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Volumn 431, Issue 2, 2013, Pages 291-295

Using E. coli-based cell-free protein synthesis to evaluate the kinetic performance of an orthogonal tRNA and aminoacyl-tRNA synthetase pair

Author keywords

Aminoacyl tRNA synthetase; Cell free protein synthesis; Escherichia coli; Glu NMP; Non natural amino acid; Orthogonal tRNA; PANOx SP

Indexed keywords

AMINO ACID; AMINO ACID TRANSFER RNA LIGASE; BACTERIAL ENZYME; PHENYLALANINE; TRANSFER RNA;

EID: 84873479729     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.12.108     Document Type: Article
Times cited : (19)

References (27)
  • 1
    • 8344222343 scopus 로고    scopus 로고
    • Prolegomena to future experimental efforts on genetic code engineering by expanding its amino acid repertoire
    • Budisa N. Prolegomena to future experimental efforts on genetic code engineering by expanding its amino acid repertoire. Angew. Chem. Int. Ed. Engl. 2004, 43:6426-6463.
    • (2004) Angew. Chem. Int. Ed. Engl. , vol.43 , pp. 6426-6463
    • Budisa, N.1
  • 2
    • 0026342056 scopus 로고
    • Biosynthetic method for introducing unnatural amino acids site-specifically into proteins
    • Ellman J., Mendel D., Anthony-Cahill S., et al. Biosynthetic method for introducing unnatural amino acids site-specifically into proteins. Methods Enzymol. 1991, 202:301-336.
    • (1991) Methods Enzymol. , vol.202 , pp. 301-336
    • Ellman, J.1    Mendel, D.2    Anthony-Cahill, S.3
  • 3
    • 0029108642 scopus 로고
    • Probing protein structure and function with an expanded genetic code
    • Cornish V.W., Mendel D., Schultz P.G. Probing protein structure and function with an expanded genetic code. Angew. Chem. Int. Ed. Engl. 1995, 34:621-633.
    • (1995) Angew. Chem. Int. Ed. Engl. , vol.34 , pp. 621-633
    • Cornish, V.W.1    Mendel, D.2    Schultz, P.G.3
  • 5
    • 73049150125 scopus 로고
    • The dependence of cell-free protein synthesis in E. coli upon naturally occurring or synthetic polyribonucleotides
    • Nirenberg M.W., Matthaei J.H. The dependence of cell-free protein synthesis in E. coli upon naturally occurring or synthetic polyribonucleotides. Proc. Natl. Acad. Sci. USA 1961, 47:1588-1602.
    • (1961) Proc. Natl. Acad. Sci. USA , vol.47 , pp. 1588-1602
    • Nirenberg, M.W.1    Matthaei, J.H.2
  • 6
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin A.S., Baranov V.I., Ryabova L.A., et al. A continuous cell-free translation system capable of producing polypeptides in high yield. Science 1988, 242:1162-1164.
    • (1988) Science , vol.242 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3
  • 7
    • 33646126496 scopus 로고    scopus 로고
    • Total amino acid stabilization during cell-free protein synthesis reactions
    • Calhoun K.A., Swartz J.R. Total amino acid stabilization during cell-free protein synthesis reactions. J. Biotechnol. 2006, 123:193-203.
    • (2006) J. Biotechnol. , vol.123 , pp. 193-203
    • Calhoun, K.A.1    Swartz, J.R.2
  • 8
    • 3242686114 scopus 로고    scopus 로고
    • Amino acid stabilization for cell-free protein synthesis by modification of the Escherichia coli genome
    • Michel-Reydellet N., Calhoun K., Swartz J. Amino acid stabilization for cell-free protein synthesis by modification of the Escherichia coli genome. Metab. Eng. 2004, 6:197-203.
    • (2004) Metab. Eng. , vol.6 , pp. 197-203
    • Michel-Reydellet, N.1    Calhoun, K.2    Swartz, J.3
  • 9
    • 1542720448 scopus 로고    scopus 로고
    • Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis
    • Jewett M.C., Swartz J.R. Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol. Bioeng. 2004, 86:19-26.
    • (2004) Biotechnol. Bioeng. , vol.86 , pp. 19-26
