메뉴 건너뛰기




Volumn 178, Issue 1, 1996, Pages 68-77

A binding-lipoprotein-dependent oligopeptide transport system in Streptococcus gordonii essential for uptake of hexa- and heptapeptides

Author keywords

[No Author keywords available]

Indexed keywords

LIPOPROTEIN; OLIGOPEPTIDE;

EID: 0030063057     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.1.68-77.1996     Document Type: Article
Times cited : (65)

References (61)
  • 1
    • 0028072561 scopus 로고
    • The dipeptide permease of Escherichia coli closely resembles other bacterial transport systems and shows growth-phase-dependent expression
    • Abouhamad, W. N., and M. D. Manson. 1994. The dipeptide permease of Escherichia coli closely resembles other bacterial transport systems and shows growth-phase-dependent expression. Mol Microbiol. 14:1077-1092.
    • (1994) Mol Microbiol. , vol.14 , pp. 1077-1092
    • Abouhamad, W.N.1    Manson, M.D.2
  • 2
    • 0025732327 scopus 로고
    • Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: Characterization of the dipeptide permease and the dipeptide-binding protein
    • Abouhamad, W. N., M. D. Manson, M. M. Gibson, and C. F. Higgins. 1991. Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: characterization of the dipeptide permease and the dipeptide-binding protein Mol. Microbiol 5:1035-1047.
    • (1991) Mol. Microbiol , vol.5 , pp. 1035-1047
    • Abouhamad, W.N.1    Manson, M.D.2    Gibson, M.M.3    Higgins, C.F.4
  • 3
    • 0028128820 scopus 로고
    • Three highly homologous membrane-bound lipoproteins participate in oligopeptide transport by the amt system of gram-positive Streptococcus pneumoniae
    • Alloing, G., P. de Philip, and J.-P. Claverys. 1994. Three highly homologous membrane-bound lipoproteins participate in oligopeptide transport by the amt system of gram-positive Streptococcus pneumoniae J. Mol. Biol. 241:44-58.
    • (1994) J. Mol. Biol. , vol.241 , pp. 44-58
    • Alloing, G.1    De Philip, P.2    Claverys, J.-P.3
  • 4
    • 0025327409 scopus 로고
    • The amt locus of the gram-positive bacterium Streptococcus pneumoniae is similar to binding protein-dependent transport operons of gram-negative bacteria
    • Alloing, G., M.-C. Trombe, and J.-P. Claverys. 1990. The amt locus of the gram-positive bacterium Streptococcus pneumoniae is similar to binding protein-dependent transport operons of gram-negative bacteria. Mol. Microbiol. 4:633-644.
    • (1990) Mol. Microbiol. , vol.4 , pp. 633-644
    • Alloing, G.1    Trombe, M.-C.2    Claverys, J.-P.3
  • 6
    • 0021733780 scopus 로고
    • Directional cloning of DNA fragments at a large distance from initial probe: A circularization method
    • Collins, F. S., and S. M. Weissman. 1984. Directional cloning of DNA fragments at a large distance from initial probe: a circularization method. Proc. Natl. Acad. Sci USA 81:6812-6816.
    • (1984) Proc. Natl. Acad. Sci USA , vol.81 , pp. 6812-6816
    • Collins, F.S.1    Weissman, S.M.2
  • 7
    • 0029042013 scopus 로고
    • Peptide permeases from Streptococcus pneumoniae affect adherence to eukaryotic cells
    • Cundell, D. R., B. J. Pearce, J. Sandros, A. M. Naughton, and H. R. Masure. 1995. Peptide permeases from Streptococcus pneumoniae affect adherence to eukaryotic cells. Infect Immun. 63:2493-2498.
