메뉴 건너뛰기




Volumn 180, Issue 7, 1998, Pages 1904-1912

An export-specific reporter designed for gram-positive bacteria: Application to Lactococcus lactis

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDOGLYCAN;

EID: 0031897112     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.7.1904-1912.1998     Document Type: Article
Times cited : (91)

References (69)
  • 1
    • 0028071361 scopus 로고
    • A conditional suicide system in Escherichia coli based on the intracellular degradation of DNA
    • Ahrenholtz, I., M. G. Lorenz, and W. Wackernagel. 1994. A conditional suicide system in Escherichia coli based on the intracellular degradation of DNA. Appl. Environ. Microhiol. 60:3746-3751.
    • (1994) Appl. Environ. Microhiol. , vol.60 , pp. 3746-3751
    • Ahrenholtz, I.1    Lorenz, M.G.2    Wackernagel, W.3
  • 2
    • 0029790464 scopus 로고    scopus 로고
    • Target cell specificity of a bacteriocin molecule: A C-terminal signal directs lysostaphin to the cell wall of Staphylococcus aureus
    • Baba, T., and O. Schneewind. 1996. Target cell specificity of a bacteriocin molecule: a C-terminal signal directs lysostaphin to the cell wall of Staphylococcus aureus. EMBO J. 15:4789-4797.
    • (1996) EMBO J. , vol.15 , pp. 4789-4797
    • Baba, T.1    Schneewind, O.2
  • 3
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J. C., K. McGovern, and J. Beckwith. 1991. Identification of a protein required for disulfide bond formation in vivo. Cell 67:581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 5
    • 0025053613 scopus 로고
    • β-Lactamase as a probe of membrane protein assembly and protein export
    • Broome-Smith, J. K., M. Tadayyon, and Y. Zhang. 1990. β-Lactamase as a probe of membrane protein assembly and protein export. Mol. Microbiol. 4:1637-1644.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1637-1644
    • Broome-Smith, J.K.1    Tadayyon, M.2    Zhang, Y.3
  • 6
    • 0028907622 scopus 로고
    • Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation
    • Buist, G., J. Kok, K. J. Leenhouts, M. Dabrowska, G. Venema, and A. J. Haandrikman. 1995. Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation. J. Bacteriol. 177:1554-1563.
    • (1995) J. Bacteriol. , vol.177 , pp. 1554-1563
    • Buist, G.1    Kok, J.2    Leenhouts, K.J.3    Dabrowska, M.4    Venema, G.5    Haandrikman, A.J.6
  • 7
    • 0019587523 scopus 로고
    • Synthetic sites for transcription termination and a functional comparison with tryptophan operon termination sites in vitro
    • Christie, G. E., P. J. Farnham, and T. Platt. 1981. Synthetic sites for transcription termination and a functional comparison with tryptophan operon termination sites in vitro. Proc. Natl. Acad. Sci. USA 78:4180-4184.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4180-4184
    • Christie, G.E.1    Farnham, P.J.2    Platt, T.3
  • 8
    • 0028872875 scopus 로고
    • Identification of mycoplasma membrane proteins by systematic TnphoA mutagenesis of a recombinant library
    • Cleavinger, C. M., M. F. Kim, J. H. Im, and K. S. Wise. 1995. Identification of mycoplasma membrane proteins by systematic TnphoA mutagenesis of a recombinant library. Mol. Microbiol. 18:283-293.
