메뉴 건너뛰기




Volumn 26, Issue 6, 2010, Pages 1558-1566

Improved recombinant protein yield using a codon deoptimized DHFR selectable marker in a CHEF1 expression plasmid

Author keywords

CHEF1; CHO; Codon deoptimization; DHFR; Recombinant protein expression

Indexed keywords

CHEF1; CHO; CODON DEOPTIMIZATION; DHFR; RECOMBINANT PROTEIN EXPRESSION;

EID: 78650197691     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.491     Document Type: Article
Times cited : (19)

References (48)
  • 2
    • 0001127374 scopus 로고
    • Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity
    • Urlaub G, Chasin LA. Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity. Proc Natl Acad Sci USA. 1980; 77: 4216-4220.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 4216-4220
    • Urlaub, G.1    Chasin, L.A.2
  • 3
    • 0020040061 scopus 로고
    • Direct demonstration of genetic alterations at the dihydrofolate reductase locus after gamma irradiation
    • Graf LH Jr, Chasin LA. Direct demonstration of genetic alterations at the dihydrofolate reductase locus after gamma irradiation. Mol Cell Biol. 1982; 2: 93-96.
    • (1982) Mol Cell Biol , vol.2 , pp. 93-96
    • Graf Jr, L.H.1    Chasin, L.A.2
  • 4
    • 0020460545 scopus 로고
    • Construction of a modular dihydrofolate reductase cDNA gene: analysis of signals utilized for efficient expression
    • Kaufman RJ, Sharp PA. Construction of a modular dihydrofolate reductase cDNA gene: analysis of signals utilized for efficient expression. Mol Cell Biol. 1982; 2: 1304-1319.
    • (1982) Mol Cell Biol , vol.2 , pp. 1304-1319
    • Kaufman, R.J.1    Sharp, P.A.2
  • 5
    • 0020574233 scopus 로고
    • Deletion of the diploid dihydrofolate reductase locus from cultured mammalian cells
    • Urlaub G, Kas E, Carothers AM, Chasin LA. Deletion of the diploid dihydrofolate reductase locus from cultured mammalian cells. Cell. 1983; 33: 405-412.
    • (1983) Cell , vol.33 , pp. 405-412
    • Urlaub, G.1    Kas, E.2    Carothers, A.M.3    Chasin, L.A.4
  • 7
    • 0017807188 scopus 로고
    • Selective multiplication of dihydrofolate reductase genes in methotrexate-resistant variants of cultured murine cells
    • Alt FW, Kellems RE, Bertino JR, Schimke RT. Selective multiplication of dihydrofolate reductase genes in methotrexate-resistant variants of cultured murine cells. J Biol Chem. 1978; 253: 1357-1370.
    • (1978) J Biol Chem , vol.253 , pp. 1357-1370
    • Alt, F.W.1    Kellems, R.E.2    Bertino, J.R.3    Schimke, R.T.4
  • 9
    • 78650208371 scopus 로고
    • Fully impaired consensus Kozak sequences for mammalian expression. World Intellectual Property Organization. International Publication Number WO Pat., 94/11523, 26 May
    • Reff ME. Fully impaired consensus Kozak sequences for mammalian expression. World Intellectual Property Organization. International Publication Number WO Pat. 94/11523, 26 May 1994.
    • (1994)
    • Reff, M.E.1
  • 10
    • 0008200829 scopus 로고
    • Isolation and expression of an altered mouse dihydrofolate reductase cDNA
    • Simonsen CC, Levinson AD. Isolation and expression of an altered mouse dihydrofolate reductase cDNA. Proc Natl Acad Sci USA. 1983; 80: 2495-2499.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 2495-2499
    • Simonsen, C.C.1    Levinson, A.D.2
  • 11
    • 0026510218 scopus 로고
    • Construction of a dominant selectable marker using a novel dihydrofolate reductase
    • Hussain A, Lewis D, Yu M, Melera PW. Construction of a dominant selectable marker using a novel dihydrofolate reductase. Gene. 1992; 112: 179-188.
