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Volumn 30, Issue 21, 2002, Pages 4692-4699

Site-specific incorporation of an unnatural amino acid into proteins in mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; IODOTYROSINE; PEPTIDE SYNTHASE; TETRACYCLINE; TRANSFER RNA; TYROSINE;

EID: 0036849244     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkf589     Document Type: Article
Times cited : (211)

References (38)
  • 1
    • 0027203297 scopus 로고
    • New photolabeling and crosslinking methods
    • Brunner, J. (1993) New photolabeling and crosslinking methods. Annu. Rev. Biochem., 62, 483-514.
    • (1993) Annu. Rev. Biochem , vol.62 , pp. 483-514
    • Brunner, J.1
  • 2
    • 0033200393 scopus 로고    scopus 로고
    • Peptide ligation and its application to protein engineering
    • Cotton, G.J. and Muir, T.W. (1999) Peptide ligation and its application to protein engineering. Chem. Biol., 6, R247-R256.
    • (1999) Chem. Biol , vol.6
    • Cotton, G.J.1    Muir, T.W.2
  • 3
    • 0023720484 scopus 로고
    • Biosynthesis of a protein containing a nonprotein amino acid by Escherichia Coli: L-2-aminohexanoic acid at position 21 in human epidermal growth factor
    • Koide, H., Yokoyama, S., Kawai, G., Ha, J., Oka, T., Kawai, S., Miyake, T., Fuwa, T. and Miyazawa, T. (1988) Biosynthesis of a protein containing a nonprotein amino acid by Escherichia Coli: L-2-aminohexanoic acid at position 21 in human epidermal growth factor. Proc. Natl Acad. Sci. USA, 85, 6237-6241.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6237-6241
    • Koide, H.1    Yokoyama, S.2    Kawai, G.3    Ha, J.4    Oka, T.5    Kawai, S.6    Miyake, T.7    Fuwa, T.8    Miyazawa, T.9
  • 4
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren, C.J., Anthony-Cahill, S.J., Griffith, M.C. and Schultz, P.G. (1989) A general method for site-specific incorporation of unnatural amino acids into proteins. Science, 244, 182-188.
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 5
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson, W.A., Horton, J.R. and LeMaster, D.M. (1990) Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J., 9, 1665-1672.
    • (1990) EMBO J , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 7
    • 0033637431 scopus 로고    scopus 로고
    • Unnatural amino acids as probes of protein structure and function
    • Dougherty, D.A. (2000) Unnatural amino acids as probes of protein structure and function. Curr. Opin. Chem. Biol., 4, 645-652.
    • (2000) Curr. Opin. Chem. Biol , vol.4 , pp. 645-652
    • Dougherty, D.A.1
  • 9
    • 0031937870 scopus 로고    scopus 로고
    • Expansion of the genetic code: Site-directed p-fluorophenylalanine incorporation in Escherichia coli
    • Furter, R. (1998) Expansion of the genetic code: site-directed p-fluorophenylalanine incorporation in Escherichia coli. Protein Sci., 7, 419-426.
    • (1998) Protein Sci , vol.7 , pp. 419-426
    • Furter, R.1
  • 10
    • 0025874005 scopus 로고
    • Site-specific incorporation of nonnatural residues during in vitro protein biosynthesis with semisynthetic aminoacyl-tRNAs
    • Bain, J.D., Diala, E.S., Glabe, C.G., Wacker, D.A., Lyttle, M.H., Dix, T.A. and Chamberlin, A.R. (1991) Site-specific incorporation of nonnatural residues during in vitro protein biosynthesis with semisynthetic aminoacyl-tRNAs. Biochemistry, 30, 5411-5421.
    • (1991) Biochemistry , vol.30 , pp. 5411-5421
    • Bain, J.D.1    Diala, E.S.2    Glabe, C.G.3    Wacker, D.A.4    Lyttle, M.H.5    Dix, T.A.6    Chamberlin, A.R.7
  • 11
    • 0034254518 scopus 로고    scopus 로고
    • Probing the S1/S1′ substrate binding pocket geometry of HIV-1 protease with modified aspartic acid analogues
    • Short, G.F., III, Laikhter, A.L., Lodder, M., Shayo, Y., Arslan, T. and Hecht, S.M. (2000) Probing the S1/S1′ substrate binding pocket geometry of HIV-1 protease with modified aspartic acid analogues. Biochemistry, 39, 8768-8781.
