메뉴 건너뛰기




Volumn 180, Issue 19, 1998, Pages 4993-5002

Colicin import into Escherichia coli cells

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; CELL MEMBRANE PROTEIN; CELL RECEPTOR; COLICIN; ENTEROCHELIN; PORIN;

EID: 0031686596     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.19.4993-5002.1998     Document Type: Review
Times cited : (167)

References (136)
  • 2
    • 0029117190 scopus 로고
    • Characterization of the exbBD operon of Escherichia coli and the role of ExbB and ExbD in TonB function and stability
    • Ahmer, B. M. M., M. G. Thomas, R. A. Larsen, and K. Postle. 1995. Characterization of the exbBD operon of Escherichia coli and the role of ExbB and ExbD in TonB function and stability. J. Bacteriol. 177:4742-4747.
    • (1995) J. Bacteriol. , vol.177 , pp. 4742-4747
    • Ahmer, B.M.M.1    Thomas, M.G.2    Larsen, R.A.3    Postle, K.4
  • 3
    • 0025365339 scopus 로고
    • Linkage map of Escherichia coli K-12, edition 8
    • Bachmann, B. J. 1990. Linkage map of Escherichia coli K-12, edition 8. Microbiol. Rev. 54:30-197.
    • (1990) Microbiol. Rev. , vol.54 , pp. 30-197
    • Bachmann, B.J.1
  • 4
    • 15444339008 scopus 로고    scopus 로고
    • Inhibition of OmpF ioop 3 movement reduces colicin N toxicity in vivo
    • abstr. W1, University of East Anglia, Norwich, England
    • Bainbridge, G., G. A. Armstrong, K. F. Whelan, L. G. Dover, and J. H. Lakey. 1998. Inhibition of OmpF ioop 3 movement reduces colicin N toxicity in vivo, abstr. W1, p. 35. In Colicins and Other Bacteriocins Workshop. University of East Anglia, Norwich, England.
    • (1998) Colicins and Other Bacteriocins Workshop , pp. 35
    • Bainbridge, G.1    Armstrong, G.A.2    Whelan, K.F.3    Dover, L.G.4    Lakey, J.H.5
  • 5
    • 0025337694 scopus 로고
    • Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli
    • Bell, P. E., C. D. Nau, J. T. Brown, J. Konisky, and K. J. Kadner. 1990. Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli. J. Bacteriol. 172:3826-3829.
    • (1990) J. Bacteriol. , vol.172 , pp. 3826-3829
    • Bell, P.E.1    Nau, C.D.2    Brown, J.T.3    Konisky, J.4    Kadner, K.J.5
  • 7
    • 77956720132 scopus 로고    scopus 로고
    • Colicin transport, channel formation and inhibition
    • W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.), Elsevier, New York, N.Y.
    • Bénédetti, H., and V. Géli. 1996. Colicin transport, channel formation and inhibition, p. 665-691. In W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.), Handbook of biological physics, vol 2. Elsevier, New York, N.Y.
    • (1996) Handbook of Biological Physics , vol.2 , pp. 665-691
    • Bénédetti, H.1    Géli, V.2
  • 8
    • 0024789570 scopus 로고
    • Comparison of the uptake systems for the entry of various BtuB group colicins into Escherichia coli
    • Bénédetti, H., M. Frenette, D. Baty, R. Lloubès, V. Géli, and C. Lazdunski. 1989. Comparison of the uptake systems for the entry of various BtuB group colicins into Escherichia coli. J. Gen. Microbiol. 135:3413-3420.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 3413-3420
    • Bénédetti, H.1    Frenette, M.2    Baty, D.3    Lloubès, R.4    Géli, V.5    Lazdunski, C.6
  • 9
    • 0026089656 scopus 로고
    • Individual domains of colicins confer specificity in colicin uptake, in pore-properties and in immunity requirements
    • Bénédetti, H., M. Frenette, D. Baty, M. Knibiehler, F. Pattus, and C. Lazdunski. 1991. Individual domains of colicins confer specificity in colicin uptake, in pore-properties and in immunity requirements. J. Mol. Biol. 217: 429-439.
    • (1991) J. Mol. Biol. , vol.217 , pp. 429-439
    • Bénédetti, H.1    Frenette, M.2    Baty, D.3    Knibiehler, M.4    Pattus, F.5    Lazdunski, C.6
  • 10
    • 0025915509 scopus 로고
    • Protein import into Escherichia coli: Colicins A and E1 interact with a component of their translocation system
    • Bénédetti, H., C. Lazdunski, and R. Lloubès. 1991. Protein import into Escherichia coli: colicins A and E1 interact with a component of their translocation system. EMBO J. 10:1989-1995.
    • (1991) EMBO J. , vol.10 , pp. 1989-1995
    • Bénédetti, H.1    Lazdunski, C.2    Lloubès, R.3
  • 12
    • 0026541379 scopus 로고
    • Colicin A unfolds during its translocation in Escherichia coli cells and spans the whole cell envelope when its pore has formed
    • Bénédetti, H., R. Lloubès, C. Lazdunski, and L. Letellier. 1992. Colicin A unfolds during its translocation in Escherichia coli cells and spans the whole cell envelope when its pore has formed. EMBO J. 11:441-447.
    • (1992) EMBO J. , vol.11 , pp. 441-447
    • Bénédetti, H.1    Lloubès, R.2    Lazdunski, C.3    Letellier, L.4
  • 13
    • 0015333430 scopus 로고
    • Specific inhibition of cell division by colicin E2 without degradation of deoxyribonucleic acid in a new colicin sensitivity mutant of Escherichia coli
    • Beppu, T., K. Kawabata, and K. Arima. 1972. Specific inhibition of cell division by colicin E2 without degradation of deoxyribonucleic acid in a new colicin sensitivity mutant of Escherichia coli. J. Bacteriol. 110:485-493.
    • (1972) J. Bacteriol. , vol.110 , pp. 485-493
    • Beppu, T.1    Kawabata, K.2    Arima, K.3
  • 15
    • 15444350969 scopus 로고
    • Identification and characterization of the exbB, exbD and and tonB genes
    • Bitter, W., J. Tommassen, and P. J. Weisbeek. 1993. Identification and characterization of the exbB, exbD and and tonB genes. Mol. Microbiol. 24:169-179.
    • (1993) Mol. Microbiol. , vol.24 , pp. 169-179
    • Bitter, W.1    Tommassen, J.2    Weisbeek, P.J.3
  • 16
    • 0025157076 scopus 로고
    • In vivo properties of colicin A: Channel activity is voltage dependent but translocation may be voltage independent
    • Bourdineaud, J, P., P. Boulanger, C. Lazdunski, and L. Letellier. 1990. In vivo properties of colicin A: channel activity is voltage dependent but translocation may be voltage independent. Proc. Natl. Acad. Sci. USA 87: 1037-1041.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1037-1041
    • Bourdineaud, J.P.1    Boulanger, P.2    Lazdunski, C.3    Letellier, L.4
  • 17
    • 0025114009 scopus 로고
    • Involvement of OmpF during reception and translocation steps of colicin N entry
    • Bourdineaud, J. P., H. Fierobe, C. Lazdunski, and J. M. Pagès. 1990. Involvement of OmpF during reception and translocation steps of colicin N entry. Mol. Microbiol. 4:1737-1743.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1737-1743
    • Bourdineaud, J.P.1    Fierobe, H.2    Lazdunski, C.3    Pagès, J.M.4
  • 18
    • 15444344560 scopus 로고    scopus 로고
    • Unpublished data
    • Bouveret, E. Unpublished data.