    • (1992) Gene , vol.112 , pp. 179-188
    • Hussain, A.1    Lewis, D.2    Yu, M.3    Melera, P.W.4
  • 13
    • 0027513392 scopus 로고
    • Effects of consecutive AGG codons on translation in Escherichia coli, demonstrated with a versatile codon test system
    • Rosenberg AH, Goldman E, Dunn JJ, Studier FW, Zubay G. Effects of consecutive AGG codons on translation in Escherichia coli, demonstrated with a versatile codon test system. J Bacteriol. 1993; 175: 716-722.
    • (1993) J Bacteriol , vol.175 , pp. 716-722
    • Rosenberg, A.H.1    Goldman, E.2    Dunn, J.J.3    Studier, F.W.4    Zubay, G.5
  • 14
    • 0024673103 scopus 로고
    • Nonrandom utilization of codon pairs in Escherichia coli
    • Gutman GA, Hatfield GW. Nonrandom utilization of codon pairs in Escherichia coli. Proc Natl Acad Sci USA. 1989; 86: 3699-3703.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3699-3703
    • Gutman, G.A.1    Hatfield, G.W.2
  • 15
    • 0038620436 scopus 로고    scopus 로고
    • Codon pairs in the genome of Escherichia coli
    • Boycheva S, Chkodrov G, Ivanov I. Codon pairs in the genome of Escherichia coli. Bioinformatics. 2003; 19: 987-998.
    • (2003) Bioinformatics , vol.19 , pp. 987-998
    • Boycheva, S.1    Chkodrov, G.2    Ivanov, I.3
  • 17
    • 0020486135 scopus 로고
    • A role for mRNA secondary structure in the control of translation initiation
    • Hall MN, Gabay J, Debarbouille M, Schwartz M. A role for mRNA secondary structure in the control of translation initiation. Nature. 1982; 295: 616-618.
    • (1982) Nature , vol.295 , pp. 616-618
    • Hall, M.N.1    Gabay, J.2    Debarbouille, M.3    Schwartz, M.4
  • 18
    • 0038463475 scopus 로고    scopus 로고
    • Effects of codon usage versus putative 5'-mRNA structure on the expression of Fusarium solani cutinase in the Escherichia coli cytoplasm
    • Griswold KE, Mahmood NA, Iverson BL, Georgiou G. Effects of codon usage versus putative 5'-mRNA structure on the expression of Fusarium solani cutinase in the Escherichia coli cytoplasm. Protein Expr Purif. 2003; 27: 134-142.
    • (2003) Protein Expr Purif , vol.27 , pp. 134-142
    • Griswold, K.E.1    Mahmood, N.A.2    Iverson, B.L.3    Georgiou, G.4
  • 19
    • 27144555357 scopus 로고    scopus 로고
    • Regulation of translation via mRNA structure in prokaryotes and eukaryotes
    • Kozak M. Regulation of translation via mRNA structure in prokaryotes and eukaryotes. Gene. 2005; 361: 13-37.
    • (2005) Gene , vol.361 , pp. 13-37
    • Kozak, M.1
  • 20
    • 64849114915 scopus 로고    scopus 로고
    • Coding-sequence determinants of gene expression in Escherichia coli
    • Kudla G, Murray AW, Tollervey D, Plotkin JB. Coding-sequence determinants of gene expression in Escherichia coli. Science. 2009; 324: 255-258.
    • (2009) Science , vol.324 , pp. 255-258
    • Kudla, G.1    Murray, A.W.2    Tollervey, D.3    Plotkin, J.B.4
  • 21
    • 0034736510 scopus 로고    scopus 로고
    • DNA G+C content of the third codon position and codon usage biases of human genes
    • Sueoka N, Kawanishi Y. DNA G+C content of the third codon position and codon usage biases of human genes. Gene. 2000; 261: 53-62.
    • (2000) Gene , vol.261 , pp. 53-62
    • Sueoka, N.1    Kawanishi, Y.2
  • 22
    • 0026010217 scopus 로고
    • Low-usage codons in Eshcerichia coli, yeast, fruit fly and primates
    • Zhang SP, Zubay G, Goldman E. Low-usage codons in Eshcerichia coli, yeast, fruit fly and primates. Gene. 1991; 105: 61-72.
