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Volumn 73, Issue 4, 2009, Pages 571-585

Genome-wide screens: Novel mecnanisms in colicin import and cytotoxicity

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ANTIGEN; COLICIN; COLICIN A; COLICIN B; COLICIN D; COLICIN E1; GENE PRODUCT; GLUCOSE; LIPOPOLYSACCHARIDE; LIPOPROTEIN; PEPTIDOGLYCAN; PERIPLASMIC PROTEIN; TRANSLOCON; UNCLASSIFIED DRUG;

EID: 70350157946     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06788.x     Document Type: Article
Times cited : (38)

References (86)
  • 1
    • 0034518219 scopus 로고    scopus 로고
    • YeiL, the third member of the CRP-FNR family in Escherichia coli
    • Anjum, M.F., Green, J., and Guest, J.R. (2000) YeiL, the third member of the CRP-FNR family in Escherichia coli. Microbiology 146 (Pt 12): 3157-3170.
    • (2000) Microbiology , vol.146 , Issue.PART 12 , pp. 3157-3170
    • Anjum, M.F.1    Green, J.2    Guest, J.R.3
  • 2
    • 65249096720 scopus 로고    scopus 로고
    • Structure and function of colicin S4, a colicin with a duplicated receptorbinding domain
    • Arnold, T., Zeth, K., and Linke, D. (2009) Structure and function of colicin S4, a colicin with a duplicated receptorbinding domain. J Bid Chem 284: 6403-6413.
    • (2009) J Bid Chem , vol.284 , pp. 6403-6413
    • Arnold, T.1    Zeth, K.2    Linke, D.3
  • 4
    • 40049110400 scopus 로고    scopus 로고
    • Colicin N Binds to the Periphery of Its Receptor and Translocator, Outer Membrane Protein F
    • DOI 10.1016/j.str.2007.12.023, PII S0969212608000555
    • Baboolal, T.G., Conroy, M.J., Gill, K., Ridley, H., Visudtiphole, V., Bullough, P.A., and Lakey, J.H. (2008) Colicin N binds to the periphery of its receptor and translocator, outer membrane protein F. Structure 16: 371-379. (Pubitemid 351324119)
    • (2008) Structure , vol.16 , Issue.3 , pp. 371-379
    • Baboolal, T.G.1    Conroy, M.J.2    Gill, K.3    Ridley, H.4    Visudtiphole, V.5    Bullough, P.A.6    Lakey, J.7
  • 5
    • 23644456999 scopus 로고    scopus 로고
    • The Escherichia coli CpxA-CpxR envelope stress response system regulates expression of the porins OmpF and OmpC
    • DOI 10.1128/JB.187.16.5723-5731.2005
    • Batchelor, E., Walthers, D., Kenney, L.J., and Goulian, M. (2005) The Escherichia coli CpxA-CpxR envelope stress response system regulates expression of the porins OmpF and OmpC. J Bacteriol 187: 5723-5731. (Pubitemid 41134309)
    • (2005) Journal of Bacteriology , vol.187 , Issue.16 , pp. 5723-5731
    • Batchelor, E.1    Walthers, D.2    Kenney, L.J.3    Goulian, M.4
  • 6
    • 0024789570 scopus 로고
    • Comparison of the uptake systems for the entry of various BtuB group colicins into Escherichia coli
    • Benedetti, H., Frenette, M., Baty, D., Lloubes, R., Geli, V., and Lazdunski, C. (1989) Comparison of the uptake systems for the entry of various BtuB group colicins into Escherichia coli. J Gen Microbiol 135: 3413-3420. (Pubitemid 20034323)
    • (1989) Journal of General Microbiology , vol.135 , Issue.12 , pp. 3413-3420
    • Benedetti, H.1    Frenette, M.2    Baty, D.3    Lloubes, R.4    Geli, V.5    Lazdunski, C.6
  • 7
    • 0026089656 scopus 로고
    • Individual domains of colicins confer specificity in colicin uptake, in pore-properties and in immunity requirement
    • Benedetti, H., Frenette, M., Baty, D., Knibiehler, M., Pattus, F., and Lazdunski, C. (1991) Individual domains of colicins confer specificity in colicin uptake, in pore-properties and in immunity requirement. J Mol Biol 217: 429-439. (Pubitemid 121003291)
    • (1991) Journal of Molecular Biology , vol.217 , Issue.3 , pp. 429-439
    • Benedetti, H.1    Frenette, M.2    Baty, D.3    Knibiehler, M.4    Pattus, F.5    Lazdunski, C.6
  • 8
    • 34249897492 scopus 로고    scopus 로고
    • A dynamic machinery for import of mitochondrial precursor proteins
    • DOI 10.1016/j.febslet.2007.03.004, PII S0014579307002530, Vienna Special Issue: Molecular Machines
    • Bohnert, M., Ranner, N., and van der Laan, M. (2007) Adynamic machinery for import of mitochondrial precursor proteins. FEBS Lett 581: 2802-2810. (Pubitemid 46874382)
    • (2007) FEBS Letters , vol.581 , Issue.15 , pp. 2802-2810
    • Bohnert, M.1    Pfanner, N.2    Van, D.L.M.3
  • 9
    • 37849035983 scopus 로고    scopus 로고
    • Multiple pathways for sorting mitochondrial precursor proteins
    • Bolender, N., Sickmann, A., Wagner, R., Meisinger, C., and Ranner, N. (2008) Multiple pathways for sorting mitochondrial precursor proteins. EMBO Rep 9: 42-49.