    • (2000) Biochemistry , vol.39 , pp. 8768-8781
    • Short G.F. III1    Laikhter, A.L.2    Lodder, M.3    Shayo, Y.4    Arslan, T.5    Hecht, S.M.6
  • 12
    • 0032541289 scopus 로고    scopus 로고
    • A photochemical switch for controlling protein-protein interactions
    • Pollitt, S.K. and Schultz, P.G. (1998) A photochemical switch for controlling protein-protein interactions. Angew. Chem. Int. Ed., 37, 2104-2107.
    • (1998) Angew. Chem. Int. Ed , vol.37 , pp. 2104-2107
    • Pollitt, S.K.1    Schultz, P.G.2
  • 13
    • 0032486776 scopus 로고    scopus 로고
    • Site-directed incorporation of p-nitrophenylalanine into streptavidin and site-to-site photoinduced electron transfer from a pyrenyl group to a nitrophenyl group on the protein framework
    • Murakami, H., Hohsaka, T., Ashizuka, Y. and Sisido, M. (1998) Site-directed incorporation of p-nitrophenylalanine into streptavidin and site-to-site photoinduced electron transfer from a pyrenyl group to a nitrophenyl group on the protein framework. J. Am. Chem. Soc., 120, 7520-7529.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 7520-7529
    • Murakami, H.1    Hohsaka, T.2    Ashizuka, Y.3    Sisido, M.4
  • 14
    • 0026523058 scopus 로고
    • Ribosome-mediated incorporation of a non-standard amino acid into a peptide through expansion of the genetic code
    • Bain, J.D., Switzer, C., Chamberlin, A.R. and Benner, S.A. (1992) Ribosome-mediated incorporation of a non-standard amino acid into a peptide through expansion of the genetic code. Nature, 356, 537-539.
    • (1992) Nature , vol.356 , pp. 537-539
    • Bain, J.D.1    Switzer, C.2    Chamberlin, A.R.3    Benner, S.A.4
  • 17
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang, L., Brock, A., Herberich, B. and Schultz, P.G. (2001) Expanding the genetic code of Escherichia coli. Science, 292, 498-500.
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 18
    • 0037028931 scopus 로고    scopus 로고
    • Adding L-3-(2-naphthyl)alanine to the genetic code of E. coli
    • Wang, L., Brock, A. and Schultz, P.G. (2002) Adding L-3-(2-naphthyl)alanine to the genetic code of E. coli. J. Am. Chem. Soc., 124, 1836-1837.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 1836-1837
    • Wang, L.1    Brock, A.2    Schultz, P.G.3
  • 19
    • 0037162453 scopus 로고    scopus 로고
    • An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system
    • Kiga, D., Sakamoto, K., Kodama, K., Kigawa, T., Matsuda, T., Yabuki, T., Shirouzu, M., Harada, Y., Nakayama, H., Takio, K. et al. (2002) An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system. Proc. Natl Acad. Sci. USA, 99, 9715-9720.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9715-9720
    • Kiga, D.1    Sakamoto, K.2    Kodama, K.3    Kigawa, T.4    Matsuda, T.5    Yabuki, T.6    Shirouzu, M.7    Harada, Y.8    Nakayama, H.9    Takio, K.10
  • 20
    • 0030029337 scopus 로고    scopus 로고
    • Amber suppression in mammalian cells dependent upon expression of an Escherichia coli aminoacyl-tRNA synthetase gene
    • Drabkin, H.J., Park, H. and RajBhandary, U.L. (1996) Amber suppression in mammalian cells dependent upon expression of an Escherichia coli aminoacyl-tRNA synthetase gene. Mol. Cell. Biol., 16, 907-913.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 907-913
    • Drabkin, H.J.1    Park, H.2    RajBhandary, U.L.3
  • 21
    • 0035807914 scopus 로고    scopus 로고
    • Import of amber and ochre suppressor tRNAs into mammalian cells: A general approach to site-specific insertion of amino acid analogues into proteins
    • Köhrer, C., Xie, L., Kellerer, S., Varshney, U. and RajBhandary, U.L. (2001) Import of amber and ochre suppressor tRNAs into mammalian cells: a general approach to site-specific insertion of amino acid analogues into proteins. Proc. Natl Acad. Sci. USA, 98, 14310-14315.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14310-14315
    • Köhrer, C.1    Xie, L.2    Kellerer, S.3    Varshney, U.4    RajBhandary, U.L.5
  • 22
    • 0025052308 scopus 로고
    • Tyr by tyrosyl-tRNA synthetase
    • Tyr by tyrosyl-tRNA synthetase. Biochimie, 72, 589-598.
