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Volumn 32, Issue 4, 1999, Pages 851-867

In vivo and in vitro studies of major surface loop deletion mutants of the Escherichia coli K-12 maltoporin: Contribution to maltose and maltooligosaccharide transport and binding

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARBOHYDRATE BINDING PROTEIN; MALTOSE; OLIGOSACCHARIDE; PORIN; STARCH;

EID: 0032970556     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01406.x     Document Type: Article
Times cited : (25)

References (48)
  • 2
    • 0000458406 scopus 로고
    • Solute uptake through bacterial outer membranes
    • Hackenbeck, R., and Ghuysen, J.-M. (eds). Amsterdam: Elsevier
    • Benz, R. (1994) Solute uptake through bacterial outer membranes. In Bacterial Cell Wall. Hackenbeck, R., and Ghuysen, J.-M. (eds). Amsterdam: Elsevier, pp. 397-423.
    • (1994) Bacterial Cell Wall , pp. 397-423
    • Benz, R.1
  • 3
    • 0023127660 scopus 로고
    • Mechanism of ion transport through the anion-selective channel of Pseudomonas aeruginosa outer membrane
    • Benz, R., and Hancock, R.E.W. (1987) Mechanism of ion transport through the anion-selective channel of Pseudomonas aeruginosa outer membrane. J Gen Physiol 89: 275-295.
    • (1987) J Gen Physiol , vol.89 , pp. 275-295
    • Benz, R.1    Hancock, R.E.W.2
  • 4
    • 0018139740 scopus 로고
    • Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli
    • Benz, R., Janko, K., Boos, W., and Läuger, P. (1978) Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta 511: 305-319.
    • (1978) Biochim Biophys Acta , vol.511 , pp. 305-319
    • Benz, R.1    Janko, K.2    Boos, W.3    Läuger, P.4
  • 5
    • 0022515322 scopus 로고
    • Pore formation by LamB of Escherichia coli in lipid bilayer membranes
    • Benz, R., Schmid, A., Nakae, T., and Vos-Scheperkeuter, G.H. (1986) Pore formation by LamB of Escherichia coli in lipid bilayer membranes. J Bacteriol 165: 978-986.
    • (1986) J Bacteriol , vol.165 , pp. 978-986
    • Benz, R.1    Schmid, A.2    Nakae, T.3    Vos-Scheperkeuter, G.H.4
  • 6
    • 0023472905 scopus 로고
    • Mechanism of sugar transport through the sugar-specific LamB channel of Escherichia coli outer membrane
    • Benz, R., Schmid, A., and Vos-Scheperkeuter, G.H. (1987) Mechanism of sugar transport through the sugar-specific LamB channel of Escherichia coli outer membrane. J Membr Biol 100: 12-29.
    • (1987) J Membr Biol , vol.100 , pp. 12-29
    • Benz, R.1    Schmid, A.2    Vos-Scheperkeuter, G.H.3
  • 7
    • 0026545214 scopus 로고
    • Investigation of the selectivity of maltoporin channels using mutant LamB proteins: Mutations changing the maltodextrin binding site
    • Benz, R., Francis, G., Nakae, T., and Ferenci, T. (1992) Investigation of the selectivity of maltoporin channels using mutant LamB proteins: mutations changing the maltodextrin binding site. Biochim Biophys Acta 1104: 299-307.
    • (1992) Biochim Biophys Acta , vol.1104 , pp. 299-307
    • Benz, R.1    Francis, G.2    Nakae, T.3    Ferenci, T.4
  • 8
    • 0027586320 scopus 로고
    • Tolc of Escherichia coli functions as an outer membrane channel
    • Benz, R., Maier, E., and Gentschev, I. (1993) TolC of Escherichia coli functions as an outer membrane channel. Zentralbl Bakteriol 278: 187-196.
    • (1993) Zentralbl Bakteriol , vol.278 , pp. 187-196
    • Benz, R.1    Maier, E.2    Gentschev, I.3
  • 9
    • 0022911351 scopus 로고
    • Mutagenesis by random linker insertion into the lamB gene of E. coli K12
    • Boulain, J.C., Charbit, A., and Hofnung, M. (1986) Mutagenesis by random linker insertion into the lamB gene of E. coli K12. Mol Gen Genet 205: 339-348.
