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Volumn 70, Issue 1, 2006, Pages 119-125

Construction of a positive selection marker by a lethal gene with the amber stop codon(s) regulator

Author keywords

Amber stop codon; C terminal ribonuclease domain (CRD); Colicin E3; Positive selection; Suppressor activity

Indexed keywords

DNA; ENCODING (SYMBOLS); ESCHERICHIA COLI; TOXICITY; VECTORS;

EID: 31444457034     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70.119     Document Type: Article
Times cited : (3)

References (38)
  • 1
    • 0026728290 scopus 로고
    • Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes
    • Bernard, P., and Couturier, M., Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes. J. Mol. Biol., 226, 735-745 (1992).
    • (1992) J. Mol. Biol. , vol.226 , pp. 735-745
    • Bernard, P.1    Couturier, M.2
  • 2
    • 0028006860 scopus 로고
    • Positive-selection vectors using the F plasmid ccdB killer gene
    • Bernard, P., Gabant, P., Bahassi, E. M., and Couturier, M., Positive-selection vectors using the F plasmid ccdB killer gene. Gene, 148, 71-74 (1994).
    • (1994) Gene , vol.148 , pp. 71-74
    • Bernard, P.1    Gabant, P.2    Bahassi, E.M.3    Couturier, M.4
  • 3
    • 0025761119 scopus 로고
    • The 41 carboxy-terminal residues of the miniF plasmid CcdA protein are sufficient to antagonize the killer activity of the CcdB protein
    • Bernard, P., and Couturier, M., The 41 carboxy-terminal residues of the miniF plasmid CcdA protein are sufficient to antagonize the killer activity of the CcdB protein. Mol. Gen. Genet., 226, 297-304 (1991).
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 297-304
    • Bernard, P.1    Couturier, M.2
  • 5
    • 0015188985 scopus 로고
    • Specific inactivation of ribosomes by colicin E3 in vitro and mechanism of immunity in colicinogenic cells
    • Bowman, C. M., Sidikaro, J., and Nomura, M., Specific inactivation of ribosomes by colicin E3 in vitro and mechanism of immunity in colicinogenic cells. Nat. New Biol., 234, 133-137 (1971).
    • (1971) Nat. New Biol. , vol.234 , pp. 133-137
    • Bowman, C.M.1    Sidikaro, J.2    Nomura, M.3
  • 7
    • 0018110316 scopus 로고
    • Colicin E3 is an endonuclease
    • Tokyo
    • Ohno, S., and Imahori, K., Colicin E3 is an endonuclease. J. Biochem. (Tokyo), 84, 1637-1640 (1978).
    • (1978) J. Biochem. , vol.84 , pp. 1637-1640
    • Ohno, S.1    Imahori, K.2
  • 8
    • 0015056478 scopus 로고
    • Effect of colicin E3 upon the 30S ribosomal subunit of Escherichia coli
    • Senior, B. W., and Holland, I. B., Effect of colicin E3 upon the 30S ribosomal subunit of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A., 68, 959-963 (1971).
    • (1971) Proc. Natl. Acad. Sci. U.S.A. , vol.68 , pp. 959-963
    • Senior, B.W.1    Holland, I.B.2
  • 9
    • 0015132507 scopus 로고
    • Inactivation of ribosomes in vitro by colicin E 3
    • Boon, T., Inactivation of ribosomes in vitro by colicin E 3. Proc. Natl. Acad. Sci. U.S.A., 68, 2421-2425 (1971).
    • (1971) Proc. Natl. Acad. Sci. U.S.A. , vol.68 , pp. 2421-2425
    • Boon, T.1
  • 10
    • 0002241966 scopus 로고
    • eds. Cohen, P., and Van Heyningen, S., Elsevier Biomedical Press
    • Jakes, K., "Molecular Action of Toxins and Viruses", eds. Cohen, P., and Van Heyningen, S., Elsevier Biomedical Press, pp. 131-167 (1982).
    • (1982) Molecular Action of Toxins and Viruses , pp. 131-167
    • Jakes, K.1
  • 11