    • (1990) Biochimie , vol.72 , pp. 589-598
    • Bedouelle, H.1
  • 23
    • 0023061746 scopus 로고
    • Tyr gene are both transcribed in a HeLa cell extract but spliced along different pathways
    • Tyr gene are both transcribed in a HeLa cell extract but spliced along different pathways. EMBO J., 6, 35-41.
    • (1987) EMBO J , vol.6 , pp. 35-41
    • van Tol, H.1    Stange, N.2    Groos, H.J.3    Beier, H.4
  • 24
    • 0036093854 scopus 로고    scopus 로고
    • Chimeric receptor analyses of the interactions of the ectodomains of ErbB-1 with epidermal growth factor and of those of ErbB-4 with neuregulin
    • Kim, J.-H., Saito, K. and Yokoyama, S. (2002) Chimeric receptor analyses of the interactions of the ectodomains of ErbB-1 with epidermal growth factor and of those of ErbB-4 with neuregulin. Eur. J. Biochem., 269, 2323-2329.
    • (2002) Eur. J. Biochem , vol.269 , pp. 2323-2329
    • Kim, J.-H.1    Saito, K.2    Yokoyama, S.3
  • 25
    • 0001875439 scopus 로고
    • Transcription of eukaryotic tRNA genes
    • Söll, D. and RajBhandary, U.L. (eds), AMS Press, Washington, DC
    • Sprague, K.U. (1994) Transcription of eukaryotic tRNA genes. In Söll, D. and RajBhandary, U.L. (eds), tRNA: Structure, Biosynthesis and Function. AMS Press, Washington, DC, pp. 31-50.
    • (1994) TRNA: Structure, Biosynthesis and Function , pp. 31-50
    • Sprague, K.U.1
  • 26
    • 0002891712 scopus 로고
    • tRNA discrimination in aminoacylation
    • Söll, D. and RajBhandary, U.L. (eds), AMS Press, Washington, DC
    • Pallanck, L., Pak, M. and Schulman, L. (1994) tRNA discrimination in aminoacylation. In Söll, D. and RajBhandary, U.L. (eds), tRNA: Structure, Biosynthesis and Function. AMS Press, Washington, DC, pp. 371-394.
    • (1994) TRNA: Structure, Biosynthesis and Function , pp. 371-394
    • Pallanck, L.1    Pak, M.2    Schulman, L.3
  • 27
    • 0024459644 scopus 로고
    • Conformation of guanosine 5′-diphosphate as bound to a human c-Ha-ras mutant protein: A nuclear Overhauser effect study
    • Ha, J.-M., Ito, Y., Kawai, G., Miyazawa, T., Miura, K., Ohtsuka, E., Noguchi, S., Nishimura, S. and Yokoyama, S. (1989) Conformation of guanosine 5′-diphosphate as bound to a human c-Ha-ras mutant protein: a nuclear Overhauser effect study. Biochemistry, 28, 8411-8416.
    • (1989) Biochemistry , vol.28 , pp. 8411-8416
    • Ha, J.-M.1    Ito, Y.2    Kawai, G.3    Miyazawa, T.4    Miura, K.5    Ohtsuka, E.6    Noguchi, S.7    Nishimura, S.8    Yokoyama, S.9
  • 29
    • 0022993694 scopus 로고
    • Introduction of UAG, UAA and UGA nonsense mutations at a specific site in Escherichia coli chloramphenicol acetyltransferase gene: Use in measurement of amber, ochre and opal suppression in mammalian cells
    • Capone, J.P., Sedivy, J.M, Sharp, P.A. and RajBhandary, U.L. (1986) Introduction of UAG, UAA and UGA nonsense mutations at a specific site in Escherichia coli chloramphenicol acetyltransferase gene: use in measurement of amber, ochre and opal suppression in mammalian cells. Mol. Cell. Biol., 6, 3059-3067.