    • (2008) EMBO Rep , vol.9 , pp. 42-49
    • Bolender, N.1    Sickmann, A.2    Wagner, R.3    Meisinger, C.4    Ranner, N.5
  • 10
    • 59149099439 scopus 로고    scopus 로고
    • Colicins exploit native disorder to gain cell entry: A hitchhiker's guide to translocation
    • Bonsor, D.A., Meenan, N.A., and Kleanthous, C. (2008) Colicins exploit native disorder to gain cell entry: a hitchhiker's guide to translocation. Biochem Soc Trans 36: 1409-1413.
    • (2008) Biochem Soc Trans , vol.36 , pp. 1409-1413
    • Bonsor, D.A.1    Meenan, N.A.2    Kleanthous, C.3
  • 11
    • 0029045244 scopus 로고
    • Peptidoglycan-associated lipoprotein-ToIB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli
    • Bouveret, E., Derouiche, R., Rigal, A., Lloubes, R., Lazdunski, C., and Benedetti, H. (1995) Peptidoglycan-associated lipoprotein-ToIB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli. J Biol Chem 270: 11071-11077.
    • (1995) J Biol Chem , vol.270 , pp. 11071-11077
    • Bouveret, E.1    Derouiche, R.2    Rigal, A.3    Lloubes, R.4    Lazdunski, C.5    Benedetti, H.6
  • 12
    • 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., and Benedetti, H. (1997) The N-terminal domain of colicin E3 interacts with ToIB which is involved in the colicin translocation step. Mol Microbiol 23: 909-920. (Pubitemid 27096727)
    • (1997) Molecular Microbiology , vol.23 , Issue.5 , pp. 909-920
    • Bouveret, E.1    Rigal, A.2    Lazdunski, C.3    Benedetti, H.4
  • 13
    • 0344631755 scopus 로고    scopus 로고
    • In vitro characterization of peptidoglycan-associated lipoprotein (PAL)- Peptidoglycan and PAL-TolB interactions
    • Bouveret, E., Benedetti, H., Rigal, A., Loret, E., and Lazdunski, C. (1999) In vitro characterization of peptidoglycanassociated lipoprotein (PAL)-peptidoglycan and PAL-ToIB interactions. J Bacterid 181: 6306-6311. (Pubitemid 29512939)
    • (1999) Journal of Bacteriology , vol.181 , Issue.20 , pp. 6306-6311
    • Bouveret, E.1    Benedetti, H.2    Rigal, A.3    Loret, E.4    Lazdunski, C.5
  • 14
    • 0036589164 scopus 로고    scopus 로고
    • Ton-dependent colicins and microcins: Modular design and evolution
    • DOI 10.1016/S0300-9084(02)01427-X, PII S030090840201427X
    • Braun, V., Patzer, S.I., and Hantke, K. (2002) Ton-dependent colicins and microcins: modular design and evolution. Biochimie 84: 365-380. (Pubitemid 35350867)
    • (2002) Biochimie , vol.84 , Issue.5-6 , pp. 365-380
    • Braun, V.1    Patzer, S.I.2    Hantke, K.3
  • 15
    • 0033637616 scopus 로고    scopus 로고
    • Proton motive force drives the interaction of the inner membrane TolA and outer membrane pal proteins in Escherichia coli
    • Cascales, E., Gavioli, M., Sturgis, J.N., and Lloubes, R. (2000) Proton motive force drives the interaction of the inner membrane TolA and outer membrane pal proteins in Escherichia coli. Mol Microbiol 38: 904-915.
    • (2000) Mol Microbiol , vol.38 , pp. 904-915
    • Cascales, E.1    Gavioli, M.2    Sturgis, J.N.3    Lloubes, R.4
  • 16
    • 0036180995 scopus 로고    scopus 로고
    • Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity
    • Cáscales, E., Bemadac, A., Gavioli, M., Lazzaroni, J.C., and Lloubes, R. (2002) Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity. J Bacteriol 184: 754-759. (Pubitemid 34150222)
    • (2002) Journal of Bacteriology , vol.184 , Issue.3 , pp. 754-759
    • Cascales, E.1    Bernadac, A.2    Gavioli, M.3    Lazzaroni, J.-C.4    Lloubes, R.5
  • 18
    • 0018485436 scopus 로고
    • Purification and molecular properties of a new colicin
    • Cavard, D., and Lazdunski, C.J. (1979) Purification and molecular properties of a new colicin. Eur J Biochem 96: 519-524.
