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Volumn 251, Issue 2, 2000, Pages 187-197

Use of the arabinose p(bad) promoter for tightly regulated display of proteins on bacteriophage

Author keywords

Filamentous phage; Gene III; Gene VIII; Phagemid

Indexed keywords

ARABINOSE; BETA LACTAMASE; HYBRID PROTEIN; PROTEIN;

EID: 0034720872     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(00)00210-9     Document Type: Article
Times cited : (16)

References (37)
  • 1
    • 0021019879 scopus 로고
    • Vectors bearing a hybrid trp-lac promoter useful for regulated expression of cloned genes in Escherichia coli
    • Amann E., Brosius J., Ptashne M. Vectors bearing a hybrid trp-lac promoter useful for regulated expression of cloned genes in Escherichia coli. Gene. 25:1983;167-178.
    • (1983) Gene , vol.25 , pp. 167-178
    • Amann, E.1    Brosius, J.2    Ptashne, M.3
  • 2
    • 0025838021 scopus 로고
    • Assembly of combinatorial antibody libraries on phage surfaces, the gene III site
    • Barbas C.F. III, Kang A.S., Lerner R.A., Benkovic S.J. Assembly of combinatorial antibody libraries on phage surfaces, the gene III site. Proc. Natl. Acad. Sci. USA. 88:1991;7978-7982.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7978-7982
    • Barbas C.F. III1    Kang, A.S.2    Lerner, R.A.3    Benkovic, S.J.4
  • 3
    • 0033522202 scopus 로고    scopus 로고
    • A phagemid vector using the E. coli phage shock promoter facilitates phage display of toxic proteins
    • Beekwilder J., Rakonjac J., Jongsma M., Bosch D. A phagemid vector using the E. coli phage shock promoter facilitates phage display of toxic proteins. Gene. 228:1999;23-31.
    • (1999) Gene , vol.228 , pp. 23-31
    • Beekwilder, J.1    Rakonjac, J.2    Jongsma, M.3    Bosch, D.4
  • 4
    • 0000182975 scopus 로고
    • XL1-Blue, a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection
    • Bullock W.O., Fernandez J.M., Short J.M. XL1-Blue, a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. BioTechniques. 5:1987;376-379.
    • (1987) BioTechniques , vol.5 , pp. 376-379
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 5
    • 0021760283 scopus 로고
    • Two improved promoter sequences for the β-lactamase expression arising from a single base-pair substitution
    • Chen S.T., Clowes R.C. Two improved promoter sequences for the β-lactamase expression arising from a single base-pair substitution. Nucleic Acids Res. 12:1984;3219-3234.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 3219-3234
    • Chen, S.T.1    Clowes, R.C.2
  • 7
    • 0028153049 scopus 로고
    • Display of expression products of cDNA libraries on phage surfaces
    • Crameri R., Jaussi R., Menz G., Blaser K. Display of expression products of cDNA libraries on phage surfaces. Eur. J. Biochem. 226:1994;53-58.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 53-58
    • Crameri, R.1    Jaussi, R.2    Menz, G.3    Blaser, K.4
  • 8
    • 0025254304 scopus 로고
    • Regulated expression of foreign genes fused to lac, control by glucose level in growth medium
    • DeBellis D., Schwartz I. Regulated expression of foreign genes fused to lac, control by glucose level in growth medium. Nucleic Acids Res. 18:1990;1311.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1311
    • Debellis, D.1    Schwartz, I.2
  • 9
    • 0028180282 scopus 로고
    • Rapid simultaneous screening for DNA integrity and antigen specificity of clones selected by phage display
    • Fischer P., Leu S.-J.C., Yang Y.-Y., Chen P.P. Rapid simultaneous screening for DNA integrity and antigen specificity of clones selected by phage display. Biotechniques. 16:1994;828-830.
    • (1994) Biotechniques , vol.16 , pp. 828-830
    • Fischer, P.1    Leu, S.-J.C.2    Yang, Y.-Y.3    Chen, P.P.4
  • 11
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene. 77:1989;51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 12
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage, methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom H.R., Griffiths A.D., Johnson K.S., Chiswell D.J., Hudson P., Winter G. Multi-subunit proteins on the surface of filamentous phage, methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res. 19:1991;4133-4137.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5    Winter, G.6
  • 13
    • 0029962946 scopus 로고    scopus 로고
    • Amino acid sequence determinants of β-lactamase structure and activity
    • Huang W., Petrosino J., Hirsch M., Shenkin P.S., Palzkill T. Amino acid sequence determinants of β-lactamase structure and activity. J. Mol. Biol. 258:1996;688-703.
    • (1996) J. Mol. Biol. , vol.258 , pp. 688-703