    • (1995) Infect Immun. , vol.63 , pp. 2493-2498
    • Cundell, D.R.1    Pearce, B.J.2    Sandros, J.3    Naughton, A.M.4    Masure, H.R.5
  • 8
    • 0018365125 scopus 로고
    • Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells
    • Dagert, M., and S. D. Ehrlich. 1979. Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells. Gene 6:23-28.
    • (1979) Gene , vol.6 , pp. 23-28
    • Dagert, M.1    Ehrlich, S.D.2
  • 9
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 10
    • 0027295459 scopus 로고
    • Characterization of allelic replacement in Streptococcus parasanguis: Transformation and homologous recombination in a nontransformable streptococcus
    • Fenno, F. C., A. Shaikh, and P. Fives-Taylor. 1993. Characterization of allelic replacement in Streptococcus parasanguis: transformation and homologous recombination in a nontransformable streptococcus. Gene 130:81-90.
    • (1993) Gene , vol.130 , pp. 81-90
    • Fenno, F.C.1    Shaikh, A.2    Fives-Taylor, P.3
  • 11
    • 0028960851 scopus 로고
    • The fimA locus of Streptococcus parasanguis encodes an ATP-binding membrane transport system
    • Fenno, J. C., A. Shaikh, G. Spatafora, and P. Fives-Taylor. 1995. The fimA locus of Streptococcus parasanguis encodes an ATP-binding membrane transport system. Mol. Microbiol. 15:849-863.
    • (1995) Mol. Microbiol. , vol.15 , pp. 849-863
    • Fenno, J.C.1    Shaikh, A.2    Spatafora, G.3    Fives-Taylor, P.4
  • 12
    • 0026178870 scopus 로고
    • Ecology of viridans streptococci in the oral cavity and pharynx
    • Frandsen, E. V. G., V. Pedrazzoli, and M. Kilian. 1991. Ecology of viridans streptococci in the oral cavity and pharynx Oral Microbiol. Immunol. 6:129-133.
    • (1991) Oral Microbiol. Immunol. , vol.6 , pp. 129-133
    • Frandsen, E.V.G.1    Pedrazzoli, V.2    Kilian, M.3
  • 13
    • 0021193852 scopus 로고
    • Genetic characterisation and molecular cloning of the tripeptide permease (tpp) genes of Salmonella typhimurium
    • Gibson, M. M., M. Price, and C. F. Higgins. 1984. Genetic characterisation and molecular cloning of the tripeptide permease (tpp) genes of Salmonella typhimurium. J. Bacteriol. 160:122-130.
    • (1984) J. Bacteriol. , vol.160 , pp. 122-130
    • Gibson, M.M.1    Price, M.2    Higgins, C.F.3
  • 14
    • 0023636673 scopus 로고
    • Uptake of cell wall peptides by Salmonella typhimurium and Escherichia coli
    • Goodell, E. W., and C. F. Higgins. 1987. Uptake of cell wall peptides by Salmonella typhimurium and Escherichia coli. J Bacteriol. 169:3861-3865.
    • (1987) J Bacteriol. , vol.169 , pp. 3861-3865
    • Goodell, E.W.1    Higgins, C.F.2
  • 15
    • 0023038504 scopus 로고
    • Binding specificity of the periplasmic oligopeptide-binding protein from Escherichia coli
    • Guyer, C. A., D. G. Morgan, and J. V. Staros. 1986. Binding specificity of the periplasmic oligopeptide-binding protein from Escherichia coli. J. Bacteriol. 168:775-779.
    • (1986) J. Bacteriol. , vol.168 , pp. 775-779
    • Guyer, C.A.1    Morgan, D.G.2    Staros, J.V.3
  • 16
    • 0000075317 scopus 로고
    • Techniques for transformation of E. coli
    • D M. Glover (ed.). IRL Press, Oxford
    • Hanahan, D. 1985 Techniques for transformation of E. coli, p. 109-135. In D M. Glover (ed.). DNA cloning, vol. 1. IRL Press, Oxford.
