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Volumn 42, Issue 5, 2013, Pages 363-369

Peptide translocation through the mesoscopic channel: Binding kinetics at the single molecule level

Author keywords

Mesoscopic channel; Nanopore; Peptide translocation; Planar lipid bilayer; Porin

Indexed keywords

ESCHERICHIA COLI;

EID: 84877800252     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-012-0885-6     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 0035844870 scopus 로고    scopus 로고
    • Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria
    • 11402060 10.1083/jcb.153.6.1151 1:CAS:528:DC%2BD3MXktlOmsLk%3D
    • Ahting U, Thieffry M, Engelhardt H, Hegerl R, Neupert W, Nussberger S (2001) Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria. J Cell Biol 153:1151-1160
    • (2001) J Cell Biol , vol.153 , pp. 1151-1160
    • Ahting, U.1    Thieffry, M.2    Engelhardt, H.3    Hegerl, R.4    Neupert, W.5    Nussberger, S.6
  • 3
    • 77954446192 scopus 로고    scopus 로고
    • Unimolecular study of the interaction between the outer membrane protein OmpF from E. coli and an analogue of the HP(2-20) antimicrobial peptide
    • 20180000 10.1007/s10863-010-9273-z 1:CAS:528:DC%2BC3cXksVaqsL4%3D
    • Apetrei A, Asandei A, Park Y, Hahm KS, Winterhalter M, Luchian T (2010) Unimolecular study of the interaction between the outer membrane protein OmpF from E. coli and an analogue of the HP(2-20) antimicrobial peptide. J Bioenerg Biomembr 42:173-180
    • (2010) J Bioenerg Biomembr , vol.42 , pp. 173-180
    • Apetrei, A.1    Asandei, A.2    Park, Y.3    Hahm, K.S.4    Winterhalter, M.5    Luchian, T.6
  • 4
    • 0023783439 scopus 로고    scopus 로고
    • Permeation of hydrophilic molecules through the outer membrane of Gram-negative bacteria
    • 10.1111/j.1432-1033.1988.tb14245.x
    • Benz R, Bauer K (1998) Permeation of hydrophilic molecules through the outer membrane of Gram-negative bacteria. Eur J Biochem 176:1-19
    • (1998) Eur J Biochem , vol.176 , pp. 1-19
    • Benz, R.1    Bauer, K.2
  • 5
    • 78149459196 scopus 로고    scopus 로고
    • Facilitated translocation of polypeptides through a single nanopore
    • 10.1088/0953-8984/22/45/454117
    • Bikwemu R, Wolfe AJ, Xing X, Movileanu L (2010) Facilitated translocation of polypeptides through a single nanopore. J Phys: Condens Matter 22:454117
    • (2010) J Phys: Condens Matter , vol.22 , pp. 454117
    • Bikwemu, R.1    Wolfe, A.J.2    Xing, X.3    Movileanu, L.4
  • 6
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: Machineries and mechanisms
    • 10.1016/j.cell.2009.08.005
    • Chacinska A, Koehler CM, Milenkovic D, Lithgow T, Pfanner N (2009) Importing mitochondrial proteins: machineries and mechanisms. Cell 2009(138):628-644
    • (2009) Cell , vol.2009 , Issue.138 , pp. 628-644
    • Chacinska, A.1    Koehler, C.M.2    Milenkovic, D.3    Lithgow, T.4    Pfanner, N.5
  • 7
    • 55349144468 scopus 로고    scopus 로고
    • Transport at the nanoscale: Temperature dependence of ion conductance
    • 18726094 10.1007/s00249-008-0366-0 1:CAS:528:DC%2BD1cXhtlShurzL
    • Chimerel C, Movileanu L, Pezeshki S, Winterhalter M, Kleinekathöfer U (2008) Transport at the nanoscale: temperature dependence of ion conductance. Eur Biophys J 38:121-125