    • (1995) Mol. Microbiol. , vol.18 , pp. 283-293
    • Cleavinger, C.M.1    Kim, M.F.2    Im, J.H.3    Wise, K.S.4
  • 9
    • 0014198139 scopus 로고
    • Catalytic properties and specificity of the extracellular nuclease of Staphylococcus aureus
    • Cuatrecasas, P., S. Fuchs, and C. B. Anfinsen. 1967. Catalytic properties and specificity of the extracellular nuclease of Staphylococcus aureus. J. Biol. Chem. 242:1541-1547.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1541-1547
    • Cuatrecasas, P.1    Fuchs, S.2    Anfinsen, C.B.3
  • 10
    • 0025776579 scopus 로고
    • A sequence assembly and editing program for efficient management of large projects
    • Dear, S., and R. Staden. 1991. A sequence assembly and editing program for efficient management of large projects. Nucleic Acids Res. 19:3907-3911.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3907-3911
    • Dear, S.1    Staden, R.2
  • 11
    • 0020600404 scopus 로고
    • Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing
    • Gasson, M. J. 1983. Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing. J. Bacteriol. 154:1-9.
    • (1983) J. Bacteriol. , vol.154 , pp. 1-9
    • Gasson, M.J.1
  • 12
    • 0027216603 scopus 로고
    • Cloning of a chromosomal gene required for phage infection of Lactococcus lactis subsp. lactis C2
    • Geller, B. L., R. G. Ivey, J. E. Trempy, and B. Hettinger-Smith. 1993. Cloning of a chromosomal gene required for phage infection of Lactococcus lactis subsp. lactis C2. J. Bacteriol. 175:5510-5519.
    • (1993) J. Bacteriol. , vol.175 , pp. 5510-5519
    • Geller, B.L.1    Ivey, R.G.2    Trempy, J.E.3    Hettinger-Smith, B.4
  • 13
    • 0028291165 scopus 로고
    • The Lactococcus lactis sex-factor aggregation gene cluA
    • Godon, J. J., K. Jury, C. A. Shearman, and M. J. Gasson. 1994. The Lactococcus lactis sex-factor aggregation gene cluA. Mol. Microbiol. 12:655-663.
    • (1994) Mol. Microbiol. , vol.12 , pp. 655-663
    • Godon, J.J.1    Jury, K.2    Shearman, C.A.3    Gasson, M.J.4
  • 14
    • 0027062784 scopus 로고
    • FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli
    • Guzman, L. M., J. J. Barondess, and J. Beckwith. 1992. FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli. J. Bacteriol. 174:7716-7728.
    • (1992) J. Bacteriol. , vol.174 , pp. 7716-7728
    • Guzman, L.M.1    Barondess, J.J.2    Beckwith, J.3
  • 15
    • 0028179387 scopus 로고
    • The di- and tripeptide transport protein of Lactococcus lactis. A new type of bacterial peptide transporter
    • Hagting, A., E. R. Kunji, K. J. Leenhouts, B. Poolman, and W. N. Konings. 1994. The di- and tripeptide transport protein of Lactococcus lactis. A new type of bacterial peptide transporter. J. Biol. Chem. 269:11391-11399.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11391-11399
    • Hagting, A.1    Kunji, E.R.2    Leenhouts, K.J.3    Poolman, B.4    Konings, W.N.5
  • 16
    • 0011864425 scopus 로고
    • Fusions of secreted proteins to alkaline phosphatase: An approach for studying protein secretion
    • Hoffman, C. S., and A. Wright. 1985. Fusions of secreted proteins to alkaline phosphatase: an approach for studying protein secretion. Proc. Natl. Acad. Sci. USA 82:5107-5111.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5107-5111
    • Hoffman, C.S.1    Wright, A.2
  • 17
    • 0026700650 scopus 로고
    • Isolation and characterization of genetic expression and secretion signals from Enterococcus faecalis through the use of broad-host-range α-amylase probe vectors
    • Hols, P., A. Baulard, D. Garmyn, B. Delplace, S. Hogan, and J. Delcour. 1992. Isolation and characterization of genetic expression and secretion signals from Enterococcus faecalis through the use of broad-host-range α-amylase probe vectors. Gene 118:21-30.