    • (1985) DNA Cloning , vol.1 , pp. 109-135
    • Hanahan, D.1
  • 18
    • 0025963832 scopus 로고
    • Mutants of Streptococcus gordonii Challis over-producing glucosyltransferase
    • Haisman, R. J., and H. F. Jenkinson. 1991. Mutants of Streptococcus gordonii Challis over-producing glucosyltransferase. J. Gen. Microbiol. 137:483-489.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 483-489
    • Haisman, R.J.1    Jenkinson, H.F.2
  • 19
    • 0026629422 scopus 로고
    • The hbpA gene of Haemophilus influenzae type b encodes a heme-binding lipoprotein conserved among heme-dependent Haemophilus species
    • Hanson, M. S., C. Slaughter, and E. J. Hansen. 1992. The hbpA gene of Haemophilus influenzae type b encodes a heme-binding lipoprotein conserved among heme-dependent Haemophilus species. Infect Immun 60:2257-2266.
    • (1992) Infect Immun , vol.60 , pp. 2257-2266
    • Hanson, M.S.1    Slaughter, C.2    Hansen, E.J.3
  • 20
    • 0026621245 scopus 로고
    • ABC transporters from microorganisms to man
    • Higgins, C. F. 1992. ABC transporters from microorganisms to man Annu Rev. Cell Biol. 8:67-113.
    • (1992) Annu Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 21
    • 0023644827 scopus 로고
    • Molecular characterization of the oligopeptide permease of Salmonella typhimurium
    • Hiles, I. D., M. P. Gallagher, D. J. Jamieson, and C. F. Higgins. 1987. Molecular characterization of the oligopeptide permease of Salmonella typhimurium. J. Mol Biol. 195:125-142
    • (1987) J. Mol Biol. , vol.195 , pp. 125-142
    • Hiles, I.D.1    Gallagher, M.P.2    Jamieson, D.J.3    Higgins, C.F.4
  • 22
    • 0022446340 scopus 로고
    • Cell-surface proteins of Streptococcus sanguis associated with cell hydrophobicity and coaggregation properties
    • Jenkinson, H. F. 1986. Cell-surface proteins of Streptococcus sanguis associated with cell hydrophobicity and coaggregation properties J. Gen Microbiol 132:1575-1589
    • (1986) J. Gen Microbiol , vol.132 , pp. 1575-1589
    • Jenkinson, H.F.1
  • 23
    • 0023199482 scopus 로고
    • Novobiocin-resistant mutants of Streptococcus sangius with reduced cell hydrophobicity and defective in coaggregation
    • Jenkinson, H. F. 1987. Novobiocin-resistant mutants of Streptococcus sangius with reduced cell hydrophobicity and defective in coaggregation. J. Gen. Microbiol. 133:1909-1918
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 1909-1918
    • Jenkinson, H.F.1
  • 24
    • 85035158804 scopus 로고
    • Phenotypic effects of inactivating the gene encoding a cell-surface binding-protein in Streptococcus gordonii Challis
    • G. M. Dunny, P P Cleary, and L. L. McKay (ed.). American Society for Microbiology, Washington, D.C.
    • Jenkinson, H. F. 1991. Phenotypic effects of inactivating the gene encoding a cell-surface binding-protein in Streptococcus gordonii Challis, p. 284-288 In G. M. Dunny, P P Cleary, and L. L. McKay (ed.). Genetics and molecular biology of streptococci, lactococci, and enterococci. American Society for Microbiology, Washington, D.C.
    • (1991) Genetics and Molecular Biology of Streptococci, Lactococci, and Enterococci , pp. 284-288
    • Jenkinson, H.F.1
  • 25
    • 0026553480 scopus 로고
    • Adherence, coaggregation, and hydrophobicity of Streptococcus gordonii associated with expression of cell-surface lipoproteins
    • Jenkinson, H. F. 1992. Adherence, coaggregation, and hydrophobicity of Streptococcus gordonii associated with expression of cell-surface lipoproteins. Infect Immun 60:1225-1228.