    • Bouveret, E.1
  • 20
    • 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., A. Rigal, C. Lazdunski, and H. Bénédetli. 1997. The N-terminal domain of colicin E3 interacts with TolB, which is involved in the colicin translocation step. Mol. Microbiol. 23:909-920.
    • (1997) Mol. Microbiol. , vol.23 , pp. 909-920
    • Bouveret, E.1    Rigal, A.2    Lazdunski, C.3    Bénédetli, H.4
  • 21
    • 0031983893 scopus 로고    scopus 로고
    • Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli
    • Bouveret, E., A. Rigal, C Lazdunski, and H. Bénédetti. 1998. Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli. Mol. Microbiol. 27:143-157.
    • (1998) Mol. Microbiol. , vol.27 , pp. 143-157
    • Bouveret, E.1    Rigal, A.2    Lazdunski, C.3    Bénédetti, H.4
  • 23
    • 0007265453 scopus 로고
    • A new colicin that adsorbs to outer-membrane protein Tsx is dependent on the tonB instead of the tolQ membrane transport system
    • Bradley, D. E., and S. P. Howard. 1992. A new colicin that adsorbs to outer-membrane protein Tsx is dependent on the tonB instead of the tolQ membrane transport system. J. Gen. Microbiol. 135:1857-1863.
    • (1992) J. Gen. Microbiol. , vol.135 , pp. 1857-1863
    • Bradley, D.E.1    Howard, S.P.2
  • 24
    • 0029155042 scopus 로고
    • Energy-coupled transport and signal transduction through the Gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins
    • Braun, V. 1995. Energy-coupled transport and signal transduction through the Gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins. FEMS Microbiol. Rev. 16:295-307.
    • (1995) FEMS Microbiol. Rev. , vol.16 , pp. 295-307
    • Braun, V.1
  • 25
    • 0027193060 scopus 로고
    • Evolutionary relationship of uptake systems for biopolymers in Escherichia coli: Cross-complementation between the TonB-ExbB-ExbD and the TolA-TolQ-TolR proteins
    • Braun, V., and C. Herrmann. 1993. Evolutionary relationship of uptake systems for biopolymers in Escherichia coli: cross-complementation between the TonB-ExbB-ExbD and the TolA-TolQ-TolR proteins. Mol. Microbiol. 8:261-268.
    • (1993) Mol. Microbiol. , vol.8 , pp. 261-268
    • Braun, V.1    Herrmann, C.2
  • 26
    • 0029913411 scopus 로고    scopus 로고
    • Energy-coupled transport across the outer membrane of Escherichia coli: ExbB binds ExbD and TonB in vitro, and leucine 132 in the periplasmic region and aspartate 25 in the transmembrane region are important for ExbD activity
    • Braun, V., S. Gaisser, C. Herrmann, K. Kampfenkel, H. Killmann, and I. Traub. 1996. Energy-coupled transport across the outer membrane of Escherichia coli: ExbB binds ExbD and TonB in vitro, and leucine 132 in the periplasmic region and aspartate 25 in the transmembrane region are important for ExbD activity. J. Bacteriol. 178:2836-2845.
    • (1996) J. Bacteriol. , vol.178 , pp. 2836-2845
    • Braun, V.1    Gaisser, S.2    Herrmann, C.3    Kampfenkel, K.4    Killmann, H.5    Traub, I.6
  • 27
    • 0030026642 scopus 로고    scopus 로고
    • Expression of the tolQRA genes of Escherichia coli K-12 is controlled by the RcsC sensor protein involved in capsule synthesis
    • Clavel, T., J. C. Lazzaroni, A. Vianney, and R. Portalier. 1996. Expression of the tolQRA genes of Escherichia coli K-12 is controlled by the RcsC sensor protein involved in capsule synthesis. Mol. Microbiol. 19:19-25.
    • (1996) Mol. Microbiol. , vol.19 , pp. 19-25
    • Clavel, T.1    Lazzaroni, J.C.2    Vianney, A.3    Portalier, R.4
  • 28
    • 15444347955 scopus 로고    scopus 로고
    • The TolB and Pal proteins of Escherichia coli K-12 form a complex with Lpp and Ompa to link the outer membrane and the peptidoglycan
    • in press
    • Clavel, T., P. Germon, A. Vianney, R. Portalier, and J. C. Lazzaroni. The TolB and Pal proteins of Escherichia coli K-12 form a complex with Lpp and OmpA to link the outer membrane and the peptidoglycan. Mol. Microbiol., in press.
    • Mol. Microbiol.
    • Clavel, T.1    Germon, P.2    Vianney, A.3    Portalier, R.4    Lazzaroni, J.C.5
  • 30
    • 0016524407 scopus 로고
    • Genetics of resistance to colicins in Escherichia coli K-12: Cross-resistance among colicins of group B
    • Davies, J. K., and P. Reeves. 1975. Genetics of resistance to colicins in Escherichia coli K-12: cross-resistance among colicins of group B. J. Bacteriol. 123:96-101.
    • (1975) J. Bacteriol. , vol.123 , pp. 96-101
    • Davies, J.K.1    Reeves, P.2
  • 31
    • 0016524407 scopus 로고
    • Genetics of resistance to colicins in Escherichia coli K-12. Cross-resistance among colicins of group A
    • Davies, J. K., and P. Reeves. 1975. Genetics of resistance to colicins in Escherichia coli K-12. Cross-resistance among colicins of group A. J. Bacteriol. 123:102-117.
    • (1975) J. Bacteriol. , vol.123 , pp. 102-117
    • Davies, J.K.1    Reeves, P.2
  • 32
    • 0023956921 scopus 로고
    • Cloning of genes encoding a 15,000-dalton peptidoglycan-associated outer membrane lipoprotein and an antigenically related 15,000-dalton protein from Haemophilus influenzae
    • Deich, R. A., B. J. Metcalf, C. W. Finn, J. E. Farley, and B. A. Green. 1988. Cloning of genes encoding a 15,000-dalton peptidoglycan-associated outer membrane lipoprotein and an antigenically related 15,000-dalton protein from Haemophilus influenzae. J. Bacteriol. 170:489-498.
    • (1988) J. Bacteriol. , vol.170 , pp. 489-498
    • Deich, R.A.1    Metcalf, B.J.2    Finn, C.W.3    Farley, J.E.4    Green, B.A.5
  • 33
    • 0028828533 scopus 로고
    • Cadaverine induces closing of E. coli porins
    • Dela Vega, A. L., and A. H. Delcour. 1995. Cadaverine induces closing of E. coli porins. EMBO J. 14:6058-6065.