    • (1992) Gene , vol.118 , pp. 21-30
    • Hols, P.1    Baulard, A.2    Garmyn, D.3    Delplace, B.4    Hogan, S.5    Delcour, J.6
  • 18
    • 0028265878 scopus 로고
    • Use of homologous expression-secretion signals and vector-free stable chromosomal integration in engineering of Lactobacillus plantarum for α-amylase and levanase expression
    • Hols, P., T. Ferain, D. Garmyn, N. Bernard, and J. Delcour. 1994. Use of homologous expression-secretion signals and vector-free stable chromosomal integration in engineering of Lactobacillus plantarum for α-amylase and levanase expression. Appl. Environ. Microbiol. 60:1401-1413.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1401-1413
    • Hols, P.1    Ferain, T.2    Garmyn, D.3    Bernard, N.4    Delcour, J.5
  • 19
    • 2642690908 scopus 로고    scopus 로고
    • Personal communication
    • Hols, P. Personal communication.
    • Hols, P.1
  • 20
    • 0028942303 scopus 로고
    • Cloning and characterization of the gene for a protein thioldisulfide oxidoreductase in Bacillus brevis
    • Ishihara, T., H. Tomita, V. Hasegawa, N. Tsukagoshi, H. Yamagata, and S. Udaka. 1995. Cloning and characterization of the gene for a protein thioldisulfide oxidoreductase in Bacillus brevis. J. Bacteriol. 177:745-749.
    • (1995) J. Bacteriol. , vol.177 , pp. 745-749
    • Ishihara, T.1    Tomita, H.2    Hasegawa, V.3    Tsukagoshi, N.4    Yamagata, H.5    Udaka, S.6
  • 21
    • 0027992299 scopus 로고
    • Cell surface protein receptors in oral streptococci
    • Jenkinson, H. F. 1994. Cell surface protein receptors in oral streptococci. FEMS Microbiol. Lett. 121:133-140.
    • (1994) FEMS Microbiol. Lett. , vol.121 , pp. 133-140
    • Jenkinson, H.F.1
  • 22
    • 0023088363 scopus 로고
    • Many random sequences functionally replace the secretion signal sequence of yeast invertase
    • Kaiser, C. A., D. Preuss, P. Grisafi, and D. Bolstein. 1987. Many random sequences functionally replace the secretion signal sequence of yeast invertase. Science 235:312-317.
    • (1987) Science , vol.235 , pp. 312-317
    • Kaiser, C.A.1    Preuss, D.2    Grisafi, P.3    Bolstein, D.4
  • 23
    • 0026567097 scopus 로고
    • Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme
    • Kamitani, S., Y. Akiyama, and K. Ho. 1992. Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme. EMBO J. 11:57-62.
    • (1992) EMBO J. , vol.11 , pp. 57-62
    • Kamitani, S.1    Akiyama, Y.2    Ho, K.3
  • 24
    • 0001763944 scopus 로고
    • Bioenergetics of lactic acid bacteria: Cytoplasmic pH and osmotolerance
    • Kashket, E. R. 1987. Bioenergetics of lactic acid bacteria: cytoplasmic pH and osmotolerance. FEMS Microbiol. Rev. 46:233-244.
    • (1987) FEMS Microbiol. Rev. , vol.46 , pp. 233-244
    • Kashket, E.R.1
  • 25
    • 0028318299 scopus 로고
    • Identification of bacterial cell-surface virulence determinants with TnphoA
    • Kaufman, M. R., and R. K. Taylor. 1994. Identification of bacterial cell-surface virulence determinants with TnphoA. Methods Enzymol. 235:426-448.
    • (1994) Methods Enzymol. , vol.235 , pp. 426-448
    • Kaufman, M.R.1    Taylor, R.K.2
  • 26
  • 27
    • 0025737510 scopus 로고
    • Nucleotide sequence of the secY gene from Lactococcus lactis and identification of conserved regions by comparison of four SecY proteins
    • Koivula, T., I. Palva, and H. Hemila. 1991. Nucleotide sequence of the secY gene from Lactococcus lactis and identification of conserved regions by comparison of four SecY proteins. FEBS Lett. 288:114-118.