    • (2008) Eur Biophys J , vol.38 , pp. 121-125
    • Chimerel, C.1    Movileanu, L.2    Pezeshki, S.3    Winterhalter, M.4    Kleinekathöfer, U.5
  • 10
    • 0041816074 scopus 로고    scopus 로고
    • Probing the orientation of reconstituted maltoporin channels at the single-protein level
    • 12835320 10.1074/jbc.M305434200 1:CAS:528:DC%2BD3sXntVajs70%3D
    • Danelon C, Brando T, Winterhalter M (2003) Probing the orientation of reconstituted maltoporin channels at the single-protein level. J Biol Chem 278:35542-35551
    • (2003) J Biol Chem , vol.278 , pp. 35542-35551
    • Danelon, C.1    Brando, T.2    Winterhalter, M.3
  • 11
    • 0022558545 scopus 로고
    • Isolation and crystallization of bacterial porin
    • 2423843 10.1016/S0076-6879(86)25027-2 1:CAS:528:DyaL28XkslGhsLY%3D
    • Garavito RM, Rosenbusch JP (1986) Isolation and crystallization of bacterial porin. Meth Enzymol 125:309-328
    • (1986) Meth Enzymol , vol.125 , pp. 309-328
    • Garavito, R.M.1    Rosenbusch, J.P.2
  • 12
    • 0036403720 scopus 로고    scopus 로고
    • Function of Pseudomonas porins in uptake and efflux
    • 12142471 10.1146/annurev.micro.56.012302.160310 1:CAS:528: DC%2BD38Xos1Gisrk%3D
    • Hancock REW, Brinkman FSL (2002) Function of Pseudomonas porins in uptake and efflux. Annu Rev Microbiol 56:17-38
    • (2002) Annu Rev Microbiol , vol.56 , pp. 17-38
    • Hancock, R.E.W.1    Brinkman, F.S.L.2
  • 14
    • 79960556321 scopus 로고    scopus 로고
    • Exploring protein import pores of cellular organelles at the single molecule level using the planar lipid bilayer technique
    • 21684628 10.1016/j.ejcb.2011.04.012 1:CAS:528:DC%2BC3MXpt1yitb4%3D
    • Harsman A, Bartsch P, Hemmis B, Krüger V, Wagner R (2011) Exploring protein import pores of cellular organelles at the single molecule level using the planar lipid bilayer technique. Eur J Cell Biol 90:721-730
    • (2011) Eur J Cell Biol , vol.90 , pp. 721-730
    • Harsman, A.1    Bartsch, P.2    Hemmis, B.3    Krüger, V.4    Wagner, R.5
  • 15
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • 9774109 10.1038/26780 1:CAS:528:DyaK1cXms1aks78%3D
    • Hill K, Model K, Ryan MT, Dietmeier K, Martin F, Wagner R, Pfanner N (1998) Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature 395:516-521
    • (1998) Nature , vol.395 , pp. 516-521
    • Hill, K.1    Model, K.2    Ryan, M.T.3    Dietmeier, K.4    Martin, F.5    Wagner, R.6    Pfanner, N.7
  • 16
    • 0034734011 scopus 로고    scopus 로고
    • Targeting of proteins to mitochondria
    • 10878243 10.1016/S0014-5793(00)01663-X 1:CAS:528:DC%2BD3cXktlKqsLY%3D
    • Lithgow T (2000) Targeting of proteins to mitochondria. FEBS Lett 476:22-26
    • (2000) FEBS Lett , vol.476 , pp. 22-26
    • Lithgow, T.1
  • 17
    • 0020636951 scopus 로고
    • Molecular architecture and functioning of the outer membrane of Escherichia coli and other gram-negative bacteria
    • 6337630 10.1016/0304-4157(83)90014-X 1:CAS:528:DyaL3sXhsVSitLw%3D
    • Lugtenberg B, Van Alphen L (1983) Molecular architecture and functioning of the outer membrane of Escherichia coli and other gram-negative bacteria. Biochim Biophys Acta 737:51-115
    • (1983) Biochim Biophys Acta , vol.737 , pp. 51-115
    • Lugtenberg, B.1    Van Alphen, L.2
  • 18