    • (1995) EMBO J. , vol.14 , pp. 6058-6065
    • Dela Vega, A.L.1    Delcour, A.H.2
  • 34
    • 0026691772 scopus 로고
    • Membrane-derived oligosaccharides (MDOs) promote closing of an E. coli porin channel
    • Delcour, A. H., C. Kung, J. Adler, and B. Martinac. 1992. Membrane-derived oligosaccharides (MDOs) promote closing of an E. coli porin channel. FEBS Lett. 304:216-220.
    • (1992) FEBS Lett. , vol.304 , pp. 216-220
    • Delcour, A.H.1    Kung, C.2    Adler, J.3    Martinac, B.4
  • 35
    • 0028263998 scopus 로고
    • The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both Gram-positive and Gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan
    • De Mot, R., and J. Vanderleyden. 1994. The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both Gram-positive and Gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan. Mol. Microbiol. 12:333-334.
    • (1994) Mol. Microbiol. , vol.12 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 36
    • 0029055749 scopus 로고
    • Protein complex within Escherichia coli inner membrane - TolA N-terminal domain interacts with TolQ and TolR proteins
    • Derouiche, R., H. Bénédetti, J. C. Lazzaroni, C. Lazdunski, and R. Lloubès. 1995. Protein complex within Escherichia coli inner membrane - TolA N-terminal domain interacts with TolQ and TolR proteins. J. Biol. Chem. 270: 11078-11084.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11078-11084
    • Derouiche, R.1    Bénédetti, H.2    Lazzaroni, J.C.3    Lazdunski, C.4    Lloubès, R.5
  • 39
    • 0027938907 scopus 로고
    • Unfolding of colicin A during its translocalion through the Escherichia coli envelope as demonstrated by disulfide bond engineering
    • Duché, D., D. Baty, M. Chartier, and L. Letellier. 1994. Unfolding of colicin A during its translocalion through the Escherichia coli envelope as demonstrated by disulfide bond engineering. J. Biol. Chem. 269:24820-24825.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24820-24825
    • Duché, D.1    Baty, D.2    Chartier, M.3    Letellier, L.4
  • 41
    • 0024730355 scopus 로고
    • Import of biopolymers into Escherichia coli: Nucleotide sequences of the exbB and exbD genes are homologous to those of the tolQ and tolR genes, respectively
    • Eick-Helmerich, K., and V. Braun. 1989. Import of biopolymers into Escherichia coli: nucleotide sequences of the exbB and exbD genes are homologous to those of the tolQ and tolR genes, respectively. J. Bacteriol. 171: 5117-5127.
    • (1989) J. Bacteriol. , vol.171 , pp. 5117-5127
    • Eick-Helmerich, K.1    Braun, V.2
  • 42
    • 0031975098 scopus 로고    scopus 로고
    • Role of the Haemophilus ducreyii Ton system in internalization of heme from hemoglobin
    • Elkins, C., P. A. Totton, B. Olsen, and C. E. Thomas. 1998. Role of the Haemophilus ducreyii Ton system in internalization of heme from hemoglobin. Infect. Immun. 66:151-160.
    • (1998) Infect. Immun. , vol.66 , pp. 151-160
    • Elkins, C.1    Totton, P.A.2    Olsen, B.3    Thomas, C.E.4
  • 43
    • 0031569354 scopus 로고    scopus 로고
    • A mechanism for toxin insertion into membranes is suggested by the crystal structure of the channel-forming domain of colicin E1
    • Elkins, P. A., A. Bunker, W. A. Cramer, and C. V. Stauffacher. 1997. A mechanism for toxin insertion into membranes is suggested by the crystal structure of the channel-forming domain of colicin E1. Structure 5:443-458.
    • (1997) Structure , vol.5 , pp. 443-458
    • Elkins, P.A.1    Bunker, A.2    Cramer, W.A.3    Stauffacher, C.V.4
  • 44
    • 0027998804 scopus 로고
    • In vitro approaches to investigation of the early steps of colicin-OmpF interaction
    • El Kouhen, R., A. Hoenger, A. Engel, and J. M. Pagès. 1994. In vitro approaches to investigation of the early steps of colicin-OmpF interaction. Eur. J. Biochem. 224:723-728.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 723-728
    • El Kouhen, R.1    Hoenger, A.2    Engel, A.3    Pagès, J.M.4
  • 45
    • 0028148013 scopus 로고
    • The colicin A pore-forming domain fused to mitochondrial intermembrane space sorting signals can be functionally inserted into the Escherichia coli plasma membrane by a mechanism that bypasses the Tol proteins
    • Espesset, D., Y. Corda, K. Cunningham, H. Bénédetti, R. Lloubès, C. Lazdunski, and V. Géli. 1994. The colicin A pore-forming domain fused to mitochondrial intermembrane space sorting signals can be functionally inserted into the Escherichia coli plasma membrane by a mechanism that bypasses the Tol proteins. Mol. Microbiol. 13:1121-1131.
    • (1994) Mol. Microbiol. , vol.13 , pp. 1121-1131
    • Espesset, D.1    Corda, Y.2    Cunningham, K.3    Bénédetti, H.4    Lloubès, R.5    Lazdunski, C.6    Géli, V.7
  • 46
    • 0029963892 scopus 로고    scopus 로고
    • Direct measurement of the association of a protein with a family of membrane receptors
    • Evans, L. J. A., A. Cooper, and J. H. Lakey. 1996. Direct measurement of the association of a protein with a family of membrane receptors. J. Mol. Biol. 255:559-563.
    • (1996) J. Mol. Biol. , vol.255 , pp. 559-563
    • Evans, L.J.A.1    Cooper, A.2    Lakey, J.H.3
  • 47
    • 0024723058 scopus 로고
    • Involvement of ExbB and TonB in transport across the outer membrane of Escherichia coli: Phenotypic complementation of exb mutants by overexpressed tonB and physical stabilization of TonB by ExbB
    • Fisher, E., K. Günter, and V. Braun. 1989. Involvement of ExbB and TonB in transport across the outer membrane of Escherichia coli: phenotypic complementation of exb mutants by overexpressed tonB and physical stabilization of TonB by ExbB. J. Bacteriol. 171:5127-5134.
    • (1989) J. Bacteriol. , vol.171 , pp. 5127-5134
    • Fisher, E.1    Günter, K.2    Braun, V.3
  • 48
    • 0027152155 scopus 로고
    • Specific regions of Escherichia coli OmpF involved in antigenic and colicin receptor sites and in stable trimerization
    • Fourel, D., S. Mizushima, A. Bernadac, and J. M. Pagès. 1992. Specific regions of Escherichia coli OmpF involved in antigenic and colicin receptor sites and in stable trimerization. J. Bacteriol. 175:2754-2757.
    • (1992) J. Bacteriol. , vol.175 , pp. 2754-2757
    • Fourel, D.1    Mizushima, S.2    Bernadac, A.3    Pagès, J.M.4
  • 49
    • 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
    • Garinot-Schneider, C., C. N. Penfold, G. R. Moore, C. Kleanthous, and R. James. 1997. Identification of residues in the putative TolA box which are essential for the toxicity of the endonuclease toxin colicin E9. Microbiology 143:2931-2938.