    • (1992) Infect Immun , vol.60 , pp. 1225-1228
    • Jenkinson, H.F.1
  • 26
    • 0028352296 scopus 로고
    • Adherence and accumulation of oral streptococci
    • Jenkinson, H. F. 1994 Adherence and accumulation of oral streptococci Trends Microbiol. 2:209-212
    • (1994) Trends Microbiol. , vol.2 , pp. 209-212
    • Jenkinson, H.F.1
  • 27
    • 0027992299 scopus 로고
    • Cell-surface protein receptors of oral streptococci
    • Jenkinson, H. F. 1994. Cell-surface protein receptors of oral streptococci FEMS Microbiol Lett. 121:133-140.
    • (1994) FEMS Microbiol Lett. , vol.121 , pp. 133-140
    • Jenkinson, H.F.1
  • 28
    • 0025054603 scopus 로고
    • Insertional inactivation of the gene encoding a 76 kilodalton cell-surface polypeptide in Streptococcus gordomi Challis has a pletotropic effect on cell surface composition and properties
    • Jenkinson, H. F., and R. A. Easingwood. 1990. Insertional inactivation of the gene encoding a 76 kilodalton cell-surface polypeptide in Streptococcus gordomi Challis has a pletotropic effect on cell surface composition and properties. Infect. Immun. 58:3689-3697
    • (1990) Infect. Immun. , vol.58 , pp. 3689-3697
    • Jenkinson, H.F.1    Easingwood, R.A.2
  • 29
    • 0027254512 scopus 로고
    • Inactivation of the gene encoding surface protein SspA in Streptococcus gordonii DL1 affects cell interactions with human salivary agglutinin and oral actinomyces
    • Jenkinson, H. F., S. D. Terry, R. McNab, and G. W. Tannuck. 1993. Inactivation of the gene encoding surface protein SspA in Streptococcus gordonii DL1 affects cell interactions with human salivary agglutinin and oral actinomyces. Infect. Immun. 61:3199-3208
    • (1993) Infect. Immun. , vol.61 , pp. 3199-3208
    • Jenkinson, H.F.1    Terry, S.D.2    McNab, R.3    Tannuck, G.W.4
  • 30
    • 0027971083 scopus 로고
    • Identification of a second oligopeptide transport system in Bacillus subtilis and determination of its role in sporulation
    • Koide, A., and J. A. Hoch. 1994. Identification of a second oligopeptide transport system in Bacillus subtilis and determination of its role in sporulation. Mol. Microbiol. 13:417-426.
    • (1994) Mol. Microbiol. , vol.13 , pp. 417-426
    • Koide, A.1    Hoch, J.A.2
  • 31
    • 0028100391 scopus 로고
    • Nucleotide sequence of the Streptococcus gordonii PK488 coaggregation adhesin gene, scaA, and ATP-binding cassette
    • Kolenbrander, P. E., R. N. Andersen, and N. Ganeshkumar. 1994. Nucleotide sequence of the Streptococcus gordonii PK488 coaggregation adhesin gene, scaA, and ATP-binding cassette. Infect. Immun. 62:4469-4480.
    • (1994) Infect. Immun. , vol.62 , pp. 4469-4480
    • Kolenbrander, P.E.1    Andersen, R.N.2    Ganeshkumar, N.3
  • 32
    • 0027528827 scopus 로고
    • Di-tripeptides and oligopeptides are taken up via distinct transport mechanisms in Lactococcus lactis
    • Kunji, E. R. S., E. J. Smid, R. Plapp, B. Poolman, and W. N. Konings. 1993. Di-tripeptides and oligopeptides are taken up via distinct transport mechanisms in Lactococcus lactis. J. Bacteriol. 175:2052-2059.