    • 0020350235 scopus 로고
    • Colicins and other bacteriocins with established modes of action
    • Konisky, J., Colicins and other bacteriocins with established modes of action. Annu. Rev. Microbiol., 36, 125-144 (1982).
    • (1982) Annu. Rev. Microbiol. , vol.36 , pp. 125-144
    • Konisky, J.1
  • 12
    • 0021771497 scopus 로고
    • Comparative nucleotide sequences encoding the immunity proteins and the carboxyl-terminal peptides of colicins E2 and E3
    • Lau, P. C., Rowsome, R. W., Zuker, M., and Visentin, L. P., Comparative nucleotide sequences encoding the immunity proteins and the carboxyl-terminal peptides of colicins E2 and E3. Nucl. Acids Res., 12, 8733-8745 (1984).
    • (1984) Nucl. Acids Res. , vol.12 , pp. 8733-8745
    • Lau, P.C.1    Rowsome, R.W.2    Zuker, M.3    Visentin, L.P.4
  • 13
    • 0020419707 scopus 로고
    • A plasmid region encoding the active fragment and the inhibitor protein of colicin E3 - CA38
    • Masaki, H., and Ohta, T., A plasmid region encoding the active fragment and the inhibitor protein of colicin E3 - CA38. FEBS Lett., 149, 129-132 (1982).
    • (1982) FEBS Lett. , vol.149 , pp. 129-132
    • Masaki, H.1    Ohta, T.2
  • 14
    • 0021100937 scopus 로고
    • Nucleotide sequence for the catalytic domain of colicin E3 and its immunity protein: Evidence for a third gene overlapping colicin
    • Mock, M., Miyada, C. G., and Gunsalus, R. P., Nucleotide sequence for the catalytic domain of colicin E3 and its immunity protein: evidence for a third gene overlapping colicin. Nucl. Acids Res., 11, 3547-3557 (1983).
    • (1983) Nucl. Acids Res. , vol.11 , pp. 3547-3557
    • Mock, M.1    Miyada, C.G.2    Gunsalus, R.P.3
  • 15
    • 0015952441 scopus 로고
    • Purification and properties of colicin E3 immunity protein
    • Jakes, K., Zinder, N. D., and Boon, T., Purification and properties of colicin E3 immunity protein. J. Biol. Chem., 249, 438-444 (1974).
    • (1974) J. Biol. Chem. , vol.249 , pp. 438-444
    • Jakes, K.1    Zinder, N.D.2    Boon, T.3
  • 16
    • 0002241966 scopus 로고
    • The mechanism of action of colicin E2, colicin E3 and cloacin DF13
    • eds. Cohen, P., and Van Heyningen, S., Elesevier, Amsterdam
    • Jakes, K. S., The mechanism of action of colicin E2, colicin E3 and cloacin DF13. In "Action of Toxins and Viruses", eds. Cohen, P., and Van Heyningen, S., Elesevier, Amsterdam, pp. 131-167 (1982).
    • (1982) Action of Toxins and Viruses , pp. 131-167
    • Jakes, K.S.1
  • 17
    • 0012852996 scopus 로고
    • Highly purified colicin E3 contains immunity protein
    • Jakes, K. S., and Zinder, N. D., Highly purified colicin E3 contains immunity protein. Proc. Natl. Acad. Sci. U.S.A., 71, 3380-3384 (1974).
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 3380-3384
    • Jakes, K.S.1    Zinder, N.D.2
  • 18
    • 0022429251 scopus 로고
    • Colicin E3 and its immunity genes
    • Masaki, H., and Ohta, T., Colicin E3 and its immunity genes. J. Mol. Biol., 182, 217-227 (1985).
    • (1985) J. Mol. Biol. , vol.182 , pp. 217-227
    • Masaki, H.1    Ohta, T.2
  • 19
    • 0019561097 scopus 로고
    • Amino acid sequence of immunity protein (B subunit) of colicin E3
    • Tokyo
    • Mochitate, K., Suzuki, K., and Imahori, K., Amino acid sequence of immunity protein (B subunit) of colicin E3. J. Biochem. (Tokyo), 89, 1609-1618 (1981).
    • (1981) J. Biochem. , vol.89 , pp. 1609-1618
    • Mochitate, K.1    Suzuki, K.2    Imahori, K.3