    • (1997) Microbiology , vol.143 , pp. 2931-2938
    • Garinot-Schneider, C.1    Penfold, C.N.2    Moore, G.R.3    Kleanthous, C.4    James, R.5
  • 51
    • 0025866063 scopus 로고
    • Regulation of capsular polysaccharide synthesis in Escherichia coli K12
    • Gottesman, S., and V. Stout. 1991. Regulation of capsular polysaccharide synthesis in Escherichia coli K12. Mol. Microbiol. 5:1599-1606.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1599-1606
    • Gottesman, S.1    Stout, V.2
  • 52
    • 0027202188 scopus 로고
    • Phosphate efflux through the channels formed by colicins and phage T5 in Escherichia coli cells is responsible for the fall in cytoplasmic ATP
    • Guihard, G., H. Bénédetti, M. Besnard, and L. Letellier. 1993. Phosphate efflux through the channels formed by colicins and phage T5 in Escherichia coli cells is responsible for the fall in cytoplasmic ATP. J. Biol. Chem. 268: 17775-17780.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17775-17780
    • Guihard, G.1    Bénédetti, H.2    Besnard, M.3    Letellier, L.4
  • 53
    • 0028021691 scopus 로고
    • Colicin A and the Tol proteins involved in its translocation are preferentially located in the contact sites between the inner and outer membranes of Escherichia coli cells
    • Guihard, G., P. Boulanger, H. Bénédetti, R. Lloubès, M. Besnard, and L. Letellier. 1993. Colicin A and the Tol proteins involved in its translocation are preferentially located in the contact sites between the inner and outer membranes of Escherichia coli cells. J. Biol. Chem. 269:5874-5880.
    • (1993) J. Biol. Chem. , vol.269 , pp. 5874-5880
    • Guihard, G.1    Boulanger, P.2    Bénédetti, H.3    Lloubès, R.4    Besnard, M.5    Letellier, L.6
  • 54
    • 0025001648 scopus 로고
    • In vivo evidence for FhuA outer membrane receptor interaction with the TonB inner membrane protein of Escherichia coli
    • Günter, K., and V. Braun. 1990. In vivo evidence for FhuA outer membrane receptor interaction with the TonB inner membrane protein of Escherichia coli. FEBS Lett. 274:85-88.
    • (1990) FEBS Lett. , vol.274 , pp. 85-88
    • Günter, K.1    Braun, V.2
  • 55
    • 0023886391 scopus 로고
    • Suppression of the btuB451 mutation by mutations of the tonB gene suggests a direct interaction between TonB and Ton-dependent receptor proteins in the outer membrane of Escherichia coli
    • Heller, K., R. J. Kadner, and K. Günther. 1988. Suppression of the btuB451 mutation by mutations of the tonB gene suggests a direct interaction between TonB and Ton-dependent receptor proteins in the outer membrane of Escherichia coli. Gene 64:147-153.
    • (1988) Gene , vol.64 , pp. 147-153
    • Heller, K.1    Kadner, R.J.2    Günther, K.3
  • 56
    • 0031568809 scopus 로고    scopus 로고
    • A conserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein g3p from phage fd
    • Holliger, P., and L. Riechmann. 1997. A conserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein g3p from phage fd. Structure 5:265-275.
    • (1997) Structure , vol.5 , pp. 265-275
    • Holliger, P.1    Riechmann, L.2
  • 57
    • 0028043861 scopus 로고
    • Maturation and localization of the TolB protein required for colicin import
    • Isnard, M., A. Rigal, J. C. Lazzaroni, C. Lazdunski, and R. Lloubès. 1994. Maturation and localization of the TolB protein required for colicin import J. Bacteriol. 176:6392-6396.
    • (1994) J. Bacteriol. , vol.176 , pp. 6392-6396
    • Isnard, M.1    Rigal, A.2    Lazzaroni, J.C.3    Lazdunski, C.4    Lloubès, R.5
  • 58
    • 0023697146 scopus 로고
    • A hybrid toxin from bacteriophage f1 attachment protein and colicin E3 has altered cell receptor specificity
    • Jakes, K. S., N. G. Davis, and N. D. Zinder. 1988. A hybrid toxin from bacteriophage f1 attachment protein and colicin E3 has altered cell receptor specificity. J. Bacteriol. 170:4231-4238.
    • (1988) J. Bacteriol. , vol.170 , pp. 4231-4238
    • Jakes, K.S.1    Davis, N.G.2    Zinder, N.D.3
  • 60
    • 0029949518 scopus 로고    scopus 로고
    • The biology of E colicins: Paradigms and paradoxes
    • James, R., C. Kleanthous, and G. R. Moore. 1996. The biology of E colicins: paradigms and paradoxes. Microbiology 142:1569-1580.
    • (1996) Microbiology , vol.142 , pp. 1569-1580
    • James, R.1    Kleanthous, C.2    Moore, G.R.3
  • 61
    • 0028887819 scopus 로고
    • Cloning and sequencing of the Haemophilus influenzae exbB and exbD genes
    • Jarosik, G. P., and E. J. Hansen. 1995. Cloning and sequencing of the Haemophilus influenzae exbB and exbD genes. Gene 152:89-92.
    • (1995) Gene , vol.152 , pp. 89-92
    • Jarosik, G.P.1    Hansen, E.J.2
  • 62
    • 0028280919 scopus 로고
    • Role of the TonB amino terminus in energy transduction between membranes
    • Jaskula, J. C., T. E. Letain, S. K. Roof, J. T. Skare, and K. Postle. 1994. Role of the TonB amino terminus in energy transduction between membranes. J. Bacteriol. 175:2326-2338.
    • (1994) J. Bacteriol. , vol.175 , pp. 2326-2338
    • Jaskula, J.C.1    Letain, T.E.2    Roof, S.K.3    Skare, J.T.4    Postle, K.5
  • 63
    • 0029738322 scopus 로고    scopus 로고
    • Haemonchus contortus GA1 antigens: Related, phospholipase C-sensitive, apical gut membrane proteins encoded as a polyprotein and released from the nematode during infection
    • Jasmer, D. P., L. E. Perryman, and T. C. McGuire. 1996. Haemonchus contortus GA1 antigens: related, phospholipase C-sensitive, apical gut membrane proteins encoded as a polyprotein and released from the nematode during infection. Proc. Natl. Acad. Sci. USA 93:8642-8647.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8642-8647
    • Jasmer, D.P.1    Perryman, L.E.2    McGuire, T.C.3
  • 65
    • 0030926805 scopus 로고    scopus 로고
    • Ligand-specific opening of a gated-porin channel in the outer membrane of living bacteria
    • Jiang, X., M. A. Payne, Z. Cao, S. B. Foster, J. B. Feix, M. C. Newton, and P. E. Klebba. 1997. Ligand-specific opening of a gated-porin channel in the outer membrane of living bacteria. Science 276:1261-1264.
    • (1997) Science , vol.276 , pp. 1261-1264
    • Jiang, X.1    Payne, M.A.2    Cao, Z.3    Foster, S.B.4    Feix, J.B.5    Newton, M.C.6    Klebba, P.E.7
  • 67
    • 0027466914 scopus 로고
    • Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli
    • Kampfenkel, K., and V. Braun. 1992. Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 268:6050-6057.