    • (1991) Gene , vol.105 , pp. 61-72
    • Zhang, S.P.1    Zubay, G.2    Goldman, E.3
  • 23
    • 0037274714 scopus 로고    scopus 로고
    • In vivo introduction of unpreferred synonymous codons into the drosophila Adh gene results in reduced levels of ADH protein
    • Carlini DB, Stephan W. In vivo introduction of unpreferred synonymous codons into the drosophila Adh gene results in reduced levels of ADH protein. Genetics. 2003; 163: 239-243.
    • (2003) Genetics , vol.163 , pp. 239-243
    • Carlini, D.B.1    Stephan, W.2
  • 24
    • 0019474499 scopus 로고
    • Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes
    • Ikemura T. Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes. J Mol Biol. 1981; 146: 1-21.
    • (1981) J Mol Biol , vol.146 , pp. 1-21
    • Ikemura, T.1
  • 25
    • 0019824131 scopus 로고
    • Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes: a proposal for a synonymous codon choice that is optimal for the E. coli translational system
    • Ikemura T. Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes: a proposal for a synonymous codon choice that is optimal for the E. coli translational system. J Mol Biol. 1981; 151: 3389-3409.
    • (1981) J Mol Biol , vol.151 , pp. 3389-3409
    • Ikemura, T.1
  • 26
    • 0019949369 scopus 로고
    • Correlation between the abundance of yeast transfer RNAs and the occurrence of the respective codons in protein genes differences in synonymous codon choice patterns of yeast and Escherichia coli with reference to the abundance of isoaccepting transfer RNAs
    • Ikemura T. Correlation between the abundance of yeast transfer RNAs and the occurrence of the respective codons in protein genes differences in synonymous codon choice patterns of yeast and Escherichia coli with reference to the abundance of isoaccepting transfer RNAs. J Mol Biol. 1982; 158: 573-597.
    • (1982) J Mol Biol , vol.158 , pp. 573-597
    • Ikemura, T.1
  • 27
    • 0021958933 scopus 로고
    • Codon usage and tRNA content in unicellular and multicellular organisms
    • Ikemura T. Codon usage and tRNA content in unicellular and multicellular organisms. Mol Biol Evol. 1985; 2: 13-34.
    • (1985) Mol Biol Evol , vol.2 , pp. 13-34
    • Ikemura, T.1
  • 28
    • 0025789743 scopus 로고
    • Evaluation of foreign gene codon optimization in yeast: expression of a mouse Ig kappa chain
    • Kotula L, Curtis PJ. Evaluation of foreign gene codon optimization in yeast: expression of a mouse Ig kappa chain. Biotechnology. 1991; 9: 1386-1389.
    • (1991) Biotechnology , vol.9 , pp. 1386-1389
    • Kotula, L.1    Curtis, P.J.2
  • 29
    • 0027733935 scopus 로고
    • HIV1 integrase expressed in Escherichia coli from a synthetic gene
    • Holler TP, Foltin SK, Ye QZ, Hupe DJ. HIV1 integrase expressed in Escherichia coli from a synthetic gene. Gene. 1993; 136: 323-328.
    • (1993) Gene , vol.136 , pp. 323-328
    • Holler, T.P.1    Foltin, S.K.2    Ye, Q.Z.3    Hupe, D.J.4
  • 30
    • 0030823320 scopus 로고    scopus 로고
    • Codon optimization for high-level expression of human erythropoietin (EPO) in mammalian cells
    • Kim CH, Oh Y, Lee TH. Codon optimization for high-level expression of human erythropoietin (EPO) in mammalian cells. Gene. 1997; 199: 293-301.
    • (1997) Gene , vol.199 , pp. 293-301
    • Kim, C.H.1    Oh, Y.2    Lee, T.H.3
  • 31
    • 33645215084 scopus 로고    scopus 로고
    • Modulation of poliovirus replicative fitness in HeLa cells by deoptimization of synonymous codon usage in the capsid region
    • Burns CC, Shaw J, Campagnoli R, Jorba J, Vincent A, Quay J,Kew O. Modulation of poliovirus replicative fitness in HeLa cells by deoptimization of synonymous codon usage in the capsid region. J Virol. 2006; 80: 3259-3272.
