메뉴 건너뛰기




Volumn 352, Issue 3, 2005, Pages 534-550

Site-directed mutagenesis of the greasy slide aromatic residues within the LamB (Maltoporin) channel of Escherichia coli: Effect on ion and maltopentaose transport

Author keywords

Greasy slide; LamB; Lipid bilayer; Maltooligosaccharide binding; Maltoporin

Indexed keywords

CARBOHYDRATE; OLIGOSACCHARIDE;

EID: 24044481300     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.07.025     Document Type: Article
Times cited : (18)

References (44)
  • 1
    • 0019395615 scopus 로고
    • Ultrastructure, chemistry, and function of the bacterial wall
    • T.J. Beveridge Ultrastructure, chemistry, and function of the bacterial wall Int. Rev. Cytol. 72 1981 229 317
    • (1981) Int. Rev. Cytol. , vol.72 , pp. 229-317
    • Beveridge, T.J.1
  • 2
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • H. Nikaido, and M. Vaara Molecular basis of bacterial outer membrane permeability Microbiol. Rev. 49 1985 1 32
    • (1985) Microbiol. Rev. , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 3
    • 33645607378 scopus 로고
    • Uptake of solutes through bacterial outer membranes
    • J.-M. Ghuysen R. Hakenbeck Elsevier Amsterdam
    • R. Benz Uptake of solutes through bacterial outer membranes J.-M. Ghuysen R. Hakenbeck New Comprehensive Biochemistry vol. 27 1994 Elsevier Amsterdam 397
    • (1994) New Comprehensive Biochemistry , vol.27 , pp. 397
    • Benz, R.1
  • 4
    • 0023054675 scopus 로고
    • Role of lysines in ion selectivity of bacterial outer membrane porins
    • R.E. Hancock, A. Schmidt, K. Bauer, and R. Benz Role of lysines in ion selectivity of bacterial outer membrane porins Biochim. Biophys. Acta 860 1986 263 267
    • (1986) Biochim. Biophys. Acta , vol.860 , pp. 263-267
    • Hancock, R.E.1    Schmidt, A.2    Bauer, K.3    Benz, R.4
  • 5
    • 0023783439 scopus 로고
    • Permeation of hydrophilic molecules through the outer membrane of Gram-negative bacteria. Review on bacterial porins
    • R. Benz, and K. Bauer Permeation of hydrophilic molecules through the outer membrane of Gram-negative bacteria. Review on bacterial porins Eur. J. Biochem. 176 1988 1 19
    • (1988) Eur. J. Biochem. , vol.176 , pp. 1-19
    • Benz, R.1    Bauer, K.2
  • 6
    • 84956827668 scopus 로고    scopus 로고
    • Reconstitution of general diffusion pores from bacterial outer membranes
    • R. Benz Wiley-VCH Weinheim
    • C. Danelon, and M. Winterhalter Reconstitution of general diffusion pores from bacterial outer membranes R. Benz Bacterial and Eukaryotic Porins 2004 Wiley-VCH Weinheim 99 117
    • (2004) Bacterial and Eukaryotic Porins , pp. 99-117
    • Danelon, C.1    Winterhalter, M.2
  • 7
    • 0017127269 scopus 로고
    • Maltose transport in Escherichia coli K12. a comparison of transport kinetics in wild-type and lambda-resistant mutants as measured by fluorescence quenching
    • S. Szmelcman, M. Schwartz, T.J. Silhavy, and W. Boos Maltose transport in Escherichia coli K12. A comparison of transport kinetics in wild-type and lambda-resistant mutants as measured by fluorescence quenching Eur. J. Biochem. 65 1976 13 19
    • (1976) Eur. J. Biochem. , vol.65 , pp. 13-19
    • Szmelcman, S.1    Schwartz, M.2    Silhavy, T.J.3    Boos, W.4
  • 8
    • 0018975651 scopus 로고
    • Outer membrane proteine of Escherichia coli K-12 is co-regulated with alkaline phosphatase
    • J. Tommassen, and B. Lugtenberg Outer membrane proteine of Escherichia coli K-12 is co-regulated with alkaline phosphatase J. Bacteriol. 143 1980 151 157
    • (1980) J. Bacteriol. , vol.143 , pp. 151-157
    • Tommassen, J.1    Lugtenberg, B.2
  • 9
    • 0019779495 scopus 로고