    • (1979) Eur J Biochem , vol.96 , pp. 519-524
    • Cavard, D.1    Lazdunski, C.J.2
  • 19
    • 0031848939 scopus 로고    scopus 로고
    • TolB protein of Escherichia coli K-12 interacts with the outer membrane peptidoglycan-associated proteins Pal, Lpp and OmpA
    • DOI 10.1046/j.1365-2958.1998.00945.x
    • Clavel, T., Germon, P., Vianney, A., Portalier, R., and Lazzaroni, J.C. (1998) ToIB protein of Escherichia coli K-12 interacts with the outer membrane peptidoglycanassociated proteins Pal, Lpp and OmpA. Mol Microbiol 29: 359-367. (Pubitemid 28318587)
    • (1998) Molecular Microbiology , vol.29 , Issue.1 , pp. 359-367
    • Clavel, T.1    Germon, P.2    Vianney, A.3    Portalier, R.4    Lazzaroni, J.C.5
  • 20
    • 0031765192 scopus 로고    scopus 로고
    • Accumulation of the enterobacterial common antigen lipid II biosynthetic intermediate stimulates degP transcription in Escherichia coli
    • Danese, P.N., Oliver, G.R., Barr, K., Bowman, G.D., Rick, P.D., and Silhavy, T.J. (1998) Accumulation of the enterobacterial common antigen lipid II biosynthetic intermediate stimulates degP transcription in Escherichia coli. J Bacteriol 180: 5875-5884. (Pubitemid 28514203)
    • (1998) Journal of Bacteriology , vol.180 , Issue.22 , pp. 5875-5884
    • Danese, P.N.1    Oliver, G.R.2    Barr, K.3    Bowman, G.D.4    Rick, P.D.5    Silhavy, T.J.6
  • 21
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Dateenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Dateenko, K.A.1    Wanner, B.L.2
  • 22
    • 0016524407 scopus 로고
    • Genetics of resistance to colicins in Escherichia coli K-12: Cross-resistance among colicins of group A
    • Davies, J.K., and Reeves, P. (1975a) 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
  • 23
    • 0016524407 scopus 로고
    • Genetics of resistance to colicins in Escherichia coli K-12: Cross-resistance among colicins of group B
    • Davies, J.K., and Reeves, P. (1975b) 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
  • 25
    • 34249792101 scopus 로고    scopus 로고
    • Colicin E2 is still in contact with its receptor and import machinery when its nuclease domain enters the cytoplasm
    • Duche, D. (2007) Colicin E2 is still in contact with its receptor and import machinery when its nuclease domain enters the cytoplasm. J Bacteriol 189: 4217-4222.
    • (2007) J Bacteriol , vol.189 , pp. 4217-4222
    • Duche, D.1
  • 26
    • 33845456098 scopus 로고    scopus 로고
    • Release of immunity protein requires functional endonuclease colicin import machinery
    • DOI 10.1128/JB.00941-06
    • Duche, D., Frenkian, A., Prima, V., and Lloubes, R. (2006) Release of immunity protein requires functional endonuclease colicin import machinery. J Bacteriol 188: 8593-8600. (Pubitemid 44894060)
    • (2006) Journal of Bacteriology , vol.188 , Issue.24 , pp. 8593-8600
    • Duche, D.1    Frenkian, A.2    Prima, V.3    Lloubes, R.4
  • 27
    • 58149133744 scopus 로고    scopus 로고
    • Immunity protein protects colicin E2 from OmpT protease
    • Duche, D., Issouf, M., and Lloubes, R. (2009) Immunity protein protects colicin E2 from OmpT protease. J Biochem 145: 95-101.
    • (2009) J Biochem , vol.145 , pp. 95-101
    • Duche, D.1    Issouf, M.2    Lloubes, R.3
  • 28
    • 0029963892 scopus 로고    scopus 로고
    • Direct measurement of the association of a protein with a family of membrane receptors
    • DOI 10.1006/jmbi.1996.0047
    • Evans, L.J., Cooper, A., and Lakey, J.H. (1996a) Direct measurement of the association of a protein with a family of membrane receptors. J Mol Biol 255: 559-563. (Pubitemid 26107186)
    • (1996) Journal of Molecular Biology , vol.255 , Issue.4 , pp. 559-563
    • Evans, L.J.A.1    Cooper, A.2    Lakey, J.H.3
  • 29
    • 0029857393 scopus 로고    scopus 로고
    • The central domain of colicin N possesses the receptor recognition site but not the binding affinity of the whole toxin
    • DOI 10.1021/bi9615497
    • Evans, L.J., Labeit, S., Cooper, A., Bond, L.H., and Lakey, J.H. (1996b) The central domain of colicin N possesses the receptor recognition site but not the binding affinity of the whole toxin. Biochemistry 35: 15143-15148. (Pubitemid 26408845)
    • (1996) Biochemistry , vol.35 , Issue.48 , pp. 15143-15148
    • Evans, L.J.A.1    Labeit, S.2    Cooper, A.3    Bond, L.H.4    Lakey, J.H.5
  • 30
    • 0034660537 scopus 로고    scopus 로고
    • A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins
    • DOI 10.1016/S0969-2126(00)00143-X
    • Ferguson, A.D., Weite, W., Hofmann, E., Lindner, B., Holst, O., Coulton, J.W., and Diederichs, K. (2000) A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins. Structure 8: 585-592. (Pubitemid 30409311)
    • (2000) Structure , vol.8 , Issue.6 , pp. 585-592
    • Ferguson, A.D.1    Welte, W.2    Hofmann, E.3    Lindner, B.4    Holst, O.5    Coulton, J.W.6    Diederichs, K.7
  • 31
    • 0023410503 scopus 로고
    • TolA, tolB and excC, three cistrons involved in the control of pleiotropic release of periplasms proteins by Escherichia coli K12
    • Fognini-Lefebvre, N., Lazzaroni, J.C., and Portalier, R. (1987) tolA, tolB and excC, three cistrons involved in the control of pleiotropic release of periplasms proteins by Escherichia coli K12. Mol Gen Genet 209: 391-395.