    • Huang, W.1    Petrosino, J.2    Hirsch, M.3    Shenkin, P.S.4    Palzkill, T.5
  • 14
    • 0030788941 scopus 로고    scopus 로고
    • A natural polymorphism in β-lactamase is a global suppressor
    • Huang W., Palzkill T. A natural polymorphism in β-lactamase is a global suppressor. Proc. Natl. Acad. Sci. USA. 94:1997;8801-8806.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8801-8806
    • Huang, W.1    Palzkill, T.2
  • 15
    • 0031724013 scopus 로고    scopus 로고
    • Display of functional β-lactamase inihibitory protein on the surface of M13 bacteriophage
    • Huang W., Petrosino J., Palzkill T. Display of functional β-lactamase inihibitory protein on the surface of M13 bacteriophage. Antimicrob. Agents Chemother. 42:1998;2893-2897.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2893-2897
    • Huang, W.1    Petrosino, J.2    Palzkill, T.3
  • 16
    • 0029170325 scopus 로고
    • Cloning of ligand-binding domains of bacterial receptors by phage display
    • Jacobsson K., Frykberg L. Cloning of ligand-binding domains of bacterial receptors by phage display. BioTechniques. 18:1995;878-885.
    • (1995) BioTechniques , vol.18 , pp. 878-885
    • Jacobsson, K.1    Frykberg, L.2
  • 17
    • 0029989081 scopus 로고    scopus 로고
    • Phage display shot gun cloning of ligand-binding domains of prokaryotic receptors approaches 100% correct clones
    • Jacobsson K., Frykberg L. Phage display shot gun cloning of ligand-binding domains of prokaryotic receptors approaches 100% correct clones. BioTechniques. 20:1996;1070-1080.
    • (1996) BioTechniques , vol.20 , pp. 1070-1080
    • Jacobsson, K.1    Frykberg, L.2
  • 18
    • 0029032444 scopus 로고
    • In vivo induction kinetics of the arabinose promoters in Escherichia coli
    • Johnson C.M., Schleif R.F. In vivo induction kinetics of the arabinose promoters in Escherichia coli. J. Bacteriol. 177:1995;3438-3442.
    • (1995) J. Bacteriol. , vol.177 , pp. 3438-3442
    • Johnson, C.M.1    Schleif, R.F.2
  • 19
    • 0030608365 scopus 로고    scopus 로고
    • Inclusion of an upstream transcriptional terminator in phage display vectors abolishes background expression of toxic fusions with coat protein g3p
    • Krebber A., Burmester J., Pluckthun A. Inclusion of an upstream transcriptional terminator in phage display vectors abolishes background expression of toxic fusions with coat protein g3p. Gene. 178:1996;71-74.
    • (1996) Gene , vol.178 , pp. 71-74
    • Krebber, A.1    Burmester, J.2    Pluckthun, A.3
  • 20
    • 0025776763 scopus 로고
    • Gly-238-Ser substitution changes the substrate specificity of the SHV class A β-lactamases
    • Lee K.Y., Hopkins J.D., O'Brien T.F., Syvanen M. Gly-238-Ser substitution changes the substrate specificity of the SHV class A β-lactamases. Prot., Struct., Func. Genet. 11:1991;45-51.
    • (1991) Prot., Struct., Func. Genet. , vol.11 , pp. 45-51
    • Lee, K.Y.1    Hopkins, J.D.2    O'Brien, T.F.3    Syvanen, M.4
  • 21
    • 0026446168 scopus 로고
    • High copy number of the pUC plasmid results from a Rom/Rop suppressible point mutation in RNA II. Mol
    • Lin-Chao S., Chen W.T., Wong T.-T. High copy number of the pUC plasmid results from a Rom/Rop suppressible point mutation in RNA II. Mol. Microbiology. 6:1992;3385-3393.
    • (1992) Microbiology , vol.6 , pp. 3385-3393
    • Lin-Chao, S.1    Chen, W.T.2    Wong, T.-T.3
  • 22
    • 0025202249 scopus 로고
    • DNA looping and unlooping by AraC protein
    • Lobell R.B., Schleif R.F. DNA looping and unlooping by AraC protein. Science. 250:1990;528-532.
    • (1990) Science , vol.250 , pp. 528-532
    • Lobell, R.B.1    Schleif, R.F.2
  • 23
    • 0026343486 scopus 로고
    • Selecting high-affinity binding proteins by monovalent phage display
    • Lowman H.B., Bass S.H., Simpson N., Wells J.A. Selecting high-affinity binding proteins by monovalent phage display. Biochemistry. 30:1991;10832-10838.
    • (1991) Biochemistry , vol.30 , pp. 10832-10838
    • Lowman, H.B.1    Bass, S.H.2    Simpson, N.3    Wells, J.A.4
  • 24
    • 0030570513 scopus 로고    scopus 로고
    • Role of capsid structure and membrane protein processing in determining the size and copy number of peptides displayed on the major coat protein of filamentous bacteriophage
    • Malik P., Terry T.D., Gowda L.R., Langara A., Petukhov S.A., Symmons M.F., Welsh L.C., Marvin D.A., Perham R.N. Role of capsid structure and membrane protein processing in determining the size and copy number of peptides displayed on the major coat protein of filamentous bacteriophage. J. Mol. Biol. 260:1996;9-21.
    • (1996) J. Mol. Biol. , vol.260 , pp. 9-21