    • Aminoglycoside uptake and mode of action - With special reference to streptomycin and gentamicin. I. Antagonists and mutants
    • R.E. Hancock Aminoglycoside uptake and mode of action - with special reference to streptomycin and gentamicin. I. Antagonists and mutants J. Antimicrob. Chemother. 8 1981 249 276
    • (1981) J. Antimicrob. Chemother. , vol.8 , pp. 249-276
    • Hancock, R.E.1
  • 10
    • 0021998366 scopus 로고
    • Maltose-binding protein does not modulate the activity of maltoporin as a general porin in Escherichia coli
    • J.M. Brass, K. Bauer, U. Ehmann, and W. Boos Maltose-binding protein does not modulate the activity of maltoporin as a general porin in Escherichia coli J. Bacteriol. 161 1985 720 726
    • (1985) J. Bacteriol. , vol.161 , pp. 720-726
    • Brass, J.M.1    Bauer, K.2    Ehmann, U.3    Boos, W.4
  • 11
    • 0018966820 scopus 로고
    • Lambda receptor in the outer membrane of Escherichia coli as a binding protein for maltodextrins and starch poly-saccharides
    • T. Ferenci, M. Schwentorat, S. Ullrich, and J. Vilmart Lambda receptor in the outer membrane of Escherichia coli as a binding protein for maltodextrins and starch poly-saccharides J. Bacteriol. 142 1980 521 526
    • (1980) J. Bacteriol. , vol.142 , pp. 521-526
    • Ferenci, T.1    Schwentorat, M.2    Ullrich, S.3    Vilmart, J.4
  • 12
    • 0022515322 scopus 로고
    • Pore formation by LamB of Escherichia coli in lipid bilayer membranes
    • R. Benz, A. Schmid, T. Nakae, and G.H. Vos-Scheperkeuter Pore formation by LamB of Escherichia coli in lipid bilayer membranes J. Bacteriol. 165 1986 978 986
    • (1986) J. Bacteriol. , vol.165 , pp. 978-986
    • Benz, R.1    Schmid, A.2    Nakae, T.3    Vos-Scheperkeuter, G.H.4
  • 13
    • 0023852792 scopus 로고
    • Pore-forming activity of the Tsx protein from the outer membrane of Escherichia coli. Demonstration of a nucleoside-specific binding site
    • C. Maier, E. Bremer, A. Schmid, and R. Benz Pore-forming activity of the Tsx protein from the outer membrane of Escherichia coli. Demonstration of a nucleoside-specific binding site J. Biol. Chem. 263 1988 2493 2499
    • (1988) J. Biol. Chem. , vol.263 , pp. 2493-2499
    • Maier, C.1    Bremer, E.2    Schmid, A.3    Benz, R.4
  • 14
    • 0023127660 scopus 로고
    • Mechanism of ion transport through the anion-selective channel of the Pseudomonas aeruginosa outer membrane
    • R. Benz, and R.E.W. Hancock Mechanism of ion transport through the anion-selective channel of the Pseudomonas aeruginosa outer membrane J. Gen. Physiol. 89 1987 275 295
    • (1987) J. Gen. Physiol. , vol.89 , pp. 275-295
    • Benz, R.1    Hancock, R.E.W.2
  • 16
    • 0023754638 scopus 로고
    • Plasmid-mediated sucrose metabolism in Escherichia coli K12: Mapping of the scr genes of pUR400
    • K. Schmid, R. Ebner, J. Altenbuchner, R. Schmitt, and J.W. Lengeler Plasmid-mediated sucrose metabolism in Escherichia coli K12: mapping of the scr genes of pUR400 Mol. Microbiol. 2 1988 1 8
    • (1988) Mol. Microbiol. , vol.2 , pp. 1-8
    • Schmid, K.1    Ebner, R.2    Altenbuchner, J.3    Schmitt, R.4    Lengeler, J.W.5
  • 17
    • 0020317258 scopus 로고
    • Plasmid-mediated uptake and metabolism of sucrose by Escherichia coli K-12
    • K. Schmid, M. Schupfner, and R. Schmitt Plasmid-mediated uptake and metabolism of sucrose by Escherichia coli K-12 J. Bacteriol. 151 1982 68 76
    • (1982) J. Bacteriol. , vol.151 , pp. 68-76
    • Schmid, K.1    Schupfner, M.2    Schmitt, R.3
  • 18
    • 0032146885 scopus 로고    scopus 로고
    • Study of sugar binding to the sucrose specific ScrY-channel of enteric bacteria using current noise analysis