    • (1987) Mol Gen Genet , vol.209 , pp. 391-395
    • Fognini-Lefebvre, N.1    Lazzaroni, J.C.2    Portalier, R.3
  • 32
    • 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., Penfold, C.N., Moore, G.R., Kleanthous, C., and James, R. (1997) Identification of residues in the putative TolA box which are essential for the toxicity of the endonuclease toxin colicin E9. Microbiology 143 (R 9): 2931-2938. (Pubitemid 27437909)
    • (1997) Microbiology , vol.143 , Issue.9 , pp. 2931-2938
    • Garinot-Schneider, C.1    Penfold, C.N.2    Moore, G.R.3    Kleanthous, C.4    James, R.5
  • 35
    • 1242297815 scopus 로고    scopus 로고
    • Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 Â resolution
    • DOI 10.1111/j.1365-2958.2003.03884.x
    • Hilsenbeck, J.L., Park, H., Chen, G., Youn, B., Postle, K., and Kang, C. (2004) Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 Â resolution. Mol Microbiol 51: 711-720. (Pubitemid 38233938)
    • (2004) Molecular Microbiology , vol.51 , Issue.3 , pp. 711-720
    • Hilsenbeck, J.L.1    Park, H.2    Chen, G.3    Youn, B.4    Postle, K.5    Kang, C.6
  • 37
    • 47749139311 scopus 로고    scopus 로고
    • Periplasmic chaperone FkpA is essential for imported colicin M toxicity
    • DOI 10.1111/j.1365-2958.2008.06327.x
    • Hullmann, J., Patzer, S.I., Romer, C., Hantke, K., and Braun, V. (2008) Periplasmic chaperone FkpA is essential for imported colicin M toxicity. Mol Microbiol 69: 926-937. (Pubitemid 352033311)
    • (2008) Molecular Microbiology , vol.69 , Issue.4 , pp. 926-937
    • Hullmann, J.1    Patzer, S.I.2    Romer, C.3    Hantke, K.4    Braun, V.5
  • 38
    • 0020326087 scopus 로고
    • The receptor for colicin E3. Isolation and some properties
    • Imajoh, S., Ohno-lwashita, Y., and lmahori, K. (1982) The receptor for colicin E3. Isolation and some properties. J Biol Chem 257: 6481-6487.
    • (1982) J Biol Chem , vol.257 , pp. 6481-6487
    • Imajoh, S.1    Ohno-lwashita, Y.2    Lmahori, K.3
  • 39
    • 0028608101 scopus 로고
    • A single amino acid substitution can restore the solubility of aggregated colicin A mutants in Escherichia coli
    • Izard, J., Parker, M.W., Chartier, M., Duche, D., and Baty, D. (1994) A single amino acid substitution can restore the solubility of aggregated colicin A mutants in Escherichia coli. Protein Eng 7: 1495-1500.
    • (1994) Protein Eng , vol.7 , pp. 1495-1500
    • Izard, J.1    Parker, M.W.2    Chartier, M.3    Duche, D.4    Baty, D.5
  • 40
    • 0036589253 scopus 로고    scopus 로고
    • Killing of E. coli cells by e group nuclease colicins
    • DOI 10.1016/S0300-9084(02)01450-5, PII S0300908402014505
    • James, R., Penfold, C.N., Moore, G.R., and Kleanthous, C. (2002) Killing of E coli cells by E group nuclease colicins. Biochimie 84: 381-389. (Pubitemid 35350868)
    • (2002) Biochimie , vol.84 , Issue.5-6 , pp. 381-389
    • James, R.1    Penfold, C.N.2    Moore, G.R.3    Kleanthous, C.4
  • 41
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): Unique resources for biological research
    • Kitagawa, M., Ara, T., Arifuzzaman, M., loka-Nakamichi, T., Inamoto, E., Toyonaga, H., and Mori, H. (2005) Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res 12: 291-299.