    • Malik, P.1    Terry, T.D.2    Gowda, L.R.3    Langara, A.4    Petukhov, S.A.5    Symmons, M.F.6    Welsh, L.C.7    Marvin, D.A.8    Perham, R.N.9
  • 25
    • 0025720555 scopus 로고
    • Design, construction and function of a multicopy display vector using fusions to the major coat protein of bacteriophage M13
    • Markland W., Roberts B.L., Saxena M.J., Guterman S.K., Ladner R.C. Design, construction and function of a multicopy display vector using fusions to the major coat protein of bacteriophage M13. Gene. 109:1991;13-19.
    • (1991) Gene , vol.109 , pp. 13-19
    • Markland, W.1    Roberts, B.L.2    Saxena, M.J.3    Guterman, S.K.4    Ladner, R.C.5
  • 26
    • 0020583709 scopus 로고
    • Effects of surrounding sequence on the suppression of nonsense codons
    • Miller J.H., Albertini A.M. Effects of surrounding sequence on the suppression of nonsense codons. J. Mol. Biol. 164:1983;59-71.
    • (1983) J. Mol. Biol. , vol.164 , pp. 59-71
    • Miller, J.H.1    Albertini, A.M.2
  • 27
    • 0021469101 scopus 로고
    • Regulation of the araC gene of Escherichia coli, catabolite repression, autoregulation and effect on araBAD expression
    • Miyada C.G., Stoltzfus L., Wilcox G. Regulation of the araC gene of Escherichia coli, catabolite repression, autoregulation and effect on araBAD expression. Proc. Natl. Acad. Sci. USA. 81:1984;4120-4124.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4120-4124
    • Miyada, C.G.1    Stoltzfus, L.2    Wilcox, G.3
  • 28
    • 0028200978 scopus 로고
    • Evolution of antibiotic resistance, several different amino acid substitutions in an active site loop alter the substrate profile of β-lactamase
    • Palzkill T., Le Q.Q., Venkatachalam K.V., LaRocco M., Ocera H. Evolution of antibiotic resistance, several different amino acid substitutions in an active site loop alter the substrate profile of β-lactamase. Mol. Microbiol. 12:1994;217-229.
    • (1994) Mol. Microbiol. , vol.12 , pp. 217-229
    • Palzkill, T.1    Le, Q.Q.2    Venkatachalam, K.V.3    Larocco, M.4    Ocera, H.5
  • 29
    • 0032500769 scopus 로고    scopus 로고
    • Mapping protein-ligand interactions using whole genome phage display libraries
    • Palzkill T., Huang W., Weinstock G.M. Mapping protein-ligand interactions using whole genome phage display libraries. Gene. 221:1998;79-83.
    • (1998) Gene , vol.221 , pp. 79-83
    • Palzkill, T.1    Huang, W.2    Weinstock, G.M.3
  • 30
    • 0015153419 scopus 로고
    • Glucose and the metabolism of adenosine 3′,5′-cyclic monophosphate in Escherichia coli
    • Peterkofsky A., Gazdar C. Glucose and the metabolism of adenosine 3′,5′-cyclic monophosphate in Escherichia coli. Proc. Natl. Acad. Sci. USA. 68:1971;2794-2798.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2794-2798
    • Peterkofsky, A.1    Gazdar, C.2
  • 31
    • 0022969124 scopus 로고
    • Ff coliphages, structural and functional relationships
    • Rasched I., Oberer E. Ff coliphages, structural and functional relationships. Microbiol. Rev. 50:1986;401-427.
    • (1986) Microbiol. Rev. , vol.50 , pp. 401-427
    • Rasched, I.1    Oberer, E.2
  • 32
    • 0028874645 scopus 로고
    • A human pancreatic secretory trypsin inhibitor presenting a hypervarible highly constrained epitope via monovalent phagemid display
    • Röttgen P., Collins J. A human pancreatic secretory trypsin inhibitor presenting a hypervarible highly constrained epitope via monovalent phagemid display. Gene. 164:1995;243-250.
    • (1995) Gene , vol.164 , pp. 243-250
    • Röttgen, P.1    Collins, J.2
  • 33
    • 0033548429 scopus 로고    scopus 로고
    • Identification of residues in β-lactamase critical for binding β-lactamase inhibitory protein
    • Rudgers G.W., Palzkill T. Identification of residues in β-lactamase critical for binding β-lactamase inhibitory protein. J. Biol. Chem. 274:1999;6963-6971.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6963-6971
    • Rudgers, G.W.1    Palzkill, T.2
  • 35
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F.W., Moffatt B.A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:1986;113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 36
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier F.W. Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J. Mol. Biol. 219:1991;37-44.
    • (1991) J. Mol. Biol. , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 37
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains, nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains, nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 33:1985;103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


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