    • (1992) J. Biol. Chem. , vol.268 , pp. 6050-6057
    • Kampfenkel, K.1    Braun, V.2
  • 68
    • 0027181940 scopus 로고
    • Membrane topologies of the TolQ and TolR proteins of Escherichia coli: Inactivation of TolQ by a missense mutation in the proposed first transmembrane segment
    • Kampfenkel, K., and V. Braun. 1993. Membrane topologies of the TolQ and TolR proteins of Escherichia coli: inactivation of TolQ by a missense mutation in the proposed first transmembrane segment. J. Bacteriol. 175: 4485-4491.
    • (1993) J. Bacteriol. , vol.175 , pp. 4485-4491
    • Kampfenkel, K.1    Braun, V.2
  • 69
    • 0027154838 scopus 로고
    • A sequence-specific function for the N-terminal signal-like sequence of the TonB protein
    • Karlsson, M., K. Hannavy, and C. F. Higgins. 1993. A sequence-specific function for the N-terminal signal-like sequence of the TonB protein. Mol. Microbiol. 8:379-388.
    • (1993) Mol. Microbiol. , vol.8 , pp. 379-388
    • Karlsson, M.1    Hannavy, K.2    Higgins, C.F.3
  • 70
    • 0028942302 scopus 로고
    • Identification of receptor binding sites by competitive peptide mapping: Phages T1, T5, and F80 and colicin M bind the gating loop
    • Killmann, H., G. Vedenov, G. Jung, H. Schwarz, and V. Braun. 1995. Identification of receptor binding sites by competitive peptide mapping: phages T1, T5, and F80 and colicin M bind the gating loop. J. Bacteriol. 177: 694-698.
    • (1995) J. Bacteriol. , vol.177 , pp. 694-698
    • Killmann, H.1    Vedenov, G.2    Jung, G.3    Schwarz, H.4    Braun, V.5
  • 71
    • 15444341761 scopus 로고    scopus 로고
    • Personal communication
    • Klebba, P. Personal communication.
    • Klebba, P.1
  • 72
    • 0029092472 scopus 로고
    • Proposal for a peptidoglycan-associated alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins
    • Koebnik, R. 1995. Proposal for a peptidoglycan-associated alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins. Mol. Microbiol. 16:1269-1270.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1269-1270
    • Koebnik, R.1
  • 73
    • 0020350235 scopus 로고
    • Colicins and other bacteriocins with established modes of action
    • Konisky, J. 1982. Colicins and other bacteriocins with established modes of action. Annu. Rev. Microbiol. 36:125-144.
    • (1982) Annu. Rev. Microbiol. , vol.36 , pp. 125-144
    • Konisky, J.1
  • 74
    • 15444361498 scopus 로고    scopus 로고
    • Unpublished data
    • Lakey, J. Unpublished data.
    • Lakey, J.1
  • 75
    • 0027730652 scopus 로고
    • The conserved proline-rich motif is not essential for energy transduction by Escherichia coli TonB protein
    • Larsen, R. A., G. E. Wood, and K. Postle. 1993. The conserved proline-rich motif is not essential for energy transduction by Escherichia coli TonB protein. Mol. Microbiol. 10:943-953.
    • (1993) Mol. Microbiol. , vol.10 , pp. 943-953
    • Larsen, R.A.1    Wood, G.E.2    Postle, K.3
  • 76
    • 0028145355 scopus 로고
    • Partial suppression of an Escherichia coli TonB transmembrane domain mutation (DV17) by a missense mutation in ExbB
    • Larsen, R. A., M. G. Thomas, G. E. Wood, and K. Postle. 1994. Partial suppression of an Escherichia coli TonB transmembrane domain mutation (DV17) by a missense mutation in ExbB. Mol. Microbiol. 13:627-640.
    • (1994) Mol. Microbiol. , vol.13 , pp. 627-640
    • Larsen, R.A.1    Thomas, M.G.2    Wood, G.E.3    Postle, K.4
  • 77
    • 0029151113 scopus 로고
    • Colicin import and pore formation: A system for studying protein transport across membranes?
    • Lazdunski, C. J. 1995. Colicin import and pore formation: a system for studying protein transport across membranes? Mol. Microbiol. 16:1059-1066.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1059-1066
    • Lazdunski, C.J.1
  • 78
  • 79
  • 80
    • 15444358956 scopus 로고    scopus 로고
    • Personal communication
    • Lazzaroni, J. C. Personal communication.
    • Lazzaroni, J.C.1
  • 81
    • 0026588350 scopus 로고
    • The excC gene of Escherichia coli K-12 required for cell envelope integrity encodes the peptidoglycan-associated lipoprotein (Pal)
    • Lazzaroni, J. C., and R. Portalier. 1992. The excC gene of Escherichia coli K-12 required for cell envelope integrity encodes the peptidoglycan-associated lipoprotein (Pal). Mol. Microbiol. 6:735-742.
    • (1992) Mol. Microbiol. , vol.6 , pp. 735-742
    • Lazzaroni, J.C.1    Portalier, R.2
  • 82
    • 0022569031 scopus 로고
    • Effects of lkyB mutations on the expression of ompF, ompC and lamB porin structural genes in Escherichia coli K-12
    • Lazzaroni, J. C., N. Fognini-Lefebvre, and R. Portalier. 1986. Effects of lkyB mutations on the expression of ompF, ompC and lamB porin structural genes in Escherichia coli K-12. FEMS Microbiol. Lett. 33:235-239.
    • (1986) FEMS Microbiol. Lett. , vol.33 , pp. 235-239
    • Lazzaroni, J.C.1    Fognini-Lefebvre, N.2    Portalier, R.3
  • 84
    • 0030943591 scopus 로고    scopus 로고
    • TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli
    • Letain, T. E., and K. Postle. 1997. TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli. Mol. Microbiol. 24:271-283.
    • (1997) Mol. Microbiol. , vol.24 , pp. 271-283
    • Letain, T.E.1    Postle, K.2
  • 85
    • 0024378898 scopus 로고
    • Nucleotide sequences of the tolA and tolB genes and localization of their products, components of a multistep translocation system in Escherichia coli
    • Levengood, S. K., and R. E. Webster. 1989. Nucleotide sequences of the tolA and tolB genes and localization of their products, components of a multistep translocation system in Escherichia coli. J. Bacteriol. 171:6600-6609.
    • (1989) J. Bacteriol. , vol.171 , pp. 6600-6609
    • Levengood, S.K.1    Webster, R.E.2
  • 86
    • 0025912823 scopus 로고
    • TolA: A membrane protein involved in colicin uptake contains an extended helical region
    • Levengood, S. K., W. F. Beyer, Jr., and R. E. Webster. 1991. TolA: a membrane protein involved in colicin uptake contains an extended helical region. Proc. Natl. Acad. Sci. USA 88:5939-5943.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5939-5943
    • Levengood, S.K.1    Beyer Jr., W.F.2    Webster, R.E.3
  • 87
    • 0027508718 scopus 로고
    • Role of the carboxy-terminal domain of TolA in protein import and integrity of the outer membrane
    • Levengood-Freyermuth, S. K., E. M. Click, and R. E. Webster. 1993. Role of the carboxy-terminal domain of TolA in protein import and integrity of the outer membrane. J. Bacteriol. 175:222-228.