    • (2005) DNA Res , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Loka-Nakamichi, T.4    Inamoto, E.5    Toyonaga, H.6    Mori, H.7
  • 42
  • 45
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar, S.W., and Kolter, R. (1996) Sur A assists the folding of Escherichia coli outer membrane proteins. J Bacteriol 178: 1770-1773. (Pubitemid 26085629)
    • (1996) Journal of Bacteriology , vol.178 , Issue.6 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 47
    • 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 Portalier, R. (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
  • 48
    • 0032774018 scopus 로고    scopus 로고
    • The Tol proteins of Escherichia coli and their involvement in the uptake of biomolecules and outer membrane stability
    • DOI 10.1016/S0378-1097(99)00293-1, PII S0378109799002931
    • Lazzaroni, J.C., Germon, P., Ray, M.C., and Vianney, A. (1999) The ToI proteins of Escherichia coli and their involvement in the uptake of biomolecules and outer membrane stability. FEMS Microbiol Lett 177: 191-197. (Pubitemid 29352212)
    • (1999) FEMS Microbiology Letters , vol.177 , Issue.2 , pp. 191-197
    • Lazzaroni, J.C.1    Germon, P.2    Ray, M.-C.3    Vianney, A.4
  • 49
    • 0036589166 scopus 로고    scopus 로고
    • The ToI proteins of Escherichia coli and their involvement in the translocation of group A colicins
    • Lazzaroni, J.C., Dubuisson, J.F., and Vianney, A. (2002) The ToI proteins of Escherichia coli and their involvement in the translocation of group A colicins. Biochimie 84: 391-397.
    • (2002) Biochimie , vol.84 , pp. 391-397
    • Lazzaroni, J.C.1    Dubuisson, J.F.2    Vianney, A.3
  • 50
    • 0034695404 scopus 로고    scopus 로고
    • Unfolding pathway of the colicin E1 channel protein on a membrane surface
    • DOI 10.1006/jmbi.1999.3396
    • Lindeberg, M., Zakharov, S.D., and Cramer, W.A. (2000) Unfolding pathway of the colicin E1 channel protein on a membrane surface. J Mol Biol 295: 679-692. (Pubitemid 30695101)
    • (2000) Journal of Molecular Biology , vol.295 , Issue.3 , pp. 679-692
    • Lindeberg, M.1    Zakharov, S.D.2    Cramer, W.A.3
  • 51
    • 0033888533 scopus 로고    scopus 로고
    • Mutations in each of the toi genes of Pseudomonas putida reveal that they are critical for maintenance of outer membrane stability
    • Llamas, M.A., Ramos, J.L., and Rodriguez-Herva, J.J. (2000) Mutations in each of the toi genes of Pseudomonas putida reveal that they are critical for maintenance of outer membrane stability. J Bacteriol 182: 4764-4772.
    • (2000) J Bacteriol , vol.182 , pp. 4764-4772
    • Llamas, M.A.1    Ramos, J.L.2    Rodriguez-Herva, J.J.3
  • 53
    • 0017096081 scopus 로고
    • Enterobacterial common antigen
    • Makela, P.H., and Mayer, H. (1976) Enterobacterial common antigen. Bacteriol Rev 40: 591-632.
    • (1976) Bacteriol Rev , vol.40 , pp. 591-632
    • Makela, P.H.1    Mayer, H.2
  • 54
    • 0018400818 scopus 로고
    • Chemistry and biology of the enterobacterial common antigen (ECA)
    • Mayer, H., and Schmidt, G. (1979) Chemistry and biology of the enterobacterial common antigen (ECA). Curr Top Microbiol Immunol 85: 99-153.
    • (1979) Curr Top Microbiol Immunol , vol.85 , pp. 99-153
    • Mayer, H.1    Schmidt, G.2
  • 55
    • 0023432172 scopus 로고
    • Role of micF in the tolC-mediated regulation of OmpF, a major outer membrane protein of Escherichia coli K-12
    • Misra, R., and Reeves, P.R. (1987) Role of micF in the tolC-mediated regulation of OmpF, a major outer membrane protein of Escherichia coli K-12. J Bacteriol 169: 4722-4730.
    • (1987) J Bacteriol , vol.169 , pp. 4722-4730
    • Misra, R.1    Reeves, P.R.2
  • 56
    • 0020267591 scopus 로고
    • The BtuB Col plasmids and homology between the colicins they encode
    • Mock, M., and Pugsley, A.P. (1982) The BtuB group col plasmids and homology between the colicins they encode. J Bacteriol 150: 1069-1076. (Pubitemid 12010874)
    • (1982) Journal of Bacteriology , vol.150 , Issue.3 , pp. 1069-1076
    • Mock, M.1    Pugsley, A.P.2
  • 57
    • 0014137931 scopus 로고
    • Genetics and physiology of colicin-tolerant mutants of Escherichia coll
    • Nagel de Zwaig, R., and Luria, S.E. (1967) Genetics and physiology of colicin-tolerant mutants of Escherichia coll. J Bacteriol 94: 1112-1123.
    • (1967) J Bacteriol , vol.94 , pp. 1112-1123
    • De Nagel Zwaig, R.1    Luria, S.E.2
  • 58
    • 47149096184 scopus 로고    scopus 로고
    • A genome-wide approach to identify the genes involved in biofilm formation in E. coli
    • Niba, ET., Naka, Y., Nagase, M., Mori, H., and Kitakawa, M. (2007) A genome-wide approach to identify the genes involved in biofilm formation in E. coli. DNA Res 14: 237-246.
    • (2007) DNA Res , vol.14 , pp. 237-246
    • Niba, E.T.1    Naka, Y.2    Nagase, M.3    Mori, H.4    Kitakawa, M.5
  • 60
    • 0026056527 scopus 로고
    • Effect of rfaH(sfrB) and temperature on expression of rfa genes of Escherichia coli K-12
    • Pradel, E., and Schnaitman, C.A. (1991) Effect of rfaH(sfrB) and temperature on expression of rfa genes of Escherichia coli K-12. J Bacteriol 173: 6428-6431.