    • (1991) FEBS Lett. , vol.288 , pp. 114-118
    • Koivula, T.1    Palva, I.2    Hemila, H.3
  • 28
    • 0021814043 scopus 로고
    • Secretion of staphylococcal nuclease by Bacillus subtilis
    • Kovacevic, S., L. E. Veal, H. M. Hsiung, and J. R. Miller. 1985. Secretion of staphylococcal nuclease by Bacillus subtilis. J. Bacteriol. 162:521-528.
    • (1985) J. Bacteriol. , vol.162 , pp. 521-528
    • Kovacevic, S.1    Veal, L.E.2    Hsiung, H.M.3    Miller, J.R.4
  • 29
    • 0015041802 scopus 로고
    • Metachromatic agar-diffusion methods for detecting staphylococcal nuclease activity
    • Lachica, R. V. F., C. Genigeorgis, and P. D. Hoeprich. 1971. Metachromatic agar-diffusion methods for detecting staphylococcal nuclease activity. Appl. Microbiol. 21:585-587.
    • (1971) Appl. Microbiol. , vol.21 , pp. 585-587
    • Lachica, R.V.F.1    Genigeorgis, C.2    Hoeprich, P.D.3
  • 30
    • 0027999002 scopus 로고
    • Direct screening of recombinants in gram-positive bacteria using the secreted staphylococcal nuclease as a reporter
    • Le Loir, Y., A. Gruss, S. D. Ehrlich, and P. Langella. 1994. Direct screening of recombinants in gram-positive bacteria using the secreted staphylococcal nuclease as a reporter. J. Bacteriol. 176:5135-5139.
    • (1994) J. Bacteriol. , vol.176 , pp. 5135-5139
    • Le Loir, Y.1    Gruss, A.2    Ehrlich, S.D.3    Langella, P.4
  • 31
    • 0031944982 scopus 로고    scopus 로고
    • A nine-residue synthetic propeptide enhances secretion efficiency of heterologous proteins in Lactococcus lactis
    • Le Loir, Y., A. Gruss, S. D. Ehrlich, and P. Langella. 1998. A nine-residue synthetic propeptide enhances secretion efficiency of heterologous proteins in Lactococcus lactis. J. Bacteriol. 180:1895-1903.
    • (1998) J. Bacteriol. , vol.180 , pp. 1895-1903
    • Le Loir, Y.1    Gruss, A.2    Ehrlich, S.D.3    Langella, P.4
  • 32
    • 0026553915 scopus 로고
    • Expression, secretion, and processing of staphylococcal nuclease by Corynebacterium glutamicum
    • Liebl, W., A. J. Sinskey, and K. H. Schleifer. 1992. Expression, secretion, and processing of staphylococcal nuclease by Corynebacterium glutamicum. J. Bacteriol. 174:1854-1861.
    • (1992) J. Bacteriol. , vol.174 , pp. 1854-1861
    • Liebl, W.1    Sinskey, A.J.2    Schleifer, K.H.3
  • 33
    • 0028833559 scopus 로고
    • Identification of Mycobacterium tuberculosis DNA sequences encoding exported proteins by using phoA gene fusions
    • Lim, E. M., J. Rauzier, J. Timm, G. Torrea, A. Murray, B. Gicquel, and D. Portnoi. 1995. Identification of Mycobacterium tuberculosis DNA sequences encoding exported proteins by using phoA gene fusions. J. Bacteriol. 177: 59-65.
    • (1995) J. Bacteriol. , vol.177 , pp. 59-65
    • Lim, E.M.1    Rauzier, J.2    Timm, J.3    Torrea, G.4    Murray, A.5    Gicquel, B.6    Portnoi, D.7
  • 34
    • 0024404941 scopus 로고
    • Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein
    • Liu, G., T. B. Topping, and L. L. Randall. 1989. Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein. Proc. Natl. Acad. Sci. USA 86:9213-9217.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9213-9217
    • Liu, G.1    Topping, T.B.2    Randall, L.L.3
  • 35
    • 2642621792 scopus 로고    scopus 로고
    • Personal communication
    • Maguin, E., and P. Duwat. Personal communication.