    • 70349669315 scopus 로고    scopus 로고
    • Antibiotic translocation through membrane channels: Temperature-dependent ion current fluctuation for catching the fast events
    • 19506850 10.1007/s00249-009-0495-0 1:CAS:528:DC%2BD1MXht1SqtL%2FJ
    • Mahendran KR, Chimerel C, Mach T, Winterhalter M (2009) Antibiotic translocation through membrane channels: temperature-dependent ion current fluctuation for catching the fast events. Eur Biophys J 38:1141-1145
    • (2009) Eur Biophys J , vol.38 , pp. 1141-1145
    • Mahendran, K.R.1    Chimerel, C.2    MacH, T.3    Winterhalter, M.4
  • 19
    • 77951100110 scopus 로고    scopus 로고
    • Molecular basis of enrofloxacin translocation through OmpF, an outer membrane channel of Escherichia coli - When binding does not imply translocation
    • 20349984 10.1021/jp911485k 1:CAS:528:DC%2BC3cXjvFeqtr0%3D
    • Mahendran KR, Hajjar E, Mach T, Lovelle M, Kumar A, Sousa I, Spiga E, Weingart H, Gameiro P, Winterhalter M, Ceccarelli M (2010) Molecular basis of enrofloxacin translocation through OmpF, an outer membrane channel of Escherichia coli - when binding does not imply translocation. J Phys Chem B 114:5170-5179
    • (2010) J Phys Chem B , vol.114 , pp. 5170-5179
    • Mahendran, K.R.1    Hajjar, E.2    MacH, T.3    Lovelle, M.4    Kumar, A.5    Sousa, I.6    Spiga, E.7    Weingart, H.8    Gameiro, P.9    Winterhalter, M.10    Ceccarelli, M.11
  • 20
    • 84855426497 scopus 로고    scopus 로고
    • Protein translocation through Tom40: Kinetics of peptide release
    • 22225796 10.1016/j.bpj.2011.11.4003 1:CAS:528:DC%2BC38XkvF2qug%3D%3D
    • Mahendran KR, Romero-Ruiz M, Schlösinger A, Winterhalter M, Nussberger S (2012) Protein translocation through Tom40: kinetics of peptide release. Biophys J 102:39-47
    • (2012) Biophys J , vol.102 , pp. 39-47
    • Mahendran, K.R.1    Romero-Ruiz, M.2    Schlösinger, A.3    Winterhalter, M.4    Nussberger, S.5
  • 22
    • 45849114386 scopus 로고    scopus 로고
    • Excursion of a single polypeptide into a protein pore: Simple physics, but complicated biology
    • 18368402 10.1007/s00249-008-0309-9 1:CAS:528:DC%2BD1cXnt1akur0%3D
    • Mohammad MM, Movileanu L (2008) Excursion of a single polypeptide into a protein pore: simple physics, but complicated biology. Eur Biophys J 37:913-925
    • (2008) Eur Biophys J , vol.37 , pp. 913-925
    • Mohammad, M.M.1    Movileanu, L.2
  • 23
    • 0035964257 scopus 로고    scopus 로고
    • Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law
    • 11504913 10.1073/pnas.181089798 1:CAS:528:DC%2BD3MXmvFWit7k%3D
    • Movileanu L, Bayley H (2001) Partitioning of a polymer into a nanoscopic protein pore obeys a simple scaling law. Proc Natl Acad Sci USA 98:10137-10141
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10137-10141
    • Movileanu, L.1    Bayley, H.2
  • 24
    • 23244467934 scopus 로고    scopus 로고
    • Interactions of peptides with a protein pore
    • 15923222 10.1529/biophysj.104.057406 1:CAS:528:DC%2BD2MXnvVSkur4%3D
    • Movileanu L, Schmittschmitt JP, Scholtz JM, Bayley H (2005) Interactions of peptides with a protein pore. Biophys J 89:1030-1045
    • (2005) Biophys J , vol.89 , pp. 1030-1045
    • Movileanu, L.1    Schmittschmitt, J.P.2    Scholtz, J.M.3    Bayley, H.4
  • 25