    • (1991) J Bacteriol , vol.173 , pp. 6428-6431
    • Pradel, E.1    Schnaitman, C.A.2
  • 62
    • 0034751710 scopus 로고    scopus 로고
    • Identification of the structural gene for the TDP-Fuc4NAc: Lipid II Fuc4NAc transferase involved in synthesis of enterobacterial common antigen in Escherichia coli K-12
    • DOI 10.1128/JB.183.22.6509-6516.2001
    • Rahman, A., Barr, K., and Rick, P.D. (2001) Identification of the structural gene for the TDP-Fuc4NAc: lipid Il Fuc4NAc transferase involved in synthesis of enterobacterial common antigen in Escherichia coll K-12. J Bacteriol 183: 6509-6516. (Pubitemid 33026739)
    • (2001) Journal of Bacteriology , vol.183 , Issue.22 , pp. 6509-6516
    • Rahman, A.1    Barr, K.2    Rick, P.D.3
  • 63
    • 28244439062 scopus 로고    scopus 로고
    • Truncation of the lipopolysaccharide outer core affects susceptibility to antimicrobial peptides and virulence of Actinobacillus pleuropneumoniae serotype 1
    • DOI 10.1074/jbc.M502852200
    • Ramjeet, M., Deslandes, V., St Michael, F., Cox, A.D., Kobisch, M., Gottschalk, M., and Jacques, M. (2005) Truncation of the lipopolysaccharide outer core affects susceptibility to antimicrobial peptides and virulence of Actinobacillus pleuropneumoniae serotype 1. J Biol Chem 280: 39104-39114. (Pubitemid 41713861)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39104-39114
    • Ramjeet, M.1    Deslandes, V.2    St Michael, F.3    Cox, A.D.4    Kobisch, M.5    Gottschalk, M.6    Jacques, M.7
  • 64
    • 51649113460 scopus 로고    scopus 로고
    • Mutation in the LPS outer core biosynthesis gene, galU, affects LPS interaction with the RTX toxins Apxl and Apxll and cytolytic activity of Actinobacillus pleuropneumoniae serotype 1
    • Ramjeet, M., Cox, A.D., Hancock, M.A., Mourez, M., Labrie, J., Gottschalk, M., and Jacques, M. (2008) Mutation in the LPS outer core biosynthesis gene, galU, affects LPS interaction with the RTX toxins Apxl and Apxll and cytolytic activity of Actinobacillus pleuropneumoniae serotype 1. Mol Microbiol 70: 221-235.
    • (2008) Mol Microbiol , vol.70 , pp. 221-235
    • Ramjeet, M.1    Cox, A.D.2    Hancock, M.A.3    Mourez, M.4    Labrie, J.5    Gottschalk, M.6    Jacques, M.7
  • 65
    • 0033966170 scopus 로고    scopus 로고
    • Identification by genetic suppression of Escherichia coli TolB residues important for TolB-Pal interaction
    • DOI 10.1128/JB.182.3.821-824.2000
    • Ray, M.C., Germon, P., Vianney, A., Portalier, R., and Lazzaroni, J.C. (2000) Identification by genetic suppression of Escherichia coli TolB residues important for TolB-Pal interaction. J Bacteriol 182: 821-824. (Pubitemid 30054017)
    • (2000) Journal of Bacteriology , vol.182 , Issue.3 , pp. 821-824
    • Ray, M.-C.1    Germon, P.2    Vianney, A.3    Portalier, R.4    Lazzaroni, J.C.5
  • 66
    • 0017650936 scopus 로고
    • Genetic locus (ompB) affecting a major outer membrane protein in Escherichia coli K 12
    • Sarma, V., and Reeves, P. (1977) Genetic locus (ompB) affecting a major outer-membrane protein in Escherichia coll K-12. J Bacteriol 132: 23-27. (Pubitemid 8194514)
    • (1977) Journal of Bacteriology , vol.132 , Issue.1 , pp. 23-27
    • Sarma, V.1    Reeves, P.2
  • 67
    • 0027202811 scopus 로고
    • Genetics of lipopolysaccharide biosynthesis in enteric bacteria
    • Schnaitman, C.A., and Klena, J.D. (1993) Genetics of lipopolysaccharide biosynthesis in enteric bacteria. Microbiol Rev 57: 655-682. (Pubitemid 23262513)
    • (1993) Microbiological Reviews , vol.57 , Issue.3 , pp. 655-682
    • Schnaitman, C.A.1    Klena, J.D.2
  • 68
    • 33846220225 scopus 로고    scopus 로고
    • Minimum length requirement of the flexible N-terminal translocation subdomain of colicin E3
    • DOI 10.1128/JB.01344-06
    • Sharma, O., and Cramer, W.A. (2007) Minimum length requirement of the flexible N-terminal translocation subdomain of colicin E3. J Bacteriol 189: 363-368. (Pubitemid 46106368)
