.7
  • 39
    • 0345701261 scopus 로고    scopus 로고
    • Thermodynamic consequences of bipartite immunity protein binding to the ribosomal ribonuclease colicin E3
    • Walker D, Moore GR, James R, Kleanthous C Thermodynamic consequences of bipartite immunity protein binding to the ribosomal ribonuclease colicin E3. Biochemistry 2003, 42:4161-4171.
    • (2003) Biochemistry , vol.42 , pp. 4161-4171
    • Walker, D.1    Moore, G.R.2    James, R.3    Kleanthous, C.4
  • 45
    • 0027231701 scopus 로고
    • Intramembrane helix-helix interactions as the basis of inhibition of the colin E1 ion channel by its immunity protein
    • Zhang YL, Cramer WA Intramembrane helix-helix interactions as the basis of inhibition of the colin E1 ion channel by its immunity protein. J Biol Chem 1993, 268.
    • (1993) J Biol Chem , vol.268
    • Zhang, Y.L.1    Cramer, W.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.