    • Maguin, E.1    Duwat, P.2
  • 36
    • 0025095225 scopus 로고
    • Alkaline phosphatase fusions: Sensors of subcellular location
    • Manoil, C., J. J. Mekalanos, and J. Beckwith. 1990. Alkaline phosphatase fusions: sensors of subcellular location. J. Bacteriol. 172:515-518.
    • (1990) J. Bacteriol. , vol.172 , pp. 515-518
    • Manoil, C.1    Mekalanos, J.J.2    Beckwith, J.3
  • 37
    • 0000632797 scopus 로고
    • TnphoA: A transposon probe for protein export signals
    • Manoil, C., and J. Beckwith. 1985. TnphoA: a transposon probe for protein export signals. Proc. Natl. Acad. Sci. USA 82:8129-8133.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8129-8133
    • Manoil, C.1    Beckwith, J.2
  • 38
    • 0025083165 scopus 로고
    • Applications for biotechnology: Present and future improvements in lactic acid bacteria
    • McKay, L. L., and K. A. Baldwin. 1990. Applications for biotechnology: present and future improvements in lactic acid bacteria. FEMS Microbiol. Rev. 7:3-14.
    • (1990) FEMS Microbiol. Rev. , vol.7 , pp. 3-14
    • McKay, L.L.1    Baldwin, K.A.2
  • 39
    • 0023393604 scopus 로고
    • Secretion and processing of staphylococcal nuclease by Bacillus subtilis
    • Miller, J. R., S. Kovacevic, and L. E. Veal. 1987. Secretion and processing of staphylococcal nuclease by Bacillus subtilis. J. Bacteriol. 169:3508-3514.
    • (1987) J. Bacteriol. , vol.169 , pp. 3508-3514
    • Miller, J.R.1    Kovacevic, S.2    Veal, L.E.3
  • 41
    • 0030614959 scopus 로고    scopus 로고
    • Identification of procaryotic and eucaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., J. Engelbrecht, S. Brunak, and G. von Heijne. 1997. Identification of procaryotic and eucaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 42
    • 0028135021 scopus 로고
    • A Lactococcus lactis gene encodes a membrane protein with putative ATPase activity that is homologous to the essential Escherichia coli ftsH gene product
    • Nilsson, D., A. A. Lauridsen, T. Tomoyasu, and T. Ogura. 1994. A Lactococcus lactis gene encodes a membrane protein with putative ATPase activity that is homologous to the essential Escherichia coli ftsH gene product. Microbiology 140:2601-2610.
    • (1994) Microbiology , vol.140 , pp. 2601-2610
    • Nilsson, D.1    Lauridsen, A.A.2    Tomoyasu, T.3    Ogura, T.4
  • 44
    • 0027219646 scopus 로고
    • Genetic identification of exported proteins in Streptococcus pneumoniae
    • Pearce, B. J., Y. B. Yin, and H. R. Masure. 1993. Genetic identification of exported proteins in Streptococcus pneumoniae. Mol. Microbiol. 9:1037-1050.
    • (1993) Mol. Microbiol. , vol.9 , pp. 1037-1050
    • Pearce, B.J.1    Yin, Y.B.2    Masure, H.R.3
  • 46
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A. P. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 47
    • 0026289515 scopus 로고
    • Initiation of translation at AUC, AUA and AUU codons in Escherichia coli
    • Romero, A., and P. Garcia. 1991. Initiation of translation at AUC, AUA and AUU codons in Escherichia coli. FEMS Microbiol. Lett. 68:325-330.