    • (2007) Journal of Bacteriology , vol.189 , Issue.2 , pp. 363-368
    • Sharma, O.1    Cramer, W.A.2
  • 69
    • 34548179597 scopus 로고    scopus 로고
    • Structure of the complex of the colicin E2 R-domain and its BtuB receptor: The outer membrane colicin translocon
    • DOI 10.1074/jbc.M703004200
    • Sharma, O., Yamashita, E., Zhalnina, M.V., Zakharov, S.D., Datsenko, K.A., Wanner, B.L., and Cramer, W.A. (2007) Structure of the complex of the colicin E2 R-domain and its BtuB receptor: the outer membrane colicin translocon. J Biol Chem 282: 23163-23170. (Pubitemid 47311941)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.32 , pp. 23163-23170
    • Sharma, O.1    Yamashita, E.2    Zhalnina, M.V.3    Zakharov, S.D.4    Datsenko, K.A.5    Wanner, B.L.6    Cramer, W.A.7
  • 70
    • 21644453615 scopus 로고    scopus 로고
    • Identification of an essential cleavage site in ColE7 required for import and killing of cells
    • DOI 10.1074/jbc.M501216200
    • Shi, Z., Chak, K.F., and Yuan, H.S. (2005) Identification of an essential cleavage site in ColE7 required for import and killing of cells. J Biol Chem 280: 24663-24668. (Pubitemid 40934555)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24663-24668
    • Shi, Z.1    Chak, K.-F.2    Yuan, H.S.3
  • 71
    • 0023612042 scopus 로고
    • Bacteriophage K20 requires both the OmpF porin and lipopolysaccharide for receptor function
    • Silverman, J.A., and Benson, S.A. (1987) Bacteriophage K20 requires both the OmpF porin and lipopolysaccharide for receptor function. J Bacteriol 169: 4830-4833.
    • (1987) J Bacteriol , vol.169 , pp. 4830-4833
    • Silverman, J.A.1    Benson, S.A.2
  • 72
    • 26444481955 scopus 로고    scopus 로고
    • Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: A system-level analysis
    • Skerker, J.M., Prasol, M.S., Perchuk, B.S., Biondi, E.G., and Laub, MT. (2005) Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis. PLoS Biol 3: e334.
    • (2005) PLoS Biol , vol.3
    • Skerker, J.M.1    Prasol, M.S.2    Perchuk, B.S.3    Biondi, E.G.4    Laub, M.T.5
  • 73
    • 0023225017 scopus 로고
    • Nucleotide sequence of a gene cluster involved in entry of e colicins and singlestranded DNA of infecting filamentous bacteriophages into Escherichia coll
    • Sun, T.P., and Webster, R.E. (1987) Nucleotide sequence of a gene cluster involved in entry of E colicins and singlestranded DNA of infecting filamentous bacteriophages into Escherichia coll. J Bacteriol 169: 2667-2674.
    • (1987) J Bacteriol , vol.169 , pp. 2667-2674
    • Sun, T.P.1    Webster, R.E.2
  • 74
    • 0029888551 scopus 로고    scopus 로고
    • H-NS regulates OmpF expression through micF antisense RNA in Escherichia coli
    • Suzuki, T., Ueguchi, C., and Mizuno, T. (1996) H-NS regulates OmpF expression through micF antisense RNA in Escherichia coli. J Bacteriol 178: 3650-3653.
    • (1996) J Bacteriol , vol.178 , pp. 3650-3653
    • Suzuki, T.1    Ueguchi, C.2    Mizuno, T.3
  • 75
    • 0032553533 scopus 로고    scopus 로고
    • 12 receptor with high affinity for colicin E3
    • DOI 10.1074/jbc.273.47.31113
    • Taylor, R., Burgner, J.W., Clifton, J., and Cramer, W.A. (1998) Purification and characterization of monomeric Escherichia coli vitamin B12 receptor with high affinity for colicin E3. J Biol Chem 273: 31113-31118. (Pubitemid 28533121)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.47 , pp. 31113-31118
    • Taylor, R.1    Burgner, J.W.2    Clifton, J.3    Cramer, W.A.4
  • 76
    • 0021738087 scopus 로고
    • Gene encoding a hybrid OmpF - PhoE pore protein in the outer membrane of Escherichia coli K12
    • Tommassen, J., Pugsley, A.P., Korteland, J., Verbakel, J., and Lugtenberg, B. (1984) Gene encoding a hybrid OmpF - PhoE pore protein in the outer membrane of Escherichia coli K12. Mol Gen Genet 197: 503-508.