    • (1993) J. Bacteriol. , vol.175 , pp. 222-228
    • Levengood-Freyermuth, S.K.1    Click, E.M.2    Webster, R.E.3
  • 88
    • 17544375221 scopus 로고    scopus 로고
    • Membrane insertion characteristics of the various transmembrane domains of the Escherichia coli TolQ protein
    • Lewin, T. M., and R. E. Webster. 1996. Membrane insertion characteristics of the various transmembrane domains of the Escherichia coli TolQ protein. J. Biol. Chem. 271:14143-14149.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14143-14149
    • Lewin, T.M.1    Webster, R.E.2
  • 89
    • 0028051476 scopus 로고
    • A site-directed spin-labeling study of ligand-induced conformational change in the ferric enterobactin receptor, FepA
    • Liu, J., J. M. Rutz, P. E. Klebba, and J. B. Feix. 1994. A site-directed spin-labeling study of ligand-induced conformational change in the ferric enterobactin receptor, FepA. Biochemistry 33:13274-13283.
    • (1994) Biochemistry , vol.33 , pp. 13274-13283
    • Liu, J.1    Rutz, J.M.2    Klebba, P.E.3    Feix, J.B.4
  • 90
    • 0031911439 scopus 로고    scopus 로고
    • The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p
    • Lubkowski, J., F. Hennecke, A. Plückthun, and A. Wlodawer. 1998. The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p. Nat. Struct. Biol. 5:140-147.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 140-147
    • Lubkowski, J.1    Hennecke, F.2    Plückthun, A.3    Wlodawer, A.4
  • 91
    • 0030663775 scopus 로고    scopus 로고
    • A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli
    • Matsuyama, S., N. Yokota, and H. Tokuda. 1997. A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli. EMBO J. 16:6947-6955.
    • (1997) EMBO J. , vol.16 , pp. 6947-6955
    • Matsuyama, S.1    Yokota, N.2    Tokuda, H.3
  • 92
    • 0025049224 scopus 로고
    • Import-defective colicin B derivatives mutated in the TonB box
    • Mende, J., and V. Braun. 1990. Import-defective colicin B derivatives mutated in the TonB box. Mol. Microbiol. 4:1523-1533.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1523-1533
    • Mende, J.1    Braun, V.2
  • 93
    • 0018566728 scopus 로고
    • A novel peptidoglycan-associated lipoprotein found in the cell envelopes of Pseudomonas aeruginosa and Escherichia coli
    • Mizuno, T. 1979. A novel peptidoglycan-associated lipoprotein found in the cell envelopes of Pseudomonas aeruginosa and Escherichia coli. J. Biochem. 86:991-1000.
    • (1979) J. Biochem. , vol.86 , pp. 991-1000
    • Mizuno, T.1
  • 94
    • 0020267591 scopus 로고
    • The BtuB group Col plasmids and homology between the colicins they encode
    • Mock, M., and A. P. Pugsley. 1982. The BtuB group Col plasmids and homology between the colicins they encode. J. Bacteriol. 150:1069-1076.
    • (1982) J. Bacteriol. , vol.150 , pp. 1069-1076
    • Mock, M.1    Pugsley, A.P.2
  • 95
    • 0028234448 scopus 로고
    • Genetic insertion and exposure of a reporter epitope in the ferrichrome-iron receptor of Escherichia coli K-12
    • Moeck, G. S., B. S. F. Bazzaz, M. F. Gras, T. S. Ravi, M. J. H. Ratcliffe, and J. W. Coulton. 1994. Genetic insertion and exposure of a reporter epitope in the ferrichrome-iron receptor of Escherichia coli K-12. J. Bacteriol. 176: 4250-4259.
    • (1994) J. Bacteriol. , vol.176 , pp. 4250-4259
    • Moeck, G.S.1    Bazzaz, B.S.F.2    Gras, M.F.3    Ravi, T.S.4    Ratcliffe, M.J.H.5    Coulton, J.W.6
  • 96
    • 0027464626 scopus 로고
    • pH-dependent stability and membrane interaction of the pore-forming domain of colicin A
    • Muga, A., J. M. Gonzalez-Manas, J. H. Lakey, F. Pattus, and W. S. Surewicz. 1993. pH-dependent stability and membrane interaction of the pore-forming domain of colicin A. J. Biol. Chem. 268:1553-1557.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1553-1557
    • Muga, A.1    Gonzalez-Manas, J.M.2    Lakey, J.H.3    Pattus, F.4    Surewicz, W.S.5
  • 97
    • 0027169054 scopus 로고
    • Membrane topology of the Escherichia coli TolR protein required for cell envelope integrity
    • Müller, M. M., A. Vianney, J. C. Lazzaroni, R. E. Webster, and R. Portalier. 1993. Membrane topology of the Escherichia coli TolR protein required for cell envelope integrity. J. Bacteriol. 175:6059-6061.
    • (1993) J. Bacteriol. , vol.175 , pp. 6059-6061
    • Müller, M.M.1    Vianney, A.2    Lazzaroni, J.C.3    Webster, R.E.4    Portalier, R.5
  • 98
    • 0014137931 scopus 로고
    • Genetics and physiology of colicin-tolerant mutants of Escherichia coli
    • Nagel de Zwaig, R., and S. E. Luria. 1967. Genetics and physiology of colicin-tolerant mutants of Escherichia coli. J. Bacteriol. 94:1112-1123.
    • (1967) J. Bacteriol. , vol.94 , pp. 1112-1123
    • Nagel De Zwaig, R.1    Luria, S.E.2
  • 100
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaïdo, H., and M. Vaara. 1985. Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 49:1-32.
    • (1985) Microbiol. Rev. , vol.49 , pp. 1-32
    • Nikaïdo, H.1    Vaara, M.2
  • 101
    • 0014303959 scopus 로고
    • Degradation of ribosomes in Escherichia coli cells treated with colicin E2
    • Nose, K., and D. Mizuno. 1968. Degradation of ribosomes in Escherichia coli cells treated with colicin E2. J. Biochem. 64:1-6.
    • (1968) J. Biochem. , vol.64 , pp. 1-6
    • Nose, K.1    Mizuno, D.2
  • 102
    • 0026581661 scopus 로고
    • Refined structure of the pore-forming domain of colicin A at 2.4 Å resolution
    • Parker, M. W., J. P. M. Pastman, F. Pattus, A. D. Tucker, and D. Tsenoglou. 1992. Refined structure of the pore-forming domain of colicin A at 2.4 Å resolution. J. Mol. Biol. 224:639-657.
    • (1992) J. Mol. Biol. , vol.224 , pp. 639-657
    • Parker, M.W.1    Pastman, J.P.M.2    Pattus, F.3    Tucker, A.D.4    Tsenoglou, D.5
  • 103
    • 0028905676 scopus 로고
    • Novel colicin 10: Assignment of four domains to TonB- and TolC-dependent uptake via the Tsx receptor and to pore formation
    • Pilsl, H., and V. Braun. 1995. Novel colicin 10: assignment of four domains to TonB- and TolC-dependent uptake via the Tsx receptor and to pore formation. Mol. Microbiol. 16:57-67.