    • (1986) Mol. Cell. Biol , vol.6 , pp. 3059-3067
    • Capone, J.P.1    Sedivy, J.M.2    Sharp, P.A.3    RajBhandary, U.L.4
  • 30
    • 0034002603 scopus 로고    scopus 로고
    • Suppression of nonsense mutations in cell culture and mice by multimerized suppressor tRNA genes
    • Buvoli, M. Buvoli, A. and Leinwand, L. (2000) Suppression of nonsense mutations in cell culture and mice by multimerized suppressor tRNA genes. Mol. Cell. Biol., 20, 3116-3124.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 3116-3124
    • Buvoli, M.1    Buvoli, A.2    Leinwand, L.3
  • 31
    • 0025095302 scopus 로고
    • Role of amino acid transport and countertransport in nutrition and metabolism
    • Christensen, H.N. (1990) Role of amino acid transport and countertransport in nutrition and metabolism. Physiol. Rev., 70, 43-77.
    • (1990) Physiol. Rev , vol.70 , pp. 43-77
    • Christensen, H.N.1
  • 32
    • 0013906161 scopus 로고
    • The catalytic properties of tyrosyl ribonucleic acid synthetases from Escherichia coli and Bacillus subtilis
    • Calendar, R. and Berg, P. (1966) The catalytic properties of tyrosyl ribonucleic acid synthetases from Escherichia coli and Bacillus subtilis. Biochemistry, 5, 1690-1695.
    • (1966) Biochemistry , vol.5 , pp. 1690-1695
    • Calendar, R.1    Berg, P.2
  • 33
    • 0017904430 scopus 로고
    • Incorporation of radioiodotyrosines into proteins formed during cell-free translation
    • Scherberg, N.H., Seo, H. and Hynes, R. (1978) Incorporation of radioiodotyrosines into proteins formed during cell-free translation. J. Biol. Chem., 253, 1773-1779.
    • (1978) J. Biol. Chem , vol.253 , pp. 1773-1779
    • Scherberg, N.H.1    Seo, H.2    Hynes, R.3
  • 34
    • 0034846960 scopus 로고    scopus 로고
    • Changing the amino acid specificity of yeast tyrosyl-tRNA synthetase by genetic engineering
    • Ohno, S., Yokogawa, T. and Nishikawa, K. (2001) Changing the amino acid specificity of yeast tyrosyl-tRNA synthetase by genetic engineering. J. Biochem. (Tokyo), 130, 417-423.
    • (2001) J. Biochem. (Tokyo) , vol.130 , pp. 417-423
    • Ohno, S.1    Yokogawa, T.2    Nishikawa, K.3
  • 35
    • 0031857535 scopus 로고    scopus 로고
    • Tetracycline-regulated suppression of amber codons in mammalian cells
    • Park, H. and RajBhandary, U.L. (1998) Tetracycline-regulated suppression of amber codons in mammalian cells. Mol. Cell. Biol., 18, 4418-4425.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 4418-4425
    • Park, H.1    RajBhandary, U.L.2
  • 36
    • 0020327122 scopus 로고
    • Construction of a functional human suppressor tRNA gene: An approach to gene therapy for β-thalassaemia
    • Temple, G.F., Dozy, A.M., Roy, K.L. and Kan, Y.W. (1982) Construction of a functional human suppressor tRNA gene: an approach to gene therapy for β-thalassaemia. Nature, 296, 537-540.
    • (1982) Nature , vol.296 , pp. 537-540
    • Temple, G.F.1    Dozy, A.M.2    Roy, K.L.3    Kan, Y.W.4
  • 37
    • 0028241478 scopus 로고
    • Mutations to nonsense codons in human genetic disease: Implications for gene therapy by nonsense suppressor tRNAs
    • Atkinson, J. and Martin, R. (1994) Mutations to nonsense codons in human genetic disease: implications for gene therapy by nonsense suppressor tRNAs. Nucleic Acids Res., 22, 1327-1334.
    • (1994) Nucleic Acids Res , vol.22 , pp. 1327-1334
    • Atkinson, J.1    Martin, R.2
  • 38
    • 0025736352 scopus 로고
    • Ablation of Drosophila photoreceptor cells by conditional expression of a toxin gene
    • Kunes, S. and Steller, H. (1991) Ablation of Drosophila photoreceptor cells by conditional expression of a toxin gene. Genes Dev., 5, 970-983.
    • (1991) Genes Dev , vol.5 , pp. 970-983
    • Kunes, S.1    Steller, H.2


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