    • (2006) J Virol , vol.80 , pp. 3259-3272
    • Burns, C.C.1    Shaw, J.2    Campagnoli, R.3    Jorba, J.4    Vincent, A.5    Quay, J.6    Kew, O.7
  • 32
    • 33748923860 scopus 로고    scopus 로고
    • Reduction of the rate of poliovirus protein synthesis through large-scale codon deoptimization causes attenuation of viral virulence by lowering specific infectivity
    • Mueller S, Papamichail D, Coleman JR, Skiena S, Wimmer E. Reduction of the rate of poliovirus protein synthesis through large-scale codon deoptimization causes attenuation of viral virulence by lowering specific infectivity. J Virol. 2006; 80: 9687-9696.
    • (2006) J Virol , vol.80 , pp. 9687-9696
    • Mueller, S.1    Papamichail, D.2    Coleman, J.R.3    Skiena, S.4    Wimmer, E.5
  • 33
    • 2942709860 scopus 로고    scopus 로고
    • High-level expression of proteins in mammalian cells using transcription regulatory sequences from the Chinese hamster EF-1α gene
    • Running Deer J, Allison DS. High-level expression of proteins in mammalian cells using transcription regulatory sequences from the Chinese hamster EF-1α gene. Biotechnol Prog. 2004; 20: 880.
    • (2004) Biotechnol Prog , vol.20 , pp. 880
    • Running Deer, J.1    Allison, D.S.2
  • 34
    • 0004136246 scopus 로고
    • Molecular Cloning: A Laboratory Manual
    • 2nd ed., New York, USA, Cold Spring Harbor Laboratory Press.
    • Sambrook J, Fritsch EF, Maniatis T. Molecular Cloning: A Laboratory Manual, 2nd ed. New York, USA: Cold Spring Harbor Laboratory Press; 1989.
    • (1989)
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 35
    • 0017847677 scopus 로고
    • Quantitation of dihydrofolate reductase in individual parental and methotrexate-resistant murine cells. Use of a fluorescence activated cell sorter
    • Kaufman RJ, Bertino JR, Schimke RT. Quantitation of dihydrofolate reductase in individual parental and methotrexate-resistant murine cells. Use of a fluorescence activated cell sorter. J Biol Chem. 1978; 253: 5852-5860.
    • (1978) J Biol Chem , vol.253 , pp. 5852-5860
    • Kaufman, R.J.1    Bertino, J.R.2    Schimke, R.T.3
  • 36
    • 0020408737 scopus 로고
    • A new fluorescent dihydrofolate reductase probe for studies of methotrexate resistance
    • Rosowsky A, Wright JE, Shapiro H, Beardsley P, Lazarus H. A new fluorescent dihydrofolate reductase probe for studies of methotrexate resistance. J Biol Chem. 1982; 257: 14162-14167.
    • (1982) J Biol Chem , vol.257 , pp. 14162-14167
    • Rosowsky, A.1    Wright, J.E.2    Shapiro, H.3    Beardsley, P.4    Lazarus, H.5
  • 37
    • 0020530971 scopus 로고
    • Rapid spontaneous dihydrofolate reductase gene amplification shown by fluorescence-activated cell sorting
    • Johnston RN, Beverley SM, Schimke RT. Rapid spontaneous dihydrofolate reductase gene amplification shown by fluorescence-activated cell sorting. Proc Natl Acad Sci USA. 1983; 80: 3711-3715.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 3711-3715
    • Johnston, R.N.1    Beverley, S.M.2    Schimke, R.T.3
  • 38
    • 0025159807 scopus 로고
    • Flow cytometric characterization of antifolate resistance in cultured mammalian cells using fluoresceinated methotrexate and daunorubicin
    • Sherwood SW, Assaraf YG, Molina A, Schimke RT. Flow cytometric characterization of antifolate resistance in cultured mammalian cells using fluoresceinated methotrexate and daunorubicin. Cancer Res. 1990; 50: 4946-4950.