    • (1991) FEMS Microbiol. Lett. , vol.68 , pp. 325-330
    • Romero, A.1    Garcia, P.2
  • 48
    • 0028902788 scopus 로고
    • Transmembrane helices predicted at 95% accuracy
    • Rost, B., R. Casadio, P. Fariselli, and C. Sander. 1995. Transmembrane helices predicted at 95% accuracy. Protein Sci. 4:521-533.
    • (1995) Protein Sci. , vol.4 , pp. 521-533
    • Rost, B.1    Casadio, R.2    Fariselli, P.3    Sander, C.4
  • 51
    • 0027442464 scopus 로고
    • Cell wall sorting signals in surface proteins of gram-positive bacteria
    • Schneewind, O., D. Mihaylova Petkov, and P. Model. 1993. Cell wall sorting signals in surface proteins of gram-positive bacteria. EMBO J. 12:4803-4811.
    • (1993) EMBO J. , vol.12 , pp. 4803-4811
    • Schneewind, O.1    Mihaylova Petkov, D.2    Model, P.3
  • 52
    • 0020583027 scopus 로고
    • A genetic system for analysis of staphylococcal nuclease
    • Shortle, D. 1983. A genetic system for analysis of staphylococcal nuclease. Gene 22:181-189.
    • (1983) Gene , vol.22 , pp. 181-189
    • Shortle, D.1
  • 53
    • 0026022091 scopus 로고
    • Secretion of TEM β-lactamase with signal sequences isolated from the chromosome of Lactococcus lactis subsp. lactis
    • Sibakov, M., T. Koivula, A. von Wright, and I. Palva. 1991. Secretion of TEM β-lactamase with signal sequences isolated from the chromosome of Lactococcus lactis subsp. lactis. Appl. Environ. Microbiol. 57:341-348.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 341-348
    • Sibakov, M.1    Koivula, T.2    Von Wright, A.3    Palva, I.4
  • 54
    • 0023992075 scopus 로고
    • Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis
    • Simon, D., and A. Chopin. 1988. Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis. Biochimie 70:559-566.
    • (1988) Biochimie , vol.70 , pp. 559-566
    • Simon, D.1    Chopin, A.2
  • 55
    • 0027401020 scopus 로고
    • Protein secretion in Bacillus species
    • Simonen, M., and I. Palva. 1993. Protein secretion in Bacillus species. Microbiol. Rev. 57:109-137.
    • (1993) Microbiol. Rev. , vol.57 , pp. 109-137
    • Simonen, M.1    Palva, I.2
  • 56
    • 0023191360 scopus 로고
    • Construction and use of signal sequence selection vectors in Escherichia coli and Bacillus subtilis
    • Smith, H., S. Bron, J. Van Ee, and G. Venema. 1987. Construction and use of signal sequence selection vectors in Escherichia coli and Bacillus subtilis. J. Bacteriol. 169:3321-3328.
    • (1987) J. Bacteriol. , vol.169 , pp. 3321-3328
    • Smith, H.1    Bron, S.2    Van Ee, J.3    Venema, G.4
  • 57
    • 0023823396 scopus 로고
    • Characterization of signal-sequence-coding regions selected from the Bacillus subtilis chromosome
    • Smith, H., A. de Jong, S. Bron, and G. Venema. 1988. Characterization of signal-sequence-coding regions selected from the Bacillus subtilis chromosome. Gene 70:351-361.
    • (1988) Gene , vol.70 , pp. 351-361
    • Smith, H.1    De Jong, A.2    Bron, S.3    Venema, G.4
  • 58
  • 59
    • 0028983021 scopus 로고
    • β-Galactosidase is inactivated by intermolecular disulfide bonds and is toxic when secreted to the periplasm of Escherichia coli
    • Snyder, W. B., and T. J. Silhavy. 1995. β-Galactosidase is inactivated by intermolecular disulfide bonds and is toxic when secreted to the periplasm of Escherichia coli. J. Bacteriol. 177:953-963.