    • (1986) Mol Gen Genet , vol.205 , pp. 339-348
    • Boulain, J.C.1    Charbit, A.2    Hofnung, M.3
  • 10
    • 0019845615 scopus 로고
    • In vivo and in vitro functional alterations of the bacteriophage lambda receptor in lamB missense mutants of Escherichia coli K12
    • Braun-Breton, C., and Hofnung, M. (1981) In vivo and in vitro functional alterations of the bacteriophage lambda receptor in lamB missense mutants of Escherichia coli K12. J Bacteriol 148: 845-852.
    • (1981) J Bacteriol , vol.148 , pp. 845-852
    • Braun-Breton, C.1    Hofnung, M.2
  • 11
    • 0024278661 scopus 로고
    • Maltose transport and starch binding in phage resistant point mutants of maltoporin functional and topological implications
    • Charbit, A., Gehring, K., Nikaido, H., Ferenci, T., and Hofnung, M. (1988) Maltose transport and starch binding in phage resistant point mutants of maltoporin functional and topological implications. J Mol Biol 201: 487-496.
    • (1988) J Mol Biol , vol.201 , pp. 487-496
    • Charbit, A.1    Gehring, K.2    Nikaido, H.3    Ferenci, T.4    Hofnung, M.5
  • 12
    • 0028277842 scopus 로고
    • A role of residue 151 of LamB in bacteriophage lambda adsorption: Possible steric effect of amino acid substitutions
    • Charbit, A., Werts, C., Michel, V., Klebba, P.E., Quillardet, P., and Hofnung, M. (1994) A role of residue 151 of LamB in bacteriophage lambda adsorption: possible steric effect of amino acid substitutions. J Bacteriol 176: 3204-3209.
    • (1994) J Bacteriol , vol.176 , pp. 3204-3209
    • Charbit, A.1    Werts, C.2    Michel, V.3    Klebba, P.E.4    Quillardet, P.5    Hofnung, M.6
  • 13
    • 0031736256 scopus 로고    scopus 로고
    • A cluster of charged and aromatic residues in the C-terminal portion of maltoporin participates in sugar binding and uptake
    • Charbit, A., Wang, J., Michel, V., and Hofnung, M. (1998) A cluster of charged and aromatic residues in the C-terminal portion of maltoporin participates in sugar binding and uptake. Mol Gen Genet 260: 185-192.
    • (1998) Mol Gen Genet , vol.260 , pp. 185-192
    • Charbit, A.1    Wang, J.2    Michel, V.3    Hofnung, M.4
  • 14
    • 0019856948 scopus 로고
    • Gene sequence of the lambda receptor, an outer membrane protein of Escherichia coli K-12
    • Clement, J.M., and Hofnung, M. (1981) Gene sequence of the lambda receptor, an outer membrane protein of Escherichia coli K-12. Cell 27: 507-514.
    • (1981) Cell , vol.27 , pp. 507-514
    • Clement, J.M.1    Hofnung, M.2
  • 15
    • 0026779245 scopus 로고
    • Crystal structures explain functional properties of two E. coli porins
    • Cowan, S.W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R.A., et al. (1992) Crystal structures explain functional properties of two E. coli porins. Nature 358: 727-733.
    • (1992) Nature , vol.358 , pp. 727-733
    • Cowan, S.W.1    Schirmer, T.2    Rummel, G.3    Steiert, M.4    Ghosh, R.5    Pauptit, R.A.6
  • 16
    • 0023650005 scopus 로고
    • Selectivity for maltose and maltodextrin of maltoporin, a pore-forming protein of E. coli outer membrane
    • Dargent, B., Rosenbusch, J.P., and Pattus, F. (1987) Selectivity for maltose and maltodextrin of maltoporin, a pore-forming protein of E. coli outer membrane. FEBS Lett 220: 136-142.