    • C. Andersen, R. Cseh, K. Schülein, and R. Benz Study of sugar binding to the sucrose specific ScrY-channel of enteric bacteria using current noise analysis J. Membr. Biol. 164 1998 263 274
    • (1998) J. Membr. Biol. , vol.164 , pp. 263-274
    • Andersen, C.1    Cseh, R.2    Schülein, K.3    Benz, R.4
  • 19
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
    • T. Schirmer, T.A. Keller, Y.F. Wang, and J.P. Rosenbusch Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution Science 267 1995 512 514
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbusch, J.P.4
  • 20
    • 0029644059 scopus 로고    scopus 로고
    • Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway
    • R. Dutzler, Y.F. Wang, P.J. Rizkallah, J.P. Rosenbusch, and T. Schirmer Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway Structure 4 1996 127 134
    • (1996) Structure , vol.4 , pp. 127-134
    • Dutzler, R.1    Wang, Y.F.2    Rizkallah, P.J.3    Rosenbusch, J.P.4    Schirmer, T.5
  • 21
    • 0030596521 scopus 로고    scopus 로고
    • Rate constants of sugar transport through two lamB mutants of Escherichia coli: Comparison to wild-type maltoporin and to LamB of Salmonella typhimurium
    • M. Jordy, C. Andersen, K. Schülein, T. Ferenci, and R. Benz Rate constants of sugar transport through two lamB mutants of Escherichia coli: comparison to wild-type maltoporin and to LamB of Salmonella typhimurium J. Mol. Biol. 259 1996 666 678
    • (1996) J. Mol. Biol. , vol.259 , pp. 666-678
    • Jordy, M.1    Andersen, C.2    Schülein, K.3    Ferenci, T.4    Benz, R.5
  • 22
    • 0036232212 scopus 로고    scopus 로고
    • Site-directed mutagenesis of tyrosine 118 within the central constriction site of the LamB (maltoporin) channel of Escherichia coli: I. Effect on ion transport
    • F. Orlik, C. Andersen, and R. Benz Site-directed mutagenesis of tyrosine 118 within the central constriction site of the LamB (maltoporin) channel of Escherichia coli: I. Effect on ion transport Biophys. J. 82 2002 2466 2475
    • (2002) Biophys. J. , vol.82 , pp. 2466-2475
    • Orlik, F.1    Andersen, C.2    Benz, R.3
  • 23
    • 0036280688 scopus 로고    scopus 로고
    • Site-directed mutagenesis of tyrosine 118 within the central constriction site of the LamB (maltoporin) channel of Escherichia coli: II. Effect on maltose and maltooligosaccharide binding kinetics
    • F. Orlik, C. Andersen, and R. Benz Site-directed mutagenesis of tyrosine 118 within the central constriction site of the LamB (maltoporin) channel of Escherichia coli: II. Effect on maltose and maltooligosaccharide binding kinetics Biophys J. 83 2002 309 321
    • (2002) Biophys J. , vol.83 , pp. 309-321
    • Orlik, F.1    Andersen, C.2    Benz, R.3
  • 25
    • 0023472905 scopus 로고
    • Mechanism of sugar transport through the sugar-specific LamB-channel of Escherichia coli outer membrane
    • R. Benz, A. Schmid, and G.H. Vos-Scheperkeuter Mechanism of sugar transport through the sugar-specific LamB-channel of Escherichia coli outer membrane J. Membr. Biol. 100 1987 12 29
    • (1987) J. Membr. Biol. , vol.100 , pp. 12-29
    • Benz, R.1    Schmid, A.2    Vos-Scheperkeuter, G.H.3
  • 26
    • 0028266944 scopus 로고
    • Noise analysis of ion current through the open and the sugar-induced closed state of the LamB-channel of Escherichia coli outer membrane: Evaluation of the sugar binding kinetics to the channel interior
    • S. Nekolla, C. Andersen, and R. Benz Noise analysis of ion current through the open and the sugar-induced closed state of the LamB-channel of Escherichia coli outer membrane: evaluation of the sugar binding kinetics to the channel interior Biophys. J. 66 1994 1388 1397