    • (1995) Mol. Microbiol. , vol.16 , pp. 57-67
    • Pilsl, H.1    Braun, V.2
  • 104
    • 0028817894 scopus 로고
    • Strong function-related homology between the pore-forming colicins K and 5
    • Pilsl, H., and V. Braun. 1995. Strong function-related homology between the pore-forming colicins K and 5. J. Bacteriol. 177:6973-6977.
    • (1995) J. Bacteriol. , vol.177 , pp. 6973-6977
    • Pilsl, H.1    Braun, V.2
  • 106
    • 0029906434 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa tonB gene encodes a novel TonB protein
    • Poole, K., Q. Zhao, S. Neshat, D. E. Heinrichs, and C. R. Dean. 1996. The Pseudomonas aeruginosa tonB gene encodes a novel TonB protein. Microbiology 142:1449-1458.
    • (1996) Microbiology , vol.142 , pp. 1449-1458
    • Poole, K.1    Zhao, Q.2    Neshat, S.3    Heinrichs, D.E.4    Dean, C.R.5
  • 107
    • 0025666854 scopus 로고
    • TonB protein and the gram-negative dilemma
    • Postle, K. 1990. TonB protein and the gram-negative dilemma. Mol. Microbiol. 4:2019-2026.
    • (1990) Mol. Microbiol. , vol.4 , pp. 2019-2026
    • Postle, K.1
  • 108
    • 0027752437 scopus 로고
    • TonB protein and energy transduction between membranes
    • Postle, K. 1993. TonB protein and energy transduction between membranes. J. Bioenerg. Biomembr. 25:591-601.
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 591-601
    • Postle, K.1
  • 109
    • 15444352459 scopus 로고    scopus 로고
    • Unpublished data
    • Postle, K. Unpublished data.
    • Postle, K.1
  • 110
    • 0023715782 scopus 로고
    • Escherichia coli TonB proteins exported from the cytoplasm without proteolytic cleavage of its amino terminus
    • Postle, K., and J. T. Skare. 1988. Escherichia coli TonB proteins exported from the cytoplasm without proteolytic cleavage of its amino terminus. J. Biol. Chem. 263:11000-11007.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11000-11007
    • Postle, K.1    Skare, J.T.2
  • 111
    • 0024022151 scopus 로고
    • Genetics of the iron dicitrate transport system of Escherichia coli
    • Pressler, U., H. Staudenmaier, L. Zimmermann, and V. Braun. 1981. Genetics of the iron dicitrate transport system of Escherichia coli. J. Bacteriol. 170:2716-2724.
    • (1981) J. Bacteriol. , vol.170 , pp. 2716-2724
    • Pressler, U.1    Staudenmaier, H.2    Zimmermann, L.3    Braun, V.4
  • 112
    • 0021548002 scopus 로고
    • The ins and outs of colicins. Part I. Production and translocation across membranes
    • Pugsley, A. P. 1984. The ins and outs of colicins. Part I. Production and translocation across membranes. Microbiol. Sci. 1:168-175.
    • (1984) Microbiol. Sci. , vol.1 , pp. 168-175
    • Pugsley, A.P.1
  • 113
    • 0021561221 scopus 로고
    • The ins and outs of colicins. Part II. Lethal action, immunity and ecological implications
    • Pugsley, A. P. 1984. The ins and outs of colicins. Part II. Lethal action, immunity and ecological implications. Microbiol. Sci. 1:203-205.
    • (1984) Microbiol. Sci. , vol.1 , pp. 203-205
    • Pugsley, A.P.1
  • 114
    • 15444340752 scopus 로고    scopus 로고
    • Biophysical characterisation of a novel colicin N-TolA binding region
    • abstr. 8, University of East Anglia, Norwich, England
    • Raggett, E. M., G. Bainbridge, L. J. Evans, A. Cooper, and J. H. Lakey. 1998. Biophysical characterisation of a novel colicin N-TolA binding region, abstr. 8, p. 15. In Colicins and Other Bacteriocins Workshop. University of East Anglia, Norwich, England.
    • (1998) Colicins and Other Bacteriocins Workshop , pp. 15
    • Raggett, E.M.1    Bainbridge, G.2    Evans, L.J.3    Cooper, A.4    Lakey, J.H.5
  • 115
    • 0024790115 scopus 로고
    • Nucleotide sequences of Erwinia chrysanthemi ogl and pelE genes negatively regulated by the kdgR gene product
    • Reverchon, S., Y. Huan, C. Bourson, and J. Robert-Boudouy. 1989. Nucleotide sequences of Erwinia chrysanthemi ogl and pelE genes negatively regulated by the kdgR gene product. Gene 85:125-134.
    • (1989) Gene , vol.85 , pp. 125-134
    • Reverchon, S.1    Huan, Y.2    Bourson, C.3    Robert-Boudouy, J.4
  • 117
    • 0027324050 scopus 로고
    • Positive selection for colicin diversity in bacteria
    • Riley, M. A. 1993. Positive selection for colicin diversity in bacteria. Mol. Biol. Evol. 10:1048-1059.
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 1048-1059
    • Riley, M.A.1
  • 118
    • 0029928154 scopus 로고    scopus 로고
    • The Pseudomonas putida peptidoglycan-associated outer membrane lipoprotein is involved in maintenance of the integrity of the cell envelope
    • Rodriguez-Herva, J. J., M. I. Ramos-Gonzalez, and J. L. Ramos. 1996. The Pseudomonas putida peptidoglycan-associated outer membrane lipoprotein is involved in maintenance of the integrity of the cell envelope. J. Bacteriol. 178:1699-1706.
    • (1996) J. Bacteriol. , vol.178 , pp. 1699-1706
    • Rodriguez-Herva, J.J.1    Ramos-Gonzalez, M.I.2    Ramos, J.L.3
  • 119
    • 0025992835 scopus 로고
    • Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions
    • Roof, S. K., J. D. Allard, K. P. Bertrand, and K. Postle. 1991. Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions. J. Bacteriol. 173:5554-5557.
    • (1991) J. Bacteriol. , vol.173 , pp. 5554-5557
    • Roof, S.K.1    Allard, J.D.2    Bertrand, K.P.3    Postle, K.4
  • 121
    • 0030944701 scopus 로고    scopus 로고
    • The TolA protein interacts with colicin E1 differently than with other group A colicins
    • Schendel, S. L., E. M. Click, R. E. Webster, and W. A. Cramer. 1997. The TolA protein interacts with colicin E1 differently than with other group A colicins. J. Bacteriol. 179:3683-3690.
    • (1997) J. Bacteriol. , vol.179 , pp. 3683-3690
    • Schendel, S.L.1    Click, E.M.2    Webster, R.E.3    Cramer, W.A.4
  • 122
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
    • Schirmer, T., T. A. Keller, Y. F. Wang, and J. P. Rosenbush. 1995. Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science 267:512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbush, J.P.4
  • 123
    • 0024676062 scopus 로고
    • Transport across the outer membrane of Escherichia coli via the FhuA receptor is regulated by the TonB protein of the cytoplasmic membrane
    • Schöffler, H., and V. Braun. 1989. Transport across the outer membrane of Escherichia coli via the FhuA receptor is regulated by the TonB protein of the cytoplasmic membrane. Mol. Gen. Genet. 217:378-383.