    • (1987) FEBS Lett , vol.220 , pp. 136-142
    • Dargent, B.1    Rosenbusch, J.P.2    Pattus, F.3
  • 17
    • 0024278648 scopus 로고
    • Effect of point mutations on the in vitro pore properties of maltoporin, a protein of Escherichia coli outer membrane
    • Dargent, B., Charbit, A., Hofnung, M., and Pattus, F. (1988) Effect of point mutations on the in vitro pore properties of maltoporin, a protein of Escherichia coli outer membrane. J Mol Biol 201: 497-506.
    • (1988) J Mol Biol , vol.201 , pp. 497-506
    • Dargent, B.1    Charbit, A.2    Hofnung, M.3    Pattus, F.4
  • 18
    • 0022727889 scopus 로고
    • Mutations affecting antigenic determinants of an outer membrane protein of Escherichia coli
    • Desaymard, C., Debarbouillé, M., Jolit, M., and Schwartz, M. (1986) Mutations affecting antigenic determinants of an outer membrane protein of Escherichia coli. EMBO J 5: 1383-1388.
    • (1986) EMBO J , vol.5 , pp. 1383-1388
    • Desaymard, C.1    Debarbouillé, M.2    Jolit, M.3    Schwartz, M.4
  • 19
    • 0029644059 scopus 로고    scopus 로고
    • Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway
    • Dutzler, R., Wang, Y.F., Rizkallah, P.J., Rosenbusch, J.P., and Schirmer, T. (1996) Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure 4: 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
  • 20
    • 0020491174 scopus 로고
    • Directed evolution of the lambda receptor of Escherichia coli through affinity chromatographic selection
    • Ferenci, T., and Lee, K.-S. (1982) Directed evolution of the lambda receptor of Escherichia coli through affinity chromatographic selection. J Mol Biol 160: 431-444.
    • (1982) J Mol Biol , vol.160 , pp. 431-444
    • Ferenci, T.1    Lee, K.-S.2
  • 21
    • 0018966820 scopus 로고
    • Lambda receptor in the outer membrane of Escherichia coli as a binding protein for maltodextrin and starch poly-saccharides
    • Ferenci, T., Schwentorat, M., Ullrich, S., and Vilmart, J. (1980) Lambda receptor in the outer membrane of Escherichia coli as a binding protein for maltodextrin and starch poly-saccharides. J Bacteriol 142: 521-526.
    • (1980) J Bacteriol , vol.142 , pp. 521-526
    • Ferenci, T.1    Schwentorat, M.2    Ullrich, S.3    Vilmart, J.4
  • 22
    • 0025761083 scopus 로고
    • Genetic mapping of starch- and lambda- receptor sites in maltoporin: Identification of substitutions causing direct and indirect effects on binding sites by cysteine mutagenesis
    • Francis, G., Brennan, Stretton, S., and Ferenci, T. (1991a) Genetic mapping of starch- and lambda- receptor sites in maltoporin: identification of substitutions causing direct and indirect effects on binding sites by cysteine mutagenesis. Mol Microbiol 5: 2293-2301.
    • (1991) Mol Microbiol , vol.5 , pp. 2293-2301
    • Francis, G.1    Brennan2    Stretton, S.3    Ferenci, T.4
  • 23
    • 0025912181 scopus 로고
    • Affinity-Chromatographic purification of sixteen cysteine-substituted maltoporin variants: Thiol reactivity and cross-linking in an outer membrane protein of Escherichia coli
    • Francis, G., Brennan, L., and Ferenci, T. (1991b) Affinity-Chromatographic purification of sixteen cysteine-substituted maltoporin variants: thiol reactivity and cross-linking in an outer membrane protein of Escherichia coli. Biochim Biophys Acta 1067: 89-96.
    • (1991) Biochim Biophys Acta , vol.1067 , pp. 89-96
    • Francis, G.1    Brennan, L.2    Ferenci, T.3
  • 24
    • 0020318345 scopus 로고
    • Monoclonal antibodies as a probe for structure and function of Escherichia coli outer membrane protein
    • Gabay, J., and Schwartz, M. (1982) Monoclonal antibodies as a probe for structure and function of Escherichia coli outer membrane protein. J Biol Chem 257: 6627-6630.