    • (1984) Mol Gen Genet , vol.197 , pp. 503-508
    • Tommassen, J.1    Pugsley, A.P.2    Korteland, J.3    Verbakel, J.4    Lugtenberg, B.5
  • 77
    • 0032702005 scopus 로고    scopus 로고
    • Identification of bacteriophage K20 binding regions of OmpF and lipopolysaccharide in Escherichia coli K-12
    • DOI 10.1016/S0378-1097(99)00519-4, PII S0378109799005194
    • Traurig, M., and Misra, R. (1999) Identification of bacteriophage K20 binding regions of OmpF and lipopolysaccharide in Escherichia coli K-12. FEMS Microbiol Lett 181: 101 108. (Pubitemid 29516608)
    • (1999) FEMS Microbiology Letters , vol.181 , Issue.1 , pp. 101-108
    • Traurig, M.1    Misra, R.2
  • 78
    • 0035903650 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protease Ompt from Escherichia coli suggests a novel catalytic site
    • DOI 10.1093/emboj/20.18.5033
    • Vandeputte-Rutten, L., Kramer, R.A., Kroon, J., Dekker, N., Egmond, M.R., and Gros, P. (2001) Crystal structure of the outer membrane protease OmpT from Escherichia coll suggests a novel catalytic site. EMBO J 20: 5033-5039. (Pubitemid 32910899)
    • (2001) EMBO Journal , vol.20 , Issue.18 , pp. 5033-5039
    • Vandeputte-Rutten, L.1    Kramer, R.A.2    Kroon, J.3    Dekker, N.4    Egmond, M.R.5    Gros, P.6
  • 79
    • 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., Lewin, T.M., Beyer, W.F., Jr, Lazzaroni, J.C., Portalier, R., and Webster, R.E. (1994) Membrane topology and mutational analysis of the ToIQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity. J Bacteriol 176: 822-829. (Pubitemid 24043972)
    • (1994) Journal of Bacteriology , vol.176 , Issue.3 , 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
  • 80
    • 8944230187 scopus 로고    scopus 로고
    • Characterization of the tol-pal region of Escherichia coli K-12: Translational control of tolR expression by tolQ and identification of a new open reading frame downstream of pal encoding a periplasmic protein
    • Vianney, A., Muller, M.M., Clavel, T., Lazzaroni, J.C., Portalier, R., and Webster, R.E. (1996) Characterization of the tol-pal region of Escherichia coll K-12: translational control of tolR expression by ToIQ and identification of a new open reading frame downstream of pal encoding a periplasmic protein. J Bacteriol 178: 4031-4038. (Pubitemid 26240881)
    • (1996) Journal of Bacteriology , vol.178 , Issue.14 , pp. 4031-4038
    • Vianney, A.1    Michelle, M.M.2    Clavel, T.3    Lazzaroni, J.C.4    Portalier, R.5    Webster, R.E.6
  • 81
    • 0027404233 scopus 로고
    • Involvement of lipopolysaccharide in the secretion of Escherichia coli α-haemolysin and Erwinia chrysanthemi proteases
    • DOI 10.1111/j.1365-2958.1993.tb01105.x
    • Wandersman, C., and Letoffe, S. (1993) Involvement of lipopolysaccharide in the secretion of Escherichia coll alpha-haemolysin and Erwinia chrysanthemi proteases. Mol Microbiol 7: 141-150. (Pubitemid 23011104)
    • (1993) Molecular Microbiology , vol.7 , Issue.1 , pp. 141-150
    • Wandersman, C.1    Letoffe, S.2
  • 82
    • 49149127813 scopus 로고    scopus 로고
    • Crystal structures of the OmpF porin: Function in a colicin translocon
    • Yamashita, E., Zhalnina, M.V., Zakharov, S.D., Sharma, O., and Cramer, W.A. (2008) Crystal structures of the OmpF porin: function in a colicin translocon. EMBO J 27: 2171-2180.
    • (2008) EMBO J , vol.27 , pp. 2171-2180
    • Yamashita, E.1    Zhalnina, M.V.2    Zakharov, S.D.3    Sharma, O.4    Cramer, W.A.5
  • 84
    • 33748667290 scopus 로고    scopus 로고
    • The colicin E3 outer membrane translocon: Immunity protein release allows interaction of the cytotoxic domain with OmpF porin
    • DOI 10.1021/bi060694+
    • Zakharov, S.D., Zhalnina, M.V., Sharma, O., and Cramer, W.A. (2006) The colicin E3 outer membrane translocon: immunity protein release allows interaction of the cytotoxic domain with OmpF porin. Biochemistry 45: 10199-10207. (Pubitemid 44384795)
    • (2006) Biochemistry , vol.45 , Issue.34 , pp. 10199-10207
    • Zakharov, S.D.1    Zhalnina, M.V.2    Sharma, O.3    Cramer, W.A.4
  • 85
    • 0036589208 scopus 로고    scopus 로고
    • Importation of nuclease colicins into E. coli cells: Endoproteolytic cleavage and its prevention by the immunity protein
    • de Zamaroczy, M., and Buckingham, R.H. (2002) Importation of nuclease colicins into E. coli cells: endoproteolytic cleavage and its prevention by the immunity protein. Biochimie 84: 423-432.
    • (2002) Biochimie , vol.84 , pp. 423-432
    • De Zamaroczy, M.1    Buckingham, R.H.2
  • 86
    • 0034881923 scopus 로고    scopus 로고
    • Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase LepB
    • DOI 10.1016/S1097-2765(01)00276-3
    • de Zamaroczy, M., Mora, L., Lecuyer, A., Geli, V., and Buckingham, R.H. (2001) Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase LepB. Mol Cell 8: 159-168. (Pubitemid 32772914)
    • (2001) Molecular Cell , vol.8 , Issue.1 , pp. 159-168
    • De, Z.M.1    Mora, L.2    Lecuyer, A.3    Geli, V.4    Buckingham, R.H.5


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