    • (1993) J. Bacteriol. , vol.175 , pp. 2052-2059
    • Kunji, E.R.S.1    Smid, E.J.2    Plapp, R.3    Poolman, B.4    Konings, W.N.5
  • 33
    • 0015853344 scopus 로고
    • Maturation of the head of bacteriophage T4. I. DNA packaging events
    • Laemmli, U. K., and M. Favre. 1973 Maturation of the head of bacteriophage T4. I. DNA packaging events. J. Mol. Biol. 80:575-599.
    • (1973) J. Mol. Biol. , vol.80 , pp. 575-599
    • Laemmli, U.K.1    Favre, M.2
  • 35
    • 0019187242 scopus 로고
    • Chimeric streptococcal plasmids and their use as molecular cloning vehicles in Streptococcus sanguis (Challis)
    • Macrina, F. L., K. R. Jones, and P. H. Wood. 1980 Chimeric streptococcal plasmids and their use as molecular cloning vehicles in Streptococcus sanguis (Challis). J. Bacteriol. 143:1425-1435.
    • (1980) J. Bacteriol. , vol.143 , pp. 1425-1435
    • Macrina, F.L.1    Jones, K.R.2    Wood, P.H.3
  • 36
    • 0028284877 scopus 로고
    • Biochemical and genetic characterization of a competence pheromone from Bacillus subtilis
    • Magnuson, R., J. Solomon, and A. D. Grossman. 1994. Biochemical and genetic characterization of a competence pheromone from Bacillus subtilis Cell 77:207-216.
    • (1994) Cell , vol.77 , pp. 207-216
    • Magnuson, R.1    Solomon, J.2    Grossman, A.D.3
  • 38
    • 0026728196 scopus 로고
    • Gene disruption identifies a 290 kilodalton cell-surface polypeptide conferring hydrophobicity and coaggregation properties in Streptococcus gordonn
    • McNab, R., and H. F. Jenkinson. 1992. Gene disruption identifies a 290 kilodalton cell-surface polypeptide conferring hydrophobicity and coaggregation properties in Streptococcus gordonn. Mol. Microbiol. 6:2939-2949.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2939-2949
    • McNab, R.1    Jenkinson, H.F.2
  • 39
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels a modified procedure with enhanced uniform sensitivity
    • Morrissey, J. H. 1981. Silver stain for proteins in polyacrylamide gels a modified procedure with enhanced uniform sensitivity. Anal. Biochem 117:307-310.
    • (1981) Anal. Biochem , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 40
    • 0026084296 scopus 로고
    • Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein
    • Olson, E. R., D. S. Dunyak, L. M. Jurss, and R. A. Poorman. 1991. Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein. J. Bacteriol. 173:234-244.
    • (1991) J. Bacteriol. , vol.173 , pp. 234-244
    • Olson, E.R.1    Dunyak, D.S.2    Jurss, L.M.3    Poorman, R.A.4
  • 41
    • 0001255656 scopus 로고
    • On the nature of competence of transformable streptococci
    • Pakula, R., and W. Walczak. 1963. On the nature of competence of transformable streptococci. J Gen. Microbiol 31:125-133.
    • (1963) J Gen. Microbiol , vol.31 , pp. 125-133
    • Pakula, R.1    Walczak, W.2
  • 42
    • 0014410253 scopus 로고
    • Size restriction on peptide utilization in Escherichia coli
    • Payne, J. W., and C. Gilvarg. 1968. Size restriction on peptide utilization in Escherichia coli. J. Biol. Chem. 243:6292-6299.
    • (1968) J. Biol. Chem. , vol.243 , pp. 6292-6299
    • Payne, J.W.1    Gilvarg, C.2
  • 43
    • 0028286632 scopus 로고
    • Peptide permeases modulate transformation in Streptococcus pneumoniae
    • Pearce, B. J., A. M. Naughton, and H. R. Masure. 1994. Peptide permeases modulate transformation in Streptococcus pneumoniae. Mol. Microbiol 12:881-892
    • (1994) Mol. Microbiol , vol.12 , pp. 881-892
    • Pearce, B.J.1    Naughton, A.M.2    Masure, H.R.3
  • 44
    • 0026031219 scopus 로고
    • The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation
    • Perego, M., C. F. Higgins, S. R. Pearce, M. P. Gallagher, and J. A. Hoch. 1991 The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation. Mol. Microbiol. 5:173-185.