    • (1982) J Biol Chem , vol.257 , pp. 6627-6630
    • Gabay, J.1    Schwartz, M.2
  • 25
    • 0020309419 scopus 로고
    • Outer membrane protein P of Pseudomonas aeruginosa: Regulation by phosphate deficiency and formation of small anion-specific channels in lipid bilayer membranes
    • Hancock, R.E.W., Poole, K., and Benz, R. (1982) Outer membrane protein P of Pseudomonas aeruginosa: regulation by phosphate deficiency and formation of small anion-specific channels in lipid bilayer membranes. J Bacteriol 150: 730-738.
    • (1982) J Bacteriol , vol.150 , pp. 730-738
    • Hancock, R.E.W.1    Poole, K.2    Benz, R.3
  • 26
    • 0023986359 scopus 로고
    • Genetic analysis of sequences in maltoporin that contribute to binding domains and pore structure
    • Heine, H.G., Francis, G., Lee, K.S., and Ferenci, T. (1988) Genetic analysis of sequences in maltoporin that contribute to binding domains and pore structure. J Bacteriol 170: 1730-1738.
    • (1988) J Bacteriol , vol.170 , pp. 1730-1738
    • Heine, H.G.1    Francis, G.2    Lee, K.S.3    Ferenci, T.4
  • 27
    • 0028933982 scopus 로고
    • An intelligent channel (and more)
    • Hofnung, M. (1995) An intelligent channel (and more). Science 267: 473-474.
    • (1995) Science , vol.267 , pp. 473-474
    • Hofnung, M.1
  • 28
    • 0030596521 scopus 로고    scopus 로고
    • Rate constants of sugar transport through two LamB mutants of Escherichia coli: Comparison with wild-type maltoporin and LamB of Salmonella typhimurium
    • Jordy, M., Andersen, C., Schulein, K., Ferenci, T., and Benz, R. (1996) Rate constants of sugar transport through two LamB mutants of Escherichia coli: comparison with wild-type maltoporin and LamB of Salmonella typhimurium. J Mol Biol 259: 666-678.
    • (1996) J Mol Biol , vol.259 , pp. 666-678
    • Jordy, M.1    Andersen, C.2    Schulein, K.3    Ferenci, T.4    Benz, R.5
  • 29
    • 0027959128 scopus 로고
    • A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis
    • Klebba, P., Hofnung, M., and Charbit, A. (1994) A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis. EMBO J 13: 4670-4675.
    • (1994) EMBO J , vol.13 , pp. 4670-4675
    • Klebba, P.1    Hofnung, M.2    Charbit, A.3
  • 30
    • 0030871753 scopus 로고    scopus 로고
    • Further genetic analysis of the C-terminal external loop region in Escherichia coli maltoporin
    • Klebba, P.E., Newton, S.M.C., Charbit, A., Michel, V., Perrin, D., and Hofnung, M. (1997) Further genetic analysis of the C-terminal external loop region in Escherichia coli maltoporin. Res Microbiol 148: 375-387.
    • (1997) Res Microbiol , vol.148 , pp. 375-387
    • Klebba, P.E.1    Newton, S.M.C.2    Charbit, A.3    Michel, V.4    Perrin, D.5    Hofnung, M.6
  • 31
    • 0009551491 scopus 로고
    • Specificity of diffusion channels produced by λ-phage receptor protein of Escherichia coli
    • Luckey, M., and Nikaido, H. (1980) Specificity of diffusion channels produced by λ-phage receptor protein of Escherichia coli. Proc Natl Acad Sci USA 77: 165-171.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 165-171
    • Luckey, M.1    Nikaido, H.2
  • 32
    • 0023852792 scopus 로고
    • Pore-forming activity of the Tsx protein from the outer membrane of Escherichia coli. Demonstration of a nucleoside-specific binding site
    • Maier, C., Bremer, E., Schmid, A., and Benz, R. (1988) 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: 2493-2499.