    • 0037162486 scopus 로고    scopus 로고
    • Designed to penetrate. Time resolved interaction of single antibiotic molecules with bacterial pores
    • 12119404 10.1073/pnas.152206799 1:CAS:528:DC%2BD38XlslKgs70%3D
    • Nestorovich EM, Danelon C, Winterhalter M, Bezrukov SM (2002) Designed to penetrate. Time resolved interaction of single antibiotic molecules with bacterial pores. Proc Natl Acad Sci USA 99:9789
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9789
    • Nestorovich, E.M.1    Danelon, C.2    Winterhalter, M.3    Bezrukov, S.M.4
  • 26
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • 17263664 10.1146/annurev.biochem.76.052705.163409 1:CAS:528: DC%2BD2sXhtVehtbzE
    • Neupert W, Herrmann JM (2007) Translocation of proteins into mitochondria. Annu Rev Biochem 76:723-749
    • (2007) Annu Rev Biochem , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 27
    • 0041843740 scopus 로고    scopus 로고
    • CymA of Klebsiella oxytoca outer membrane. Binding of cyclodextrins and study of the current noise of open channels
    • 12885635 10.1016/S0006-3495(03)74527-5 1:CAS:528:DC%2BD3sXmtVyksr8%3D
    • Orlik F, Andersen C, Danelon C, Winterhalter M, Pajatsch M, Böck A, Benz R (2003) CymA of Klebsiella oxytoca outer membrane. Binding of cyclodextrins and study of the current noise of open channels. Biophys J 85:876-885
    • (2003) Biophys J , vol.85 , pp. 876-885
    • Orlik, F.1    Andersen, C.2    Danelon, C.3    Winterhalter, M.4    Pajatsch, M.5    Böck, A.6    Benz, R.7
  • 28
    • 34147108667 scopus 로고    scopus 로고
    • Unfolding of proteins and long transient conformations detected by single nanopore recording
    • 17501386 10.1103/PhysRevLett.98.158101 1:STN:280:DC%2BD2szjtVOrsQ%3D%3D
    • Oukhaled G, Mathé J, Biance AL, Bacari L, Betton JM, Lairez D, Pelta J, Auvray L (2007) Unfolding of proteins and long transient conformations detected by single nanopore recording. Phys Rev Lett 98:158101-158104
    • (2007) Phys Rev Lett , vol.98 , pp. 158101-158104
    • Oukhaled, G.1    Mathé, J.2    Biance, A.L.3    Bacari, L.4    Betton, J.M.5    Lairez, D.6    Pelta, J.7    Auvray, L.8
  • 30
    • 70350035648 scopus 로고    scopus 로고
    • Understanding ion conductance on a molecular level: An all-atom modeling of the bacterial porin OmpF
    • 19804720 10.1016/j.bpj.2009.07.018 1:CAS:528:DC%2BD1MXhsVCiu7bN
    • Pezeshki S, Chimerel C, Bessonov AN, Winterhalter M, Kleinekathöfer U (2009) Understanding ion conductance on a molecular level: an all-atom modeling of the bacterial porin OmpF. Biophys J 97:1898-1906
    • (2009) Biophys J , vol.97 , pp. 1898-1906
    • Pezeshki, S.1    Chimerel, C.2    Bessonov, A.N.3    Winterhalter, M.4    Kleinekathöfer, U.5
  • 31
    • 0032102987 scopus 로고    scopus 로고
    • Coupling site-directed mutagenesis with high-level expression: Large scale production of mutant porins from E. coli
    • 9631547 10.1111/j.1574-6968.1998.tb13027.x 1:CAS:528:DyaK1cXjsVegs78%3D
    • Prilipov A, Phale PS, Van Gelder P, Rosenbusch JP, Koebnik R (1998) Coupling site-directed mutagenesis with high-level expression: large scale production of mutant porins from E. coli. FEMS Microbiol Lett 163:65-72
    • (1998) FEMS Microbiol Lett , vol.163 , pp. 65-72