    • (1991) Mol. Microbiol. , vol.5 , pp. 173-185
    • Perego, M.1    Higgins, C.F.2    Pearce, S.R.3    Gallagher, M.P.4    Hoch, J.A.5
  • 45
    • 0015016327 scopus 로고
    • A comparison of streptococcal competence factors produced by strain Challis in chemically defined and complex media
    • Ranhand, J. M., R. M. Cole, and C. G. Leonard. 1970 A comparison of streptococcal competence factors produced by strain Challis in chemically defined and complex media. J. Gen. Microbiol. 65:131-138.
    • (1970) J. Gen. Microbiol. , vol.65 , pp. 131-138
    • Ranhand, J.M.1    Cole, R.M.2    Leonard, C.G.3
  • 46
    • 0025971265 scopus 로고
    • The spoOK locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence
    • Rudner, D. Z., J. R. LeDeaux, K. Ireton, and A. D. Grossman. 1991 The spoOK locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence. J. Bacteriol. 173:1388-1398.
    • (1991) J. Bacteriol. , vol.173 , pp. 1388-1398
    • Rudner, D.Z.1    LeDeaux, J.R.2    Ireton, K.3    Grossman, A.D.4
  • 47
    • 0027258080 scopus 로고
    • Cloning and characterization of a region of the Enterococcus faecalis conjugative plasmid, pCF10, encoding a sex pheromone-bmding function
    • Ruhfel, R. E., D. A. Manias, and G. M. Dunny. 1993 Cloning and characterization of a region of the Enterococcus faecalis conjugative plasmid, pCF10, encoding a sex pheromone-bmding function. J Bacteriol 175:5253-5259.
    • (1993) J Bacteriol , vol.175 , pp. 5253-5259
    • Ruhfel, R.E.1    Manias, D.A.2    Dunny, G.M.3
  • 49
    • 0013837696 scopus 로고
    • Genetic recombination in DNA-induced transformation of pneumococcus. II. Mapping the amiA locus
    • Sicard, A. M., and H. Ephrussi-Taylor. 1965. Genetic recombination in DNA-induced transformation of pneumococcus. II. Mapping the amiA locus. Genetics 52:1207-1227.
    • (1965) Genetics , vol.52 , pp. 1207-1227
    • Sicard, A.M.1    Ephrussi-Taylor, H.2
  • 50
    • 0024528551 scopus 로고
    • Mechanism and energetics of dipeptide transport in membrane vesicles of Lactococcus lactis
    • Smid, E., A. J. M. Driessen, and W. N. Konings. 1989. Mechanism and energetics of dipeptide transport in membrane vesicles of Lactococcus lactis. J. Bacteriol. 171:292-298.
    • (1989) J. Bacteriol. , vol.171 , pp. 292-298
    • Smid, E.1    Driessen, A.J.M.2    Konings, W.N.3
  • 51
    • 0028987131 scopus 로고
    • Lipoproteins of gram-positive bacteria
    • Sutcliffe, I. C., and R. R. B. Russell. 1995. Lipoproteins of gram-positive bacteria J Bacteriol. 177:1123-1128.
    • (1995) J Bacteriol. , vol.177 , pp. 1123-1128
    • Sutcliffe, I.C.1    Russell, R.R.B.2
  • 52
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R., and M. H. Saier, Jr. 1993. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria Microbiol. Rev. 57:320-346.