    • (1990) Cancer Res , vol.50 , pp. 4946-4950
    • Sherwood, S.W.1    Assaraf, Y.G.2    Molina, A.3    Schimke, R.T.4
  • 40
    • 0342614926 scopus 로고    scopus 로고
    • Codon usage tabulated from international DNA sequence databases: status for the year 2000
    • Nakamura Y, Gojobori T, Ikemura T. Codon usage tabulated from international DNA sequence databases: status for the year 2000. Nucleic Acid Res 2000; 28: 292.
    • (2000) Nucleic Acid Res , vol.28 , pp. 292
    • Nakamura, Y.1    Gojobori, T.2    Ikemura, T.3
  • 41
    • 78650220593 scopus 로고
    • Recombinant cloning vehicle microbial polypeptide expression. US Pat., 4,704,362.
    • Itakura K, Riggs AD. Recombinant cloning vehicle microbial polypeptide expression. US Pat. 4, 704, 362; 1987.
    • (1987)
    • Itakura, K.1    Riggs, A.D.2
  • 42
    • 78650182092 scopus 로고    scopus 로고
    • High level expression of proteins. US Pat., 5,795,737.
    • Seed B, Haas J. High level expression of proteins. US Pat. 5, 795, 737; 1998.
    • (1998)
    • Seed, B.1    Haas, J.2
  • 43
    • 78650215604 scopus 로고    scopus 로고
    • Modulation of replicative fitness by deoptimization of synonymous codons. US Pat., US2008/0118530.
    • Kew O, Burns CC, Shaw J, Campagnoli R, Quay J. Modulation of replicative fitness by deoptimization of synonymous codons. US Pat. US2008/0118530; 2008.
    • (2008)
    • Kew, O.1    Burns, C.C.2    Shaw, J.3    Campagnoli, R.4    Quay, J.5
  • 44
    • 0004246255 scopus 로고
    • Molecular Biology of the Gene
    • 4th ed., Menlo Park, CA: The Benjamin/Cummings Publishing Company, Inc.
    • Watson JD, Hopkins, NH, Roberts JW, Steitz JA, Weiner AM. Molecular Biology of the Gene, 4th ed. Menlo Park, CA: The Benjamin/Cummings Publishing Company, Inc.; 1989: 1163.
    • (1989) , pp. 1163
    • Watson, J.D.1    Hopkins, N.H.2    Roberts, J.W.3    Steitz, J.A.4    Weiner, A.M.5
  • 45
    • 20444469682 scopus 로고    scopus 로고
    • Expression levels influence ribosomal frameshifting at the tandem rare arginine codons AGG_AGG and AGA_AGA in Escherichia coli
    • Gurvich OL, Baranov PV, Gesteland RF, Atkins JF. Expression levels influence ribosomal frameshifting at the tandem rare arginine codons AGG_AGG and AGA_AGA in Escherichia coli. J Bacteriol. 2005; 187: 4023-4032.
    • (2005) J Bacteriol , vol.187 , pp. 4023-4032
    • Gurvich, O.L.1    Baranov, P.V.2    Gesteland, R.F.3    Atkins, J.F.4
  • 46
    • 0023650543 scopus 로고
    • The codon adaptation index-a measure of directional synonomous codon usage bias, and its potential applications
    • Sharp PM, Li WH. The codon adaptation index-a measure of directional synonomous codon usage bias, and its potential applications. Nucleic Acids Res. 1987; 15: 1281-1295.
    • (1987) Nucleic Acids Res , vol.15 , pp. 1281-1295
    • Sharp, P.M.1    Li, W.H.2
  • 47
    • 0024966993 scopus 로고
    • Codon usage and secondary structure of MS2 phage RNA
    • Bulmer M. Codon usage and secondary structure of MS2 phage RNA. Nucleic Acids Res. 1989; 17: 1839-1843.
    • (1989) Nucleic Acids Res , vol.17 , pp. 1839-1843
    • Bulmer, M.1
  • 48
    • 0023350617 scopus 로고
    • The involvement of mRNA secondary structure in protein synthesis
    • Pelletier J, Sonenberg N. The involvement of mRNA secondary structure in protein synthesis. Biochem Cell Biol. 1987; 65: 576-581.
    • (1987) Biochem Cell Biol , vol.65 , pp. 576-581
    • Pelletier, J.1    Sonenberg, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.