    • Jewett, M.C.1    Swartz, J.R.2
  • 10
    • 53949093950 scopus 로고    scopus 로고
    • An integrated cell-free metabolic platform for protein production and synthetic biology
    • Jewett M.C., Calhoun K.A., Voloshin A., et al. An integrated cell-free metabolic platform for protein production and synthetic biology. Mol. Syst. Biol. 2008, 4:1-10.
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 1-10
    • Jewett, M.C.1    Calhoun, K.A.2    Voloshin, A.3
  • 11
    • 77049113819 scopus 로고    scopus 로고
    • Site-specific incorporation of p-propargyloxyphenylalanine in a cell-free environment for direct protein-protein click conjugation
    • Bundy B.C., Swartz J.R. Site-specific incorporation of p-propargyloxyphenylalanine in a cell-free environment for direct protein-protein click conjugation. Bioconjugate Chem. 2010, 21:255-263.
    • (2010) Bioconjugate Chem. , vol.21 , pp. 255-263
    • Bundy, B.C.1    Swartz, J.R.2
  • 12
    • 58249085422 scopus 로고    scopus 로고
    • High-level cell-free synthesis yields of proteins containing site-specific non-natural amino acids
    • Goerke A.R., Swartz J.R. High-level cell-free synthesis yields of proteins containing site-specific non-natural amino acids. Biotechnol. Bioeng. 2009, 102:400-416.
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 400-416
    • Goerke, A.R.1    Swartz, J.R.2
  • 13
    • 0141732270 scopus 로고    scopus 로고
    • Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae
    • Deiters A., Cropp T.A., Mukherji M., et al. Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae. J. Am. Chem. Soc. 2003, 125:11782-11783.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11782-11783
    • Deiters, A.1    Cropp, T.A.2    Mukherji, M.3
  • 14
    • 34249750450 scopus 로고    scopus 로고
    • Photochemistry of aromatic azides and nitrenes
    • Budyka M.F. Photochemistry of aromatic azides and nitrenes. High Energy Chem. 2007, 41:176-187.
    • (2007) High Energy Chem. , vol.41 , pp. 176-187
    • Budyka, M.F.1
  • 15
    • 23244440886 scopus 로고    scopus 로고
    • An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates
    • Calhoun K.A., Swartz J.R. An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates. Biotechnol. Prog. 2005, 21:1146-1153.
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1146-1153
    • Calhoun, K.A.1    Swartz, J.R.2
  • 16
    • 0034833416 scopus 로고    scopus 로고
    • A general approach for the generation of orthogonal tRNAs
    • Wang L., Schultz P.G. A general approach for the generation of orthogonal tRNAs. Chem. Biol. 2001, 8:883-890.
    • (2001) Chem. Biol. , vol.8 , pp. 883-890
    • Wang, L.1    Schultz, P.G.2
  • 17
    • 0034730077 scopus 로고    scopus 로고
    • Studies of promoter recognition and start site selection by T7 RNA polymerase using a comprehensive collection of promoter variants
    • Imburgio D., Rong M., Ma K., et al. Studies of promoter recognition and start site selection by T7 RNA polymerase using a comprehensive collection of promoter variants. Biochemistry 2000, 39:10419-10430.
    • (2000) Biochemistry , vol.39 , pp. 10419-10430
    • Imburgio, D.1    Rong, M.2    Ma, K.3
  • 18
    • 0026067489 scopus 로고
    • Specific contacts between the bacteriophage T3, T7, and SP6 RNA polymerases and their promoters
    • Jorgensen E.D., Durbin R.K., Risman S.S., et al. Specific contacts between the bacteriophage T3, T7, and SP6 RNA polymerases and their promoters. J. Biol. Chem. 1991, 266:645-651.
    • (1991) J. Biol. Chem. , vol.266 , pp. 645-651
    • Jorgensen, E.D.1    Durbin, R.K.2    Risman, S.S.3
  • 19
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson J.R., Uhlenbeck O.C. Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc. Natl. Acad. Sci. USA 1988, 85:1033-1037.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 20