    • (1993) Microbiol. Rev. , vol.57 , pp. 320-346
    • Tam, R.1    Saier Jr., M.H.2
  • 54
    • 0027327752 scopus 로고
    • Characterization of the traC determinant of the Enterococcus faecalis hemolysin-bacteriocin plasmid pAD1: Binding of sex pheromone
    • Taniomoto, K., F. Y. An, and D. B. Clewell. 1993. Characterization of the traC determinant of the Enterococcus faecalis hemolysin-bacteriocin plasmid pAD1: binding of sex pheromone. J. Bacteriol 175:5260-5264.
    • (1993) J. Bacteriol , vol.175 , pp. 5260-5264
    • Taniomoto, K.1    An, F.Y.2    Clewell, D.B.3
  • 55
    • 0021687513 scopus 로고
    • Characterization and expression of a cloned tetracycline resistance determinant from the chromosome of Streptococcus mutans
    • Tobian, J. A., M. L. Cline, and F. L. Macrina. 1984. Characterization and expression of a cloned tetracycline resistance determinant from the chromosome of Streptococcus mutans J. Bacteriol. 160:556-563.
    • (1984) J. Bacteriol. , vol.160 , pp. 556-563
    • Tobian, J.A.1    Cline, M.L.2    Macrina, F.L.3
  • 56
    • 0020604683 scopus 로고
    • Nucleotide sequence of the Streptococcus faecalis plasmid gene encoding the 3′5′-aminoglycoside phosphotransferase type III
    • Trieu-Cuot, P., and P. Courvalin. 1983. Nucleotide sequence of the Streptococcus faecalis plasmid gene encoding the 3′5′-aminoglycoside phosphotransferase type III. Gene 23:331-341.
    • (1983) Gene , vol.23 , pp. 331-341
    • Trieu-Cuot, P.1    Courvalin, P.2
  • 57
    • 0021875214 scopus 로고
    • Entry of methotrexate into Streptococcus pneumoniae: A study on a wild-type strain and a methotrexate resistant mutant
    • Trombe, M. C. 1985. Entry of methotrexate into Streptococcus pneumoniae: a study on a wild-type strain and a methotrexate resistant mutant. J. Gen. Microbiol. 131:1273-1278.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 1273-1278
    • Trombe, M.C.1
  • 58
    • 0021166269 scopus 로고
    • Characterization of a Streptococcus pneumoniae mutant with altered electric transmembrane potential
    • Trombe, M. C., G. Laneelle, and A. M. Sicard. 1984. Characterization of a Streptococcus pneumoniae mutant with altered electric transmembrane potential J Bacteriol. 158:1109-1114.
    • (1984) J Bacteriol. , vol.158 , pp. 1109-1114
    • Trombe, M.C.1    Laneelle, G.2    Sicard, A.M.3
  • 59
    • 0027375439 scopus 로고
    • Genetic and biochemical characterization of the oligopeptide transport system of Lactococcus lactis
    • Tynkkynen, S., G. Buist, E. Kunji, J. Kok, B. Poolman, G. Venema, and A. Haandrikman. 1993 Genetic and biochemical characterization of the oligopeptide transport system of Lactococcus lactis. J. Bacteriol. 175:7523-7532.
    • (1993) J. Bacteriol. , vol.175 , pp. 7523-7532
    • Tynkkynen, S.1    Buist, G.2    Kunji, E.3    Kok, J.4    Poolman, B.5    Venema, G.6    Haandrikman, A.7
  • 60
    • 0024279918 scopus 로고
    • A single amino acid determinant of the membrane localization of lipoproteins in e coli
    • Yamaguchi, K., F. Yu, and M. Inouye. 1988 A single amino acid determinant of the membrane localization of lipoproteins in E coli. Cell 53:423-432.
    • (1988) Cell , vol.53 , pp. 423-432
    • Yamaguchi, K.1    Yu, F.2    Inouye, M.3
  • 61
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains, nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985 Improved M13 phage cloning vectors and host strains, nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.