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Volumn 35, Issue 4, 2007, Pages

Use of signal sequences as an in situ removable sequence element to stimulate protein synthesis in cell-free extracts

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DNA; RECOMBINANT PROTEIN; SIGNAL PEPTIDASE; TRITON X 100; HYBRID PROTEIN; SIGNAL PEPTIDE;

EID: 34047120198     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkl917     Document Type: Article
Times cited : (32)

References (32)
  • 2
    • 0037069324 scopus 로고    scopus 로고
    • A cell-free protein synthesis system for high-throughput proteomics
    • Sawasaki,T., Ogasawara,T., Morishita,R. and Endo,Y. (2002) A cell-free protein synthesis system for high-throughput proteomics. Proc. Natl Acad. Sci. USA, 99, 14652-14657.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 14652-14657
    • Sawasaki, T.1    Ogasawara, T.2    Morishita, R.3    Endo, Y.4
  • 3
    • 13944274948 scopus 로고    scopus 로고
    • The past, present and future of cell-free protein synthesis
    • Katzen,F., Chang,G. and Kudlicki,W. (2005) The past, present and future of cell-free protein synthesis. Trends Biotechnol., 23, 150-156.
    • (2005) Trends Biotechnol. , vol.23 , pp. 150-156
    • Katzen, F.1    Chang, G.2    Kudlicki, W.3
  • 4
    • 3142533355 scopus 로고    scopus 로고
    • Bacterial cell-free system for high-throughput protein expression and a comparative analysis of Escherichia coli cell-free and whole cell expression systems
    • Murthy,T.V., Wu,W., Qiu,Q.Q., Shi,Z., LaBaer,J. and Brizuela,L. (2004) Bacterial cell-free system for high-throughput protein expression and a comparative analysis of Escherichia coli cell-free and whole cell expression systems. Protein Expr. Purif., 36, 217-225.
    • (2004) Protein Expr. Purif. , vol.36 , pp. 217-225
    • Murthy, T.V.1    Wu, W.2    Qiu, Q.Q.3    Shi, Z.4    LaBaer, J.5    Brizuela, L.6
  • 5
    • 19544387611 scopus 로고    scopus 로고
    • Energizing cell-free protein synthesis with glucose metabolism
    • Calhoun,K.A. and Swartz,J.R. (2005) Energizing cell-free protein synthesis with glucose metabolism. Biotechnol. Bioeng., 90, 606-613.
    • (2005) Biotechnol. Bioeng. , vol.90 , pp. 606-613
    • Calhoun, K.A.1    Swartz, J.R.2
  • 6
    • 0034045838 scopus 로고    scopus 로고
    • Prolonging cell-free protein synthesis by selective reagent additions
    • Kim,D.M. and Swartz,J.R. (2000) Prolonging cell-free protein synthesis by selective reagent additions. Biotechnol. Prog., 16, 385-390.
    • (2000) Biotechnol. Prog. , vol.16 , pp. 385-390
    • Kim, D.M.1    Swartz, J.R.2
  • 7
    • 0035921172 scopus 로고    scopus 로고
    • Regeneration of adenosine triphosphate from glycolytic intermediates for cell-free protein synthesis
    • Kim,D.M. and Swartz,J.R. (2001) Regeneration of adenosine triphosphate from glycolytic intermediates for cell-free protein synthesis. Biotechnol. Bioeng., 74, 309-316.
    • (2001) Biotechnol. Bioeng. , vol.74 , pp. 309-316
    • Kim, D.M.1    Swartz, J.R.2
  • 8
    • 0942286940 scopus 로고    scopus 로고
    • Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli
    • Kim,D.M. and Swartz,J.R. (2004) Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli. Biotechnol. Bioeng., 85, 122-129.
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 122-129
    • Kim, D.M.1    Swartz, J.R.2
  • 9
    • 33745196264 scopus 로고    scopus 로고
    • Rapid production of milligram quantities of proteins in a batch cell-free protein synthesis system
    • Kim,T.W., Kim,D.M. and Choi,C.Y. (2006) Rapid production of milligram quantities of proteins in a batch cell-free protein synthesis system. J. Biotechnol., 124, 373-380.
    • (2006) J. Biotechnol. , vol.124 , pp. 373-380
    • Kim, T.W.1    Kim, D.M.2    Choi, C.Y.3
  • 10
    • 0035827918 scopus 로고    scopus 로고
    • Cooperative effects by the initiation codon and its flanking regions on translation initiation
    • Stenstrom,C.M., Holmgren,E. and Isaksson,L.A. (2001) Cooperative effects by the initiation codon and its flanking regions on translation initiation. Gene, 273, 259-265.
    • (2001) Gene , vol.273 , pp. 259-265
    • Stenstrom, C.M.1    Holmgren, E.2    Isaksson, L.A.3
  • 11
    • 0035941484 scopus 로고    scopus 로고
    • Codon bias at the 3′-side of the initiation codon is correlated with translation initiation efficiency in Escherichia coli
    • Stenstrom,C.M., Jin,H.N., Major,L.L., Tate,W.P. and Isaksson,L.A. (2001) Codon bias at the 3′-side of the initiation codon is correlated with translation initiation efficiency in Escherichia coli. Gene, 263, 273-284.