    • (1994) Biophys. J. , vol.66 , pp. 1388-1397
    • Nekolla, S.1    Andersen, C.2    Benz, R.3
  • 27
    • 0028926959 scopus 로고
    • Evaluation of the rate constants of sugar transport through maltoporin (LamB) of Escherichia coli from the sugar-induced current noise
    • C. Andersen, M. Jordy, and R. Benz Evaluation of the rate constants of sugar transport through maltoporin (LamB) of Escherichia coli from the sugar-induced current noise J. Gen. Physiol. 105 1995 385 401
    • (1995) J. Gen. Physiol. , vol.105 , pp. 385-401
    • Andersen, C.1    Jordy, M.2    Benz, R.3
  • 28
    • 0023986359 scopus 로고
    • Genetic analysis of sequences in maltoporin that contributes to binding domains and pore structure
    • H.G. Heine, G. Francis, K.S. Lee, and T. Ferenci Genetic analysis of sequences in maltoporin that contributes to binding domains and pore structure J. Bacteriol. 170 1988 1370 1378
    • (1988) J. Bacteriol. , vol.170 , pp. 1370-1378
    • Heine, H.G.1    Francis, G.2    Lee, K.S.3    Ferenci, T.4
  • 29
    • 0029087726 scopus 로고
    • The deletion of 70 N-terminal amino acids of the sugar-specific sucrose-porin ScrY causes its functional similarity to LamB in vivo and in vitro
    • K. Schülein, C. Andersen, and R. Benz The deletion of 70 N-terminal amino acids of the sugar-specific sucrose-porin ScrY causes its functional similarity to LamB in vivo and in vitro Mol. Microbiol. 17 1995 757 767
    • (1995) Mol. Microbiol. , vol.17 , pp. 757-767
    • Schülein, K.1    Andersen, C.2    Benz, R.3
  • 30
    • 0030878435 scopus 로고    scopus 로고
    • 1/f-Noise of open bacterial porin channels
    • F. Wohnsland, and R. Benz 1/f-Noise of open bacterial porin channels J. Membr. Biol. 158 1997 77 85
    • (1997) J. Membr. Biol. , vol.158 , pp. 77-85
    • Wohnsland, F.1    Benz, R.2
  • 31
    • 0034214825 scopus 로고    scopus 로고
    • Examining noise sources at the single-molecule level: 1/f noise of an open maltoporin channel
    • S.M. Bezrukov, and M. Winterhalter Examining noise sources at the single-molecule level: 1/f noise of an open maltoporin channel Phys. Rev. Letters 85 2000 202 205
    • (2000) Phys. Rev. Letters , vol.85 , pp. 202-205
    • Bezrukov, S.M.1    Winterhalter, M.2
  • 33
    • 0016683376 scopus 로고
    • Channel noise in membranes and lipid bilayers
    • F. Conti, and I. Wanke Channel noise in membranes and lipid bilayers Quart. Rev. Biophys. 8 1975 451 506
    • (1975) Quart. Rev. Biophys. , vol.8 , pp. 451-506
    • Conti, F.1    Wanke, I.2
  • 35
    • 0025869336 scopus 로고
    • A sugar-specific porin, ScrY, is involved in sucrose uptake in enteric bacteria
    • K. Schmid, R. Ebner, K. Jahreis, J.W. Lengeler, and F. Titgemeyer A sugar-specific porin, ScrY, is involved in sucrose uptake in enteric bacteria Mol. Microbiol. 5 1991 941 950
    • (1991) Mol. Microbiol. , vol.5 , pp. 941-950
    • Schmid, K.1    Ebner, R.2    Jahreis, K.3    Lengeler, J.W.4    Titgemeyer, F.5
  • 36
    • 0025893079 scopus 로고
    • The sugar specific outer membrane channel ScrY contains functional characteristics of general diffusion pores and substrate-specific porins
    • K. Schülein, K. Schmid, and R. Benz The sugar specific outer membrane channel ScrY contains functional characteristics of general diffusion pores and substrate-specific porins Mol. Microbiol. 5 1991 2233 2241
    • (1991) Mol. Microbiol. , vol.5 , pp. 2233-2241
    • Schülein, K.1    Schmid, K.2    Benz, R.3
  • 37
    • 0031557404 scopus 로고    scopus 로고
    • Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside
