메뉴 건너뛰기




Volumn 38, Issue 3, 2008, Pages 221-232

Optimization of the AT-content of codons immediately downstream of the initiation codon and evaluation of culture conditions for high-level expression of recombinant human G-CSF in Escherichia coli

Author keywords

AT rich codon; Codon optimization; High level expression; Recombinant human G CSF; Site directed mutagenesis; Specific product yield

Indexed keywords

CELL CULTURE; CELL GROWTH; CLONING; ESCHERICHIA COLI; GLUCOSE; GROWTH KINETICS; OPTIMIZATION; WATER POLLUTION;

EID: 41549150394     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12033-007-9018-3     Document Type: Article
Times cited : (14)

References (40)
  • 7
    • 0032465272 scopus 로고    scopus 로고
    • Glycosylated and non-glycosylated recombinant hG-CSF, What is the difference?
    • M. Hoglund 1998 Glycosylated and non-glycosylated recombinant hG-CSF, What is the difference? Medical Oncology 15 229 233
    • (1998) Medical Oncology , vol.15 , pp. 229-233
    • Hoglund, M.1
  • 11
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • F. Baneyx 1999 Recombinant protein expression in Escherichia coli Current Opinion in Biotechnology 10 411 421
    • (1999) Current Opinion in Biotechnology , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 12
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Escherichia coli
    • G. Hannig S. C. Makrides 1998 Strategies for optimizing heterologous protein expression in Escherichia coli Trends in Biotechnology 16 54 60
    • (1998) Trends in Biotechnology , vol.16 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2
  • 13
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • J. F. Kane 1995 Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli Current Opinion in Biotechnology 6 494 500
    • (1995) Current Opinion in Biotechnology , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 14
    • 0027960812 scopus 로고
    • Role of AGA/AGG codons the rarest codons in global gene expression in Escherichia coli
    • G. T. Chen M. Inouye 1994 Role of AGA/AGG codons the rarest codons in global gene expression in Escherichia coli Genes and Development 8 2641 2652
    • (1994) Genes and Development , vol.8 , pp. 2641-2652
    • Chen, G.T.1    Inouye, M.2
  • 15
    • 0032030138 scopus 로고    scopus 로고
    • Codon optimization of the gene encoding a domain from the human type 1 neurofibromin protein results in three fold improvement in expression level in Escherichia coli
    • R. S. Hale G. Thompson 1998 Codon optimization of the gene encoding a domain from the human type 1 neurofibromin protein results in three fold improvement in expression level in Escherichia coli Protein Expression and Purification 12 185 188
    • (1998) Protein Expression and Purification , vol.12 , pp. 185-188
    • Hale, R.S.1    Thompson, G.2
  • 16
    • 0030151989 scopus 로고    scopus 로고
    • Specific replacement of consecutive AGG codons results in high level expression of human cardiac troponin T in Escherichia coli
    • X. Hu Q. Shi T. Yang G. Jackowski 1996 Specific replacement of consecutive AGG codons results in high level expression of human cardiac troponin T in Escherichia coli Protein Expression and Purification 7 289 293
    • (1996) Protein Expression and Purification , vol.7 , pp. 289-293
    • Hu, X.1    Shi, Q.2    Yang, T.3    Jackowski, G.4
  • 17
    • 0023946307 scopus 로고
    • Alteration of amino-terminal codons of human granulocyte-colony- stimulating factor increases expression levels and allows efficient processing by methionine aminopeptidase in Escherichia coli
    • P. E. Devlin R. J. Drummond P. Toy D. F. Mark K. W. K. Watt J. J. Devlin 1988 Alteration of amino-terminal codons of human granulocyte-colony-stimulating factor increases expression levels and allows efficient processing by methionine aminopeptidase in Escherichia coli Gene 65 13 22
    • (1988) Gene , vol.65 , pp. 13-22
    • Devlin, P.E.1    Drummond, R.J.2    Toy, P.3    Mark, D.F.4    Watt, K.W.K.5    Devlin, J.J.6
  • 18
    • 2942726734 scopus 로고    scopus 로고
    • Expression of cDNA for rhG-CSF in E. coli and characterization of the protein
    • Z. H. Shu Y. Qinong 1998 Expression of cDNA for rhG-CSF in E. coli and characterization of the protein Chinese Journal of Cancer Research 10 256 259
    • (1998) Chinese Journal of Cancer Research , vol.10 , pp. 256-259
    • Shu, Z.H.1    Qinong, Y.2
  • 19
    • 0029084794 scopus 로고
    • High-level expression and simple purification of recombinant human granulocyte colony stimulating factor in E. coli
    • S. H. Kang K. H. Na J. H. Park C. Park S. Y. Lee Y. I. Lee 1995 High-level expression and simple purification of recombinant human granulocyte colony stimulating factor in E. coli Biotechnology Letter 17 687 692
    • (1995) Biotechnology Letter , vol.17 , pp. 687-692
    • Kang, S.H.1    Na, K.H.2    Park, J.H.3    Park, C.4    Lee, S.Y.5    Lee, Y.I.6
  • 22
    • 0023605128 scopus 로고
    • Purification and fractionation of Poly a + RNA
    • A. Jacobson 1987 Purification and fractionation of Poly A + RNA Methods in Enzymology 152 254 261
    • (1987) Methods in Enzymology , vol.152 , pp. 254-261
    • Jacobson, A.1
  • 23
    • 0015437962 scopus 로고
    • Measurement of molecular weights by electrophoresis on SDS-acrylamide gel