    • (1995) J. Bacteriol. , vol.177 , pp. 953-963
    • Snyder, W.B.1    Silhavy, T.J.2
  • 60
    • 0030055788 scopus 로고    scopus 로고
    • The 19-residue pro-peptide of staphylococcal nuclease has a profound secretion-enhancing ability in Escherichia coli
    • Suciu, D., and M. Inouye. 1996. The 19-residue pro-peptide of staphylococcal nuclease has a profound secretion-enhancing ability in Escherichia coli. Mol. Microbiol. 21:181-195.
    • (1996) Mol. Microbiol. , vol.21 , pp. 181-195
    • Suciu, D.1    Inouye, M.2
  • 61
    • 0016686551 scopus 로고
    • Improved medium for lactic streptococci and their bacteriophages
    • Terzaghi, B. E., and W. E. Sandine. 1975. Improved medium for lactic streptococci and their bacteriophages. Appl. Environ. Microbiol. 29:807-813.
    • (1975) Appl. Environ. Microbiol. , vol.29 , pp. 807-813
    • Terzaghi, B.E.1    Sandine, W.E.2
  • 62
    • 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
  • 63
    • 0025252546 scopus 로고
    • Cloning of usp45, a gene encoding a secreted protein from Lactococcus lactis subsp. lactis MG1363
    • van Asseldonk, M., G. Rutten, M. Oteman, R. J. Siezen, W. M. de Vos, and G. Simons. 1990. Cloning of usp45, a gene encoding a secreted protein from Lactococcus lactis subsp. lactis MG1363. Gene 95:155-160.
    • (1990) Gene , vol.95 , pp. 155-160
    • Van Asseldonk, M.1    Rutten, G.2    Oteman, M.3    Siezen, R.J.4    De Vos, W.M.5    Simons, G.6
  • 65
    • 0023928974 scopus 로고
    • Transcending the impenetrable: How proteins come to terms with membranes
    • von Heijne, G. 1988. Transcending the impenetrable: how proteins come to terms with membranes. Biochim. Biophys. Acta 947:307-333.
    • (1988) Biochim. Biophys. Acta , vol.947 , pp. 307-333
    • Von Heijne, G.1
  • 66
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne, G. 1989. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341:456-458.
    • (1989) Nature , vol.341 , pp. 456-458
    • Von Heijne, G.1
  • 67
    • 0024571667 scopus 로고
    • Species-specific variation in signal peptide design. Implications for protein secretion in foreign hosts
    • von Heijne, G., and L. Abrahmsen. 1989. Species-specific variation in signal peptide design. Implications for protein secretion in foreign hosts. FEBS Lett. 244:439-446.
    • (1989) FEBS Lett. , vol.244 , pp. 439-446
    • Von Heijne, G.1    Abrahmsen, L.2
  • 68
    • 0026012975 scopus 로고
    • Analysis of the membrane organization of an Escherichia coli protein translocator, HlyB, a member of a large family of procaryote and eucaryote surface transport protein
    • Wang, R. C., S. J. Seror, M. Blight, J. M. Pratt, J. K. Broome-Smith, and I. B. Holland. 1991. Analysis of the membrane organization of an Escherichia coli protein translocator, HlyB, a member of a large family of procaryote and eucaryote surface transport protein. J. Mol. Biol. 217:441-454.
    • (1991) J. Mol. Biol. , vol.217 , pp. 441-454
    • Wang, R.C.1    Seror, S.J.2    Blight, M.3    Pratt, J.M.4    Broome-Smith, J.K.5    Holland, I.B.6
  • 69
    • 0024407606 scopus 로고
    • Identification of amino acid sequences that can function as translocators of β-lactamase in Escherichia coli
    • Zhang, Y., and J. K. Broome-Smith. 1989. Identification of amino acid sequences that can function as translocators of β-lactamase in Escherichia coli. Mol. Microbiol. 3:1361-1369.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1361-1369
    • Zhang, Y.1    Broome-Smith, J.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.