    • J.E.W. Meyer, M. Hofnung, and G.E. Schulz Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside J. Mol. Biol. 266 1997 761 775
    • (1997) J. Mol. Biol. , vol.266 , pp. 761-775
    • Meyer, J.E.W.1    Hofnung, M.2    Schulz, G.E.3
  • 38
    • 0038637764 scopus 로고    scopus 로고
    • On translocation through a membrane channel via an internal binding site: Kinetics and voltage dependence
    • G. Schwarz, C. Danelon, and M. Winterhalter On translocation through a membrane channel via an internal binding site: kinetics and voltage dependence Biophys. J. 84 2003 2990 2998
    • (2003) Biophys. J. , vol.84 , pp. 2990-2998
    • Schwarz, G.1    Danelon, C.2    Winterhalter, M.3
  • 39
    • 33645397302 scopus 로고
    • Rate constants of protolytic reactions in aqueous solutions
    • M. Eigen, W. Kruse, G. Maass, and L. De Maeyer Rate constants of protolytic reactions in aqueous solutions Prog. React. Kinet. 2 1964 287 318
    • (1964) Prog. React. Kinet. , vol.2 , pp. 287-318
    • Eigen, M.1    Kruse, W.2    Maass, G.3    De Maeyer, L.4
  • 40
    • 0032970556 scopus 로고    scopus 로고
    • In vivo and in vitro studies of major surface loop deletion mutants of the Escherichia coli K12 maltoporin: Contribution to maltose and maltooligosaccharide transport and binding
    • C. Andersen, C. Bachmeyer, H. Täuber, R. Benz, J. Wang, and V. Michel In vivo and in vitro studies of major surface loop deletion mutants of the Escherichia coli K12 maltoporin: contribution to maltose and maltooligosaccharide transport and binding Mol. Microbiol. 32 1999 851 867
    • (1999) Mol. Microbiol. , vol.32 , pp. 851-867
    • Andersen, C.1    Bachmeyer, C.2    Täuber, H.3    Benz, R.4    Wang, J.5    Michel, V.6
  • 41
    • 0033985885 scopus 로고    scopus 로고
    • Oriented channels reveal asymmetric energy barriers for sugar translocation through maltoporin of Escherichia coli
    • P. Van Gelder, F. Dumas, J.P. Rosenbusch, and M. Winterhalter Oriented channels reveal asymmetric energy barriers for sugar translocation through maltoporin of Escherichia coli Eur. J. Biochem. 267 2000 79 84
    • (2000) Eur. J. Biochem. , vol.267 , pp. 79-84
    • Van Gelder, P.1    Dumas, F.2    Rosenbusch, J.P.3    Winterhalter, M.4
  • 42
    • 0021998366 scopus 로고
    • Maltose-binding protein does not modulate the activity of maltoporin as a general porin in Escherichia coli
    • J.M. Brass, K. Bauer, U. Ehmann, and W. Boos Maltose-binding protein does not modulate the activity of maltoporin as a general porin in Escherichia coli J. Bacteriol. 161 1985 720 726
    • (1985) J. Bacteriol. , vol.161 , pp. 720-726
    • Brass, J.M.1    Bauer, K.2    Ehmann, U.3    Boos, W.4
  • 43
    • 0023906938 scopus 로고
    • Facilitated diffusion of p-nitrophenyl-alpha-d-maltohexaoside through the outer membrane of Escherichia coli. Characterization of LamB as a specific and saturable channel for maltooligosaccharides
    • S. Freundlieb, U. Ehmann, and W. Boos Facilitated diffusion of p-nitrophenyl-alpha-d-maltohexaoside through the outer membrane of Escherichia coli. Characterization of LamB as a specific and saturable channel for maltooligosaccharides J. Biol. Chem. 263 1988 314 320
    • (1988) J. Biol. Chem. , vol.263 , pp. 314-320
    • Freundlieb, S.1    Ehmann, U.2    Boos, W.3
  • 44
    • 0018139740 scopus 로고
    • Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli
    • R. Benz, K. Janko, W. Boos, and P. Läuger Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli Biochim. Biophys. Acta 511 1978 305 319
    • (1978) Biochim. Biophys. Acta , vol.511 , pp. 305-319
    • Benz, R.1    Janko, K.2    Boos, W.3    Läuger, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.