    • K. Weber J. R. Pringle M. Osborn 1972 Measurement of molecular weights by electrophoresis on SDS-acrylamide gel Methods in Enzymology 26 3 27
    • (1972) Methods in Enzymology , vol.26 , pp. 3-27
    • Weber, K.1    Pringle, J.R.2    Osborn, M.3
  • 24
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Helmut, B., Hildburg, B., & Gross (1987). Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophorisis, 8, 93-99.
    • (1987) Electrophorisis , vol.8 , pp. 93-99
    • Helmut, B.1    Hildburg, B.2    Gross3
  • 25
    • 0024365911 scopus 로고
    • MRNA secondary structure in an open reading frame reduces translation efficiency in Bacillus subtilis
    • M. Kubo T. Imanaka 1989 mRNA secondary structure in an open reading frame reduces translation efficiency in Bacillus subtilis Journal of Bacteriology 171 4080 4082
    • (1989) Journal of Bacteriology , vol.171 , pp. 4080-4082
    • Kubo, M.1    Imanaka, T.2
  • 26
    • 0026670290 scopus 로고
    • Translation inhibition by an mRNA coding region secondary structure is determined by its proximity to the AUG initiation codon
    • S. A. Liebhaber F. Cash S. S. Eshleman 1992 Translation inhibition by an mRNA coding region secondary structure is determined by its proximity to the AUG initiation codon Journal of Molecular Biology 226 609 621
    • (1992) Journal of Molecular Biology , vol.226 , pp. 609-621
    • Liebhaber, S.A.1    Cash, F.2    Eshleman, S.S.3
  • 28
    • 2642566651 scopus 로고    scopus 로고
    • Enhancement of translation initiation by AT-rich sequences downstream of the initiation codon in Escherichia coli
    • G. Qing B. Xia M. Inoute 2003 Enhancement of translation initiation by AT-rich sequences downstream of the initiation codon in Escherichia coli Journal of Molecular Microbiology and Biotechnology 6 133 144
    • (2003) Journal of Molecular Microbiology and Biotechnology , vol.6 , pp. 133-144
    • Qing, G.1    Xia, B.2    Inoute, M.3
  • 30
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto induction in high density shaking cultures
    • F. W. Studier 2005 Protein production by auto induction in high density shaking cultures Protein Expression and Purificaion 41 207 234
    • (2005) Protein Expression and Purificaion , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 31
    • 0032536841 scopus 로고    scopus 로고
    • Spontaneous cAMP dependent de repression of gene expression in stationary phase plays a role in recombinant expression instability
    • T. H. Grossman E. S. Kawasaki 1998 Spontaneous cAMP dependent de repression of gene expression in stationary phase plays a role in recombinant expression instability Gene 209 95 103
    • (1998) Gene , vol.209 , pp. 95-103
    • Grossman, T.H.1    Kawasaki, E.S.2
  • 32
    • 0030463296 scopus 로고    scopus 로고
    • Flux analysis and control of the central metabolic pathways in Escherichia coli
    • H. Holms 1996 Flux analysis and control of the central metabolic pathways in Escherichia coli FEMS Microbial Review 19 85 116
    • (1996) FEMS Microbial Review , vol.19 , pp. 85-116
    • Holms, H.1
  • 33
    • 0034528503 scopus 로고    scopus 로고
    • Reduced background expression and improved plasmid stability with PET vectors in BL 21 (DE3)
    • S Pan B. A. Malcolm 2000 Reduced background expression and improved plasmid stability with PET vectors in BL 21 (DE3) Biotechniques 29 1234 1238
    • (2000) Biotechniques , vol.29 , pp. 1234-1238
    • Pan, S.1    Malcolm, B.A.2
  • 34
    • 0344664014 scopus 로고    scopus 로고
    • Over expression of recombinant human interferon-gamma in high cell density fermentation of Escherichia coli
    • R. Khalilzadeh S. A. Shojaosadati A. Bahrami N. Maghsoudi 2003 Over expression of recombinant human interferon-gamma in high cell density fermentation of Escherichia coli Biotechnology Letter 25 1989 1992
    • (2003) Biotechnology Letter , vol.25 , pp. 1989-1992
    • Khalilzadeh, R.1    Shojaosadati, S.A.2    Bahrami, A.3    Maghsoudi, N.4
  • 35
    • 0014669901 scopus 로고
    • Cyclic reuse of RNA polymerase sigma factor
    • A. A. Travers R. R. Burges 1969 Cyclic reuse of RNA polymerase sigma factor Nature 222 537 540
    • (1969) Nature , vol.222 , pp. 537-540
    • Travers, A.A.1    Burges, R.R.2
  • 36
    • 0033180069 scopus 로고    scopus 로고
    • Use of Rifampicin in T7 RNA polymerase driven expression of a Plant enzyme: Rifampicin improves yield and assembly
    • A. Kuderova E Nanak M. Truksa B. Brzobohaty 1999 Use of Rifampicin in T7 RNA polymerase driven expression of a Plant enzyme: Rifampicin improves yield and assembly Protein Expression and Purification 16 405 409
    • (1999) Protein Expression and Purification , vol.16 , pp. 405-409
    • Kuderova, A.1    Nanak, E.2    Truksa, M.3    Brzobohaty, B.4
  • 37
    • 15844395096 scopus 로고    scopus 로고
    • Production of misfolding and induction formation in recombinant Ecsherichia coli cells overexpressing heat shock protein
    • J. G. Thomas F. Baneyx 1996 Production of misfolding and induction formation in recombinant Ecsherichia coli cells overexpressing heat shock protein Journal of Biological Chemistry 271 11141 11147
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 11141-11147
    • Thomas, J.G.1    Baneyx, F.2
  • 38
    • 3142726475 scopus 로고    scopus 로고
    • Role of heat shock protein in the production of recombinant proteins in Escherichia coli