    • (2001) Gene , vol.263 , pp. 273-284
    • Stenstrom, C.M.1    Jin, H.N.2    Major, L.L.3    Tate, W.P.4    Isaksson, L.A.5
  • 12
    • 4944224262 scopus 로고    scopus 로고
    • A codon window in mRNA downstream of the initiation codon where NGG codons give strongly reduced gene expression in Escherichia coli
    • de Valdivia,E.I.G. and Isaksson,L.A. (2004) A codon window in mRNA downstream of the initiation codon where NGG codons give strongly reduced gene expression in Escherichia coli. Nucleic Acids Res., 32, 5198-5205.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5198-5205
    • de Valdivia, E.I.G.1    Isaksson, L.A.2
  • 13
    • 0037123362 scopus 로고    scopus 로고
    • Influences on translation initiation and early elongation by the messenger RNA region flanking the initiation codon at the 3' side
    • Stenstrom,C.M. and Isaksson,L.A. (2002) Influences on translation initiation and early elongation by the messenger RNA region flanking the initiation codon at the 3' side. Gene, 288, 1-8.
    • (2002) Gene , vol.288 , pp. 1-8
    • Stenstrom, C.M.1    Isaksson, L.A.2
  • 14
    • 0033537948 scopus 로고    scopus 로고
    • Translational enhancement by an element downstream of the initiation codon in Escherichia coli
    • Etchegaray,J.P. and Inouye,M. (1999) Translational enhancement by an element downstream of the initiation codon in Escherichia coli. J. Biol. Chem., 274, 10079-10085.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10079-10085
    • Etchegaray, J.P.1    Inouye, M.2
  • 15
    • 0029956987 scopus 로고    scopus 로고
    • A highly efficient cell-free protein synthesis system from Escherichia coli
    • Kim,D.M., Kigawa,T., Choi,C.Y. and Yokoyama,S. (1996) A highly efficient cell-free protein synthesis system from Escherichia coli. Eur. J. Biochem., 239, 881-886.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 881-886
    • Kim, D.M.1    Kigawa, T.2    Choi, C.Y.3    Yokoyama, S.4
  • 16
    • 27744523608 scopus 로고    scopus 로고
    • Cell-free synthesis of recombinant proteins from PCR-amplified genes at a comparable productivity to that of plasmid-based reactions
    • Ahn,J.H., Chu,H.S., Kim,T.W., Oh,I.S., Choi,C.Y., Hahn,G.H., Park,C.G. and Kim,D.M. (2005) Cell-free synthesis of recombinant proteins from PCR-amplified genes at a comparable productivity to that of plasmid-based reactions. Biochem. Biophys. Res. Commun., 338, 1346-1352.
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 1346-1352
    • Ahn, J.H.1    Chu, H.S.2    Kim, T.W.3    Oh, I.S.4    Choi, C.Y.5    Hahn, G.H.6    Park, C.G.7    Kim, D.M.8
  • 18
    • 25844498435 scopus 로고    scopus 로고
    • Effect of energy source on the efficiency of translational termination during cell-free protein synthesis
    • Ahn,J.H., Choi,C.Y. and Kim,D.M. (2005) Effect of energy source on the efficiency of translational termination during cell-free protein synthesis. Biochem. Biophys. Res. Commun., 337, 325-329.
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 325-329
    • Ahn, J.H.1    Choi, C.Y.2    Kim, D.M.3
  • 19
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger,H. and von Jagow,G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 20
    • 27144528592 scopus 로고    scopus 로고
    • Abortive translation caused by peptidyl-tRNA drop-off at NGG codons in the early coding region of mRNA
    • de Valdivia,E.I.G. and Isaksson,L.A. (2005) Abortive translation caused by peptidyl-tRNA drop-off at NGG codons in the early coding region of mRNA. FEBS J., 272, 5306-5316.
    • (2005) FEBS J. , vol.272 , pp. 5306-5316
    • de Valdivia, E.I.G.1    Isaksson, L.A.2
  • 21
    • 0034949816 scopus 로고    scopus 로고
    • Codon and base biases after the initiation codon of the open reading frames in the Escherichia coli genome and their influence on the translation efficiency
    • Sato,T., Terabe,M., Watanabe,H., Gojobori,T., Hori-Takemoto,C. and Miura,K. (2001) Codon and base biases after the initiation codon of the open reading frames in the Escherichia coli genome and their influence on the translation efficiency. J. Biochem. (Tokyo), 129, 851-860.
    • (2001) J. Biochem. (Tokyo) , vol.129 , pp. 851-860
    • Sato, T.1    Terabe, M.2    Watanabe, H.3    Gojobori, T.4    Hori-Takemoto, C.5    Miura, K.6
  • 22
    • 0028942966 scopus 로고
    • Characterization of a soluble, catalytically active form of Escherichia coli leader peptidase: Requirement of detergent or phospholipid for optimal activity