    • (1988) J Biol Chem , vol.263 , pp. 2493-2499
    • Maier, C.1    Bremer, E.2    Schmid, A.3    Benz, R.4
  • 33
    • 0027787823 scopus 로고
    • The activity of ▲E, an Escherichia coli heat-inducible ▲-factor, is modulated by expression of outer membrane proteins
    • Mescas, J., Rouvière, P.E., Erickson, J.W., Donohue, T.J., and Gross, C.A. (1993) The activity of ▲E, an Escherichia coli heat-inducible ▲-factor, is modulated by expression of outer membrane proteins. Genes Dev 7: 2618-2628.
    • (1993) Genes Dev , vol.7 , pp. 2618-2628
    • Mescas, J.1    Rouvière, P.E.2    Erickson, J.W.3    Donohue, T.J.4    Gross, C.A.5
  • 34
    • 0017703344 scopus 로고
    • Outer membrane of Gram-negative bacteria. XVII. Specificity of transport process catalyzed by the λ-receptor protein in Escherichia coli
    • von Meyenburg, K., and Nikaido, H. (1977) Outer membrane of Gram-negative bacteria. XVII. Specificity of transport process catalyzed by the λ-receptor protein in Escherichia coli. Biochem Biophys Res Commun 78: 1100-1107.
    • (1977) Biochem Biophys Res Commun , vol.78 , pp. 1100-1107
    • Von Meyenburg, K.1    Nikaido, H.2
  • 35
    • 0031557404 scopus 로고    scopus 로고
    • Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside
    • Meyer, J.E.W., Hofnung, M., and Schulz, G.E. (1997) Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J Mol Biol 266: 761-775.
    • (1997) J Mol Biol , vol.266 , pp. 761-775
    • Meyer, J.E.W.1    Hofnung, M.2    Schulz, G.E.3
  • 36
    • 0023677064 scopus 로고
    • Genetic identification of the pore domain of the OmpC porin of E. coli
    • Misra, R., and Benson, S.A. (1988) Genetic identification of the pore domain of the OmpC porin of E. coli. J Bacteriol 170: 3611-3617.
    • (1988) J Bacteriol , vol.170 , pp. 3611-3617
    • Misra, R.1    Benson, S.A.2
  • 37
    • 0030976053 scopus 로고    scopus 로고
    • Signal transduction pathways in response to protein misfolding in the extracytoplasmic compartments of E. coli: Role of two new phosphoprotein phosphatases PrpA and PrpB
    • Missiakas, D., and Raina, S. (1997) Signal transduction pathways in response to protein misfolding in the extracytoplasmic compartments of E. coli: role of two new phosphoprotein phosphatases PrpA and PrpB. EMBO J 16: 1670-1685.
    • (1997) EMBO J , vol.16 , pp. 1670-1685
    • Missiakas, D.1    Raina, S.2
  • 38
    • 0017155947 scopus 로고
    • Identification of the major outer membrane protein of Escherichia coli that produces transmembrane channels in reconstituted vesicle membranes
    • Nakae, T. (1976) Identification of the major outer membrane protein of Escherichia coli that produces transmembrane channels in reconstituted vesicle membranes. Biochem Biophys Res Commun 71: 877-884.
    • (1976) Biochem Biophys Res Commun , vol.71 , pp. 877-884
    • Nakae, T.1
  • 39
    • 0029971104 scopus 로고    scopus 로고
    • Topology of the membrane protein LamB by epitope tagging and a comparison with the Xray model
    • Newton, S.M.C., Klebba, P.E., Michel, V., Hofnung, M., and Charbit, A. (1996) Topology of the membrane protein LamB by epitope tagging and a comparison with the Xray model. J Bacteriol 178: 3447-3456.
    • (1996) J Bacteriol , vol.178 , pp. 3447-3456
    • Newton, S.M.C.1    Klebba, P.E.2    Michel, V.3    Hofnung, M.4    Charbit, A.5
  • 40
    • 0001177510 scopus 로고
    • Porins and specific channels of bacterial outer membranes
    • Nikaido, H. (1992) Porins and specific channels of bacterial outer membranes. Mol Microbiol 267: 512-514.