  • 20
    • 0017712149 scopus 로고
    • Purification and characterization of active component and active fragment of colicin E3
    • Tokyo
    • Ohno, S., Ohno-Iwashita, Y., Suzuki, K., and Imahori, K., Purification and characterization of active component and active fragment of colicin E3. J. Biochem. (Tokyo), 82, 1045-1053 (1977).
    • (1977) J. Biochem. , vol.82 , pp. 1045-1053
    • Ohno, S.1    Ohno-Iwashita, Y.2    Suzuki, K.3    Imahori, K.4
  • 21
    • 0018883387 scopus 로고
    • Assignment of the functional loci in colicin E2 and E3 molecules by the characterization of their proteolytic fragments
    • Ohno-Iwashita, Y., and Imahori, K., Assignment of the functional loci in colicin E2 and E3 molecules by the characterization of their proteolytic fragments. Biochemistry, 19, 652-659 (1980).
    • (1980) Biochemistry , vol.19 , pp. 652-659
    • Ohno-Iwashita, Y.1    Imahori, K.2
  • 22
    • 0018821830 scopus 로고
    • Studies on the physicochemical structure and stability of an active fragment (T2A) of colicin E3
    • Tokyo
    • Suzuki, K., Ohno, S., and Imahori, K., Studies on the physicochemical structure and stability of an active fragment (T2A) of colicin E3. J. Biochem. (Tokyo), 87, 761-769 (1980).
    • (1980) J. Biochem. , vol.87 , pp. 761-769
    • Suzuki, K.1    Ohno, S.2    Imahori, K.3
  • 23
    • 0018178854 scopus 로고
    • Preparation and characterization of an active fragment of colicin E3
    • Tokyo
    • Suzuki, K., and Imahori, K., Preparation and characterization of an active fragment of colicin E3. J. Biochem. (Tokyo), 84, 1021-1029 (1978).
    • (1978) J. Biochem. , vol.84 , pp. 1021-1029
    • Suzuki, K.1    Imahori, K.2
  • 24
    • 0018849601 scopus 로고
    • A novel ColE1::Tn3 plasmid vector that allows direct selection of hybrid clones in E. coli
    • Ozaki, L. S., Maeda, S., Shimada, K., and Takagi, Y., A novel ColE1::Tn3 plasmid vector that allows direct selection of hybrid clones in E. coli. Gene, 8, 301-314 (1980).
    • (1980) Gene , vol.8 , pp. 301-314
    • Ozaki, L.S.1    Maeda, S.2    Shimada, K.3    Takagi, Y.4
  • 25
    • 0021812295 scopus 로고
    • A direct-selection vector derived from pColE3-CA38 and adapted for foreign gene expression
    • Vernet, T., Lau, P. C., Narang, S. A., and Visentin, L. P., A direct-selection vector derived from pColE3-CA38 and adapted for foreign gene expression. Gene, 34, 87-93 (1985).
    • (1985) Gene , vol.34 , pp. 87-93
    • Vernet, T.1    Lau, P.C.2    Narang, S.A.3    Visentin, L.P.4
  • 26
    • 0034601693 scopus 로고    scopus 로고
    • Affinity selection of cDNA libraries by lambda phage surface display
    • Niwa, M., Maruyama, H., Fujimoto, T., Dohi, K., and Maruyama, I. N., Affinity selection of cDNA libraries by lambda phage surface display. Gene, 256, 229-236 (2000).
    • (2000) Gene , vol.256 , pp. 229-236
    • Niwa, M.1    Maruyama, H.2    Fujimoto, T.3    Dohi, K.4    Maruyama, I.N.5
  • 27
    • 0022372548 scopus 로고
    • The Escherichia coli strain JM105 contains partial supE activity
    • Reha-Krantz, L. J., The Escherichia coli strain JM105 contains partial supE activity. Gene, 38, 275-276 (1985).
    • (1985) Gene , vol.38 , pp. 275-276
    • Reha-Krantz, L.J.1
  • 28
    • 0024308743 scopus 로고
    • Molecular structure and immunity specificity of colicin E6, an evolutionary intermediate between E-group colicins and cloacin DF13