    • Tschantz,W.R., Paetzel,M., Cao,G., Suciu,D., Inouye,M. and Dalbey,R.E. (1995) Characterization of a soluble, catalytically active form of Escherichia coli leader peptidase: Requirement of detergent or phospholipid for optimal activity. Biochemistry, 34, 3935-3941.
    • (1995) Biochemistry , vol.34 , pp. 3935-3941
    • Tschantz, W.R.1    Paetzel, M.2    Cao, G.3    Suciu, D.4    Inouye, M.5    Dalbey, R.E.6
  • 23
    • 14844332027 scopus 로고    scopus 로고
    • The identification of residues that control signal peptidase cleavage fidelity and substrate specificity
    • Karla,A., Lively,M.O., Paetzel,M. and Dalbey,R. (2005) The identification of residues that control signal peptidase cleavage fidelity and substrate specificity. J. Biol. Chem., 280, 6731-6741.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6731-6741
    • Karla, A.1    Lively, M.O.2    Paetzel, M.3    Dalbey, R.4
  • 24
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor
    • Paetzel,M., Dalbey,R.E. and Strynadka,N.C. (1998) Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature, 396, 186-190.
    • (1998) Nature , vol.396 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.3
  • 25
    • 0037102410 scopus 로고    scopus 로고
    • Cis control of gene expression in E.coli by ribosome queuing at an inefficient translational stop signal
    • Jin,H.N., Bjornsson,A. and Isaksson,L.A. (2002) Cis control of gene expression in E.coli by ribosome queuing at an inefficient translational stop signal. EMBO J., 21, 4357-4367.
    • (2002) EMBO J. , vol.21 , pp. 4357-4367
    • Jin, H.N.1    Bjornsson, A.2    Isaksson, L.A.3
  • 26
    • 0345306332 scopus 로고    scopus 로고
    • The structural integrity exerted by N-terminal pyroglutamate is crucial for the cytotoxicity of frog ribonuclease from Rana pipiens
    • Liao,Y.D., Wang,S.C., Leu,Y.J., Wang,C.F., Chang,S.T., Hong,Y.T., Pan,Y.R. and Chen,C. (2003) The structural integrity exerted by N-terminal pyroglutamate is crucial for the cytotoxicity of frog ribonuclease from Rana pipiens. Nucleic Acids Res., 31, 5247-5255.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5247-5255
    • Liao, Y.D.1    Wang, S.C.2    Leu, Y.J.3    Wang, C.F.4    Chang, S.T.5    Hong, Y.T.6    Pan, Y.R.7    Chen, C.8
  • 27
    • 0029871341 scopus 로고    scopus 로고
    • Role of the N terminus in RNase A homologues: Differences in catalytic activity, ribonuclease inhibitor interaction and cytotoxicity
    • Boix,E., Wu,Y., Vasandani,V.M., Saxena,S.K., Ardelt,W., Ladner,J. and Youle,R.J. (1996) Role of the N terminus in RNase A homologues: differences in catalytic activity, ribonuclease inhibitor interaction and cytotoxicity. J. Mol. Biol., 257, 992-1007.
    • (1996) J. Mol. Biol. , vol.257 , pp. 992-1007
    • Boix, E.1    Wu, Y.2    Vasandani, V.M.3    Saxena, S.K.4    Ardelt, W.5    Ladner, J.6    Youle, R.J.7
  • 29
    • 0035969980 scopus 로고    scopus 로고
    • The additional methionine residue at the N-terminus of bacterially expressed human interleukin-2 affects the interaction between the N- and C-termini
    • Endo,S., Yamamoto,Y., Sugawara,T., Nishimura,O. and Fujino,M. (2001) The additional methionine residue at the N-terminus of bacterially expressed human interleukin-2 affects the interaction between the N- and C-termini. Biochemistry, 40, 914-919.
    • (2001) Biochemistry , vol.40 , pp. 914-919
    • Endo, S.1    Yamamoto, Y.2    Sugawara, T.3    Nishimura, O.4    Fujino, M.5
  • 30
    • 0031415310 scopus 로고    scopus 로고
    • Improvement of the refolding yield and solubility of hen egg-white lysozyme by altering the Met residue attached to its N-terminus to Ser
    • Mine,S., Ueda,T., Hashimoto,Y. and Imoto,T. (1997) Improvement of the refolding yield and solubility of hen egg-white lysozyme by altering the Met residue attached to its N-terminus to Ser. Protein Eng., 10, 1333-1338.
    • (1997) Protein Eng. , vol.10 , pp. 1333-1338
    • Mine, S.1    Ueda, T.2    Hashimoto, Y.3    Imoto, T.4
  • 32
    • 0038236890 scopus 로고    scopus 로고
    • Purification, characterization, and molecular cloning of a novel amine:pyruvate transaminase from Vibrio fluvialis JS17
    • Shin,J.S., Yun,H., Jang,J.W., Park,I. and Kim,B.G. (2003) Purification, characterization, and molecular cloning of a novel amine:pYruvate transaminase from Vibrio fluvialis JS17. Appl. Microbiol. Biotechnol., 61, 463-471.
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 463-471
    • Shin, J.S.1    Yun, H.2    Jang, J.W.3    Park, I.4    Kim, B.G.5


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