    • 0032566634 scopus 로고    scopus 로고
    • Ribozyme processed tRNA transcripts with unfriendly internal promoter for T7 RNA polymerase: production and activity
    • Fechter P., Rudinger J., Giegé R., et al. Ribozyme processed tRNA transcripts with unfriendly internal promoter for T7 RNA polymerase: production and activity. FEBS Lett. 1998, 436:99-103.
    • (1998) FEBS Lett. , vol.436 , pp. 99-103
    • Fechter, P.1    Rudinger, J.2    Giegé, R.3
  • 21
    • 0000640710 scopus 로고    scopus 로고
    • Modulation of chemical composition and other parameters of the cell by growth rate
    • ASM Press, Washington, DC, F.C. Neidhardt, R. Curtiss III, J.L. Ingraham (Eds.)
    • Bremer H., Dennis P.P. Modulation of chemical composition and other parameters of the cell by growth rate. Escherichia Coli and Salmonella: Cellular and Molecular Biology 1996, 1553-1569. ASM Press, Washington, DC. second ed. F.C. Neidhardt, R. Curtiss III, J.L. Ingraham (Eds.).
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 1553-1569
    • Bremer, H.1    Dennis, P.P.2
  • 22
    • 23244446620 scopus 로고    scopus 로고
    • Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis
    • Underwood K.A., Swartz J.R., Puglisi J.D. Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis. Biotechnol. Bioeng. 2005, 91:425-435.
    • (2005) Biotechnol. Bioeng. , vol.91 , pp. 425-435
    • Underwood, K.A.1    Swartz, J.R.2    Puglisi, J.D.3
  • 23
    • 0025269273 scopus 로고
    • Genomic organization and physical mapping of the transfer RNA genes in Escherichia coli K12
    • Komine Y., Adachi T., Inokuchi H., et al. Genomic organization and physical mapping of the transfer RNA genes in Escherichia coli K12. J. Mol. Biol. 1990, 212:579-598.
    • (1990) J. Mol. Biol. , vol.212 , pp. 579-598
    • Komine, Y.1    Adachi, T.2    Inokuchi, H.3
  • 24
    • 0021173799 scopus 로고
    • Quantities of individual aminoacyl-tRNA families and their turnover in Escherichia coli
    • Jakubowski H., Goldman E. Quantities of individual aminoacyl-tRNA families and their turnover in Escherichia coli. J. Bacteriol. 1984, 158:769-776.
    • (1984) J. Bacteriol. , vol.158 , pp. 769-776
    • Jakubowski, H.1    Goldman, E.2
  • 25
    • 78049415799 scopus 로고    scopus 로고
    • Engineering of an orthogonal aminoacyl-tRNA synthetase for efficient incorporation of the non-natural amino acid O-methyl-L-tyrosine using fluorescence-based bacterial cell sorting
    • Kuhn S.M., Rubini M., Fuhrmann M., et al. Engineering of an orthogonal aminoacyl-tRNA synthetase for efficient incorporation of the non-natural amino acid O-methyl-L-tyrosine using fluorescence-based bacterial cell sorting. J. Mol. Biol. 2010, 404:70-87.
    • (2010) J. Mol. Biol. , vol.404 , pp. 70-87
    • Kuhn, S.M.1    Rubini, M.2    Fuhrmann, M.3
  • 26
    • 43049142194 scopus 로고    scopus 로고
    • High yield cell-free production of integral membrane proteins without refolding or detergents
    • Wuu J.J., Swartz J.R. High yield cell-free production of integral membrane proteins without refolding or detergents. Biochim. Biophys. Acta 2008, 1778:1237-1250.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1237-1250
    • Wuu, J.J.1    Swartz, J.R.2
  • 27
    • 77951236321 scopus 로고    scopus 로고
    • Beyond the canonical 20 amino acids: expanding the genetic lexicon
    • Young T.S., Schultz P.G. Beyond the canonical 20 amino acids: expanding the genetic lexicon. J. Biol. Chem. 2010, 285:11039-11044.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11039-11044
    • Young, T.S.1    Schultz, P.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.