    • Akutsu, A., Masaki, H., and Ohta, T., Molecular structure and immunity specificity of colicin E6, an evolutionary intermediate between E-group colicins and cloacin DF13. J. Bacteriol., 171, 6430-6436 (1989).
    • (1989) J. Bacteriol. , vol.171 , pp. 6430-6436
    • Akutsu, A.1    Masaki, H.2    Ohta, T.3
  • 29
    • 0022671848 scopus 로고
    • Primary structures of the ColE2-P9 and ColE3-CA38 lysis genes
    • Tokyo
    • Toba, M., Masaki, H., and Ohta, T., Primary structures of the ColE2-P9 and ColE3-CA38 lysis genes. J. Biochem. (Tokyo), 99, 591-596 (1986).
    • (1986) J. Biochem. , vol.99 , pp. 591-596
    • Toba, M.1    Masaki, H.2    Ohta, T.3
  • 30
    • 0029934724 scopus 로고    scopus 로고
    • Identification of a biologically significant DNA-binding peptide motif by use of a random phage display library
    • Cheng, X., Kay, B. K., and Juliano, R. L., Identification of a biologically significant DNA-binding peptide motif by use of a random phage display library. Gene, 171, 1-8 (1996).
    • (1996) Gene , vol.171 , pp. 1-8
    • Cheng, X.1    Kay, B.K.2    Juliano, R.L.3
  • 31
    • 0026792839 scopus 로고
    • Simplified methods for construction, assessment and rapid screening of peptide libraries in bacteriophage
    • Christian, R. B., Zuckermann, R. N., Kerr, J. M., Wang, L., and Malcolm, B. A., Simplified methods for construction, assessment and rapid screening of peptide libraries in bacteriophage. J. Mol. Biol., 227, 711-718 (1992).
    • (1992) J. Mol. Biol. , vol.227 , pp. 711-718
    • Christian, R.B.1    Zuckermann, R.N.2    Kerr, J.M.3    Wang, L.4    Malcolm, B.A.5
  • 33
    • 0014748362 scopus 로고
    • Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification
    • Yamamoto, K. R., Alberts, B. M., Benzinger, R., Lawhorne, L., and Treiber, G., Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification. Virology, 40, 734-744 (1970).
    • (1970) Virology , vol.40 , pp. 734-744
    • Yamamoto, K.R.1    Alberts, B.M.2    Benzinger, R.3    Lawhorne, L.4    Treiber, G.5
  • 36
    • 0021357534 scopus 로고
    • Primary structure of the Saccharomyces cerevisiae GAL4 gene
    • Laughon, A., and Gesteland, R. F., Primary structure of the Saccharomyces cerevisiae GAL4 gene. Mol. Cell. Biol., 4, 260-267 (1984).
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 260-267
    • Laughon, A.1    Gesteland, R.F.2
  • 37
    • 0028168581 scopus 로고
    • Lambda foo: A lambda phage vector for the expression of foreign proteins
    • Maruyama, I. N., Maruyama, H. I., and Brenner, S., Lambda foo: a lambda phage vector for the expression of foreign proteins. Proc. Natl. Acad. Sci. U.S.A., 91, 8273-8277 (1994).
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 8273-8277
    • Maruyama, I.N.1    Maruyama, H.I.2    Brenner, S.3
  • 38
    • 0033056797 scopus 로고    scopus 로고
    • Mapping of the minimal domain encoding a conformational epitope by lambda phage surface display: Factor VIII inhibitor antibodies from haemophilia A patients
    • Kuwabara, I., Maruyama, H., Kamisue, S., Shima, M., Yoshioka, A., and Maruyama, I. N., Mapping of the minimal domain encoding a conformational epitope by lambda phage surface display: factor VIII inhibitor antibodies from haemophilia A patients. J. Immunol. Methods, 224, 89-99 (1999).
    • (1999) J. Immunol. Methods , vol.224 , pp. 89-99
    • Kuwabara, I.1    Maruyama, H.2    Kamisue, S.3    Shima, M.4    Yoshioka, A.5    Maruyama, I.N.6


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