    • Prilipov, A.1    Phale, P.S.2    Van Gelder, P.3    Rosenbusch, J.P.4    Koebnik, R.5
  • 32
    • 77955704800 scopus 로고    scopus 로고
    • Interactions of mitochondrial presequence peptides with the mitochondrial outer membrane preprotein translocase TOM
    • 20682254 10.1016/j.bpj.2010.05.010 1:CAS:528:DC%2BC3cXpvFWnurw%3D
    • Romero-Ruiz M, Mahendran KR, Eckert R, Winterhalter M, Nussberger S (2010) Interactions of mitochondrial presequence peptides with the mitochondrial outer membrane preprotein translocase TOM. Biophys J 99:774-781
    • (2010) Biophys J , vol.99 , pp. 774-781
    • Romero-Ruiz, M.1    Mahendran, K.R.2    Eckert, R.3    Winterhalter, M.4    Nussberger, S.5
  • 33
    • 0016350456 scopus 로고
    • Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding
    • 4609976 1:CAS:528:DyaE2MXmvFCmtw%3D%3D
    • Rosenbusch JP (1974) Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding. J Biol Chem 249:8019-8029
    • (1974) J Biol Chem , vol.249 , pp. 8019-8029
    • Rosenbusch, J.P.1
  • 34
    • 0036216078 scopus 로고    scopus 로고
    • Partitioning of differently sized poly (ethylene glycol)s into OmpF porin
    • 11751305 10.1016/S0006-3495(02)75383-6 1:CAS:528:DC%2BD38XoslKlsA%3D%3D
    • Rostovtseva TK, Nestorovich EM, Bezrukov SM (2002) Partitioning of differently sized poly (ethylene glycol)s into OmpF porin. Biophys J 82:160-169
    • (2002) Biophys J , vol.82 , pp. 160-169
    • Rostovtseva, T.K.1    Nestorovich, E.M.2    Bezrukov, S.M.3
  • 35
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • 8599107 10.1126/science.271.5255.1519 1:CAS:528:DyaK28XhslSjsLo%3D
    • Schatz G, Dobberstein B (1996) Common principles of protein translocation across membranes. Science 271:1519-1526
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 36
    • 84859962388 scopus 로고    scopus 로고
    • Antibiotic permeation across the OmpF channel: Modulation of the affinity site in the presence of magnesium
    • 22369436 10.1021/jp2123136
    • Singh PR, Ceccarelli M, Lovelle M, Winterhalter M, Mahendran KR (2012) Antibiotic permeation across the OmpF channel: modulation of the affinity site in the presence of magnesium. J Phys Chem B 116:4433-4438
    • (2012) J Phys Chem B , vol.116 , pp. 4433-4438
    • Singh, P.R.1    Ceccarelli, M.2    Lovelle, M.3    Winterhalter, M.4    Mahendran, K.R.5
  • 37
    • 56349137240 scopus 로고    scopus 로고
    • Biogenesis of mitochondrial outer membrane proteins
    • 18501716 10.1016/j.bbamcr.2008.04.013 1:CAS:528:DC%2BD1cXhsVWrtL3E
    • Walther DM, Rapaport D (2009) Biogenesis of mitochondrial outer membrane proteins. Biochim Biophys Acta 1793:42-51
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 42-51
    • Walther, D.M.1    Rapaport, D.2
  • 38
    • 36148943499 scopus 로고    scopus 로고
    • Catalyzing the translocation of polypeptides through attractive interactions
    • 17949000 10.1021/ja0749340 1:CAS:528:DC%2BD2sXhtFyhu7zL
    • Wolfe AJ, Mohammad MM, Cheley S, Bayley H, Movileanu L (2007) Catalyzing the translocation of polypeptides through attractive interactions. J Am Chem Soc 129:14034-14041
    • (2007) J Am Chem Soc , vol.129 , pp. 14034-14041
    • Wolfe, A.J.1    Mohammad, M.M.2    Cheley, S.3    Bayley, H.4    Movileanu, L.5


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