    • (1992) Mol Microbiol , vol.267 , pp. 512-514
    • Nikaido, H.1
  • 41
    • 0018085911 scopus 로고
    • Major outer membrane protein in Salmonella typhimurium induced by maltose
    • Palva, E.T. (1978) Major outer membrane protein in Salmonella typhimurium induced by maltose. J Bacteriol 136: 286-294.
    • (1978) J Bacteriol , vol.136 , pp. 286-294
    • Palva, E.T.1
  • 42
    • 0026545681 scopus 로고
    • Formation of a gated channel by a ligand-specific transport protein in the bacterial outer membrane
    • Rutz, J.M., Liu, J., Lyons, J.A., Goranson, J., Armstrong, S.K., McIntosh, M.A., et al. (1992) Formation of a gated channel by a ligand-specific transport protein in the bacterial outer membrane. Science 258: 471-475.
    • (1992) Science , vol.258 , pp. 471-475
    • Rutz, J.M.1    Liu, J.2    Lyons, J.A.3    Goranson, J.4    Armstrong, S.K.5    McIntosh, M.A.6
  • 43
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.5 Å resolution
    • Schirmer, T., Keller, T., Wang, Y.F., and Rosenbush, J.P. (1995) Structural basis for sugar translocation through maltoporin channels at 3.5 Å resolution. Science 267: 512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.2    Wang, Y.F.3    Rosenbush, J.P.4
  • 44
    • 0029087726 scopus 로고
    • The deletion of 70 amino acids near the N-terminal end of the sucrose porin Scry causes its functional similarity to LamB in vivo and in vitro
    • Schülein, K., Andersen, C., and Benz, R. (1995) The deletion of 70 amino acids near the N-terminal end of the sucrose porin Scry causes its functional similarity to LamB in vivo and in vitro. Mol Microbiol 17: 757-767.
    • (1995) Mol Microbiol , vol.17 , pp. 757-767
    • Schülein, K.1    Andersen, C.2    Benz, R.3
  • 45
    • 0024673026 scopus 로고
    • Characterization of degP, a gene required for proteolysis of the cell envelope and essential for growth of Escherichia coli at high temperature
    • Strauch, K.L., Johnson, K., and Beckwith, J. (1989) Characterization of degP, a gene required for proteolysis of the cell envelope and essential for growth of Escherichia coli at high temperature. J Bacteriol 171: 2689-2696.
    • (1989) J Bacteriol , vol.171 , pp. 2689-2696
    • Strauch, K.L.1    Johnson, K.2    Beckwith, J.3
  • 46
    • 0016678144 scopus 로고
    • Maltose transport in Escherichia coli K-12: Involvement of the bacteriophage lambda receptor
    • Szmelcman, S., and Hofnung, M. (1975) Maltose transport in Escherichia coli K-12: involvement of the bacteriophage lambda receptor. J Bacteriol 124: 112-118.
    • (1975) J Bacteriol , vol.124 , pp. 112-118
    • Szmelcman, S.1    Hofnung, M.2
  • 47
    • 0027151855 scopus 로고
    • Immunological relatedness of the LamB proteins among members of Enterobacteriaceae
    • Werts, C., O'Callaghan, D., Hofnung, M., and Charbit, A. (1993) Immunological relatedness of the LamB proteins among members of Enterobacteriaceae. J Gen Microbiol 139: 881-887.
    • (1993) J Gen Microbiol , vol.139 , pp. 881-887
    • Werts, C.1    O'Callaghan, D.2    Hofnung, M.3    Charbit, A.4
  • 48
    • 0028029005 scopus 로고
    • Adsorption of bacteriophage lambda on the LamB protein of E. coli K12: Point mutations in gene J of lambda responsible for extended host range
    • Werts, C., Michel, V., Hofnung, M., and Charbit, A. (1994) Adsorption of bacteriophage lambda on the LamB protein of E. coli K12: point mutations in gene J of lambda responsible for extended host range. J Bacteriol 176: 941-947.
    • (1994) J Bacteriol , vol.176 , pp. 941-947
    • Werts, C.1    Michel, V.2    Hofnung, M.3    Charbit, A.4


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