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 378-383
    • Schöffler, H.1    Braun, V.2
  • 124
    • 0023218137 scopus 로고
    • Nucleotide sequence of the colicin B activity gene cba: Consensus pentapeptide among TonB-dependent colicins and receptors
    • Schramm, E., J. Mende, V. Braun, and R. M. Kamp. 1987. Nucleotide sequence of the colicin B activity gene cba: consensus pentapeptide among TonB-dependent colicins and receptors. J. Bacteriol. 169:3350-3357.
    • (1987) J. Bacteriol. , vol.169 , pp. 3350-3357
    • Schramm, E.1    Mende, J.2    Braun, V.3    Kamp, R.M.4
  • 125
    • 0026344184 scopus 로고
    • Evidence for a TolB-dependent energy transduction complex in Escherichia coli
    • Skare, J. T., and K. Postle. 1991. Evidence for a TolB-dependent energy transduction complex in Escherichia coli. Mol. Microbiol. 5:2883-2890.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2883-2890
    • Skare, J.T.1    Postle, K.2
  • 126
    • 0027282061 scopus 로고
    • Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vitro to the outer membrane receptor FepA
    • Skare, J. T., B. M. M. Ahmer, C. L. Seachord, R. P. Darveau, and K. Postle. 1993. Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vitro to the outer membrane receptor FepA. J. Biol. Chem. 268:16302-16308.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16302-16308
    • Skare, J.T.1    Ahmer, B.M.M.2    Seachord, C.L.3    Darveau, R.P.4    Postle, K.5
  • 127
    • 0028100898 scopus 로고
    • Identification of a translocated protein segment in a voltage-dependent channel
    • Slatin, S. L., X. Q. Qui, K. S. Jakes, and A. Finkelstein. 1994. Identification of a translocated protein segment in a voltage-dependent channel. Nature 371:158-161.
    • (1994) Nature , vol.371 , pp. 158-161
    • Slatin, S.L.1    Qui, X.Q.2    Jakes, K.S.3    Finkelstein, A.4
  • 128
    • 0023225017 scopus 로고
    • Nucleotide sequence of a gene cluster involved in entry of E colicins and single-stranded DNA of infecting filamentous bacteriophages into Escherichia coli
    • Sun, T. P., and R. E. Webster. 1987. Nucleotide sequence of a gene cluster involved in entry of E colicins and single-stranded DNA of infecting filamentous bacteriophages into Escherichia coli. J. Bacteriol. 169:2667-2674.
    • (1987) J. Bacteriol. , vol.169 , pp. 2667-2674
    • Sun, T.P.1    Webster, R.E.2
  • 129
    • 0027530729 scopus 로고
    • Role of tol genes in cloacin DF13 susceptibility of Escherichia coli K-12 stains expressing the cloacin DF13-aerobactin receptor IutA
    • Thomas, J. A., and M. A. Valvano. 1993. Role of tol genes in cloacin DF13 susceptibility of Escherichia coli K-12 stains expressing the cloacin DF13-aerobactin receptor IutA. J. Bacteriol. 175:548-552.
    • (1993) J. Bacteriol. , vol.175 , pp. 548-552
    • Thomas, J.A.1    Valvano, M.A.2
  • 130
    • 0027936377 scopus 로고
    • Molecular cloning, nucleotide sequence, and occurrence of a 16.5-kilodalton outer membrane protein of Brucella abortus with similar to Pal lipoproteins
    • Tibor, A., V. Weynants, P. Denoel, B. Lichtfouse, X. De Bolle, E. Saman, J. N. Limet, and J.-J. Letesson. 1994. Molecular cloning, nucleotide sequence, and occurrence of a 16.5-kilodalton outer membrane protein of Brucella abortus with similar to Pal lipoproteins. Infect. Immun. 62:3633-3639.
    • (1994) Infect. Immun. , vol.62 , pp. 3633-3639
    • Tibor, A.1    Weynants, V.2    Denoel, P.3    Lichtfouse, B.4    De Bolle, X.5    Saman, E.6    Limet, J.N.7    Letesson, J.-J.8
  • 131
    • 0026533769 scopus 로고
    • In vivo inhibition ot TonB-dependent processes by a TonB box consensus pentapeptide
    • Tuckman, M., and M. S. Osburn. 1992. In vivo inhibition ot TonB-dependent processes by a TonB box consensus pentapeptide. J. Bacteriol. 174: 320-323.
    • (1992) J. Bacteriol. , vol.174 , pp. 320-323
    • Tuckman, M.1    Osburn, M.S.2
  • 132
    • 0028009448 scopus 로고
    • Membrane topology and mutational analysis of the TolQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity
    • Vianney, A., T. M. Lewin, W. F. Beyer Jr., J. C. Lazzaroni, R. Portalier, and R. E. Webster. 1994. Membrane topology and mutational analysis of the TolQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity. J. Bacteriol. 176:822-829.
    • (1994) J. Bacteriol. , vol.176 , pp. 822-829
    • Vianney, A.1    Lewin, T.M.2    Beyer Jr., W.F.3    Lazzaroni, J.C.4    Portalier, R.5    Webster, R.E.6
  • 133
    • 8944230187 scopus 로고    scopus 로고
    • Characterization of the tol-pal region of Escherichia coli K-12: Translational control ot tolR expression by TolQ and identification of a new open reading frame downstream of pal encoding a periplasmic protein
    • Vianney, A., M. M. Müller, T. Clavel, J. C. Lazzaroni, R. Portalier, and R. E. Webster. 1996. Characterization of the tol-pal region of Escherichia coli K-12: translational control ot tolR expression by TolQ and identification of a new open reading frame downstream of pal encoding a periplasmic protein. J. Bacteriol. 178:4031-1038.
    • (1996) J. Bacteriol. , vol.178 , pp. 4031-11038
    • Vianney, A.1    Müller, M.M.2    Clavel, T.3    Lazzaroni, J.C.4    Portalier, R.5    Webster, R.E.6
  • 135
    • 0028291154 scopus 로고
    • Repression of tonB transcription during anaerobic growth requires fur binding at the promoter and a second factor binding upstream
    • Young, G. M., and K. Postle. 1994. Repression of tonB transcription during anaerobic growth requires Fur binding at the promoter and a second factor binding upstream. Mol. Microbiol. 11:943-954.
    • (1994) Mol. Microbiol. , vol.11 , pp. 943-954
    • Young, G.M.1    Postle, K.2
  • 136
    • 0027105109 scopus 로고
    • Constraints imposed by protease accessibility on the trans-membrane and surface topography of the colicin E1 ion channel
    • Zhang, Y. L., and W. A. Cramer. 1992. Constraints imposed by protease accessibility on the trans-membrane and surface topography of the colicin E1 ion channel. Protein Sci. 1:1666-1676.
    • (1992) Protein Sci. , vol.1 , pp. 1666-1676
    • Zhang, Y.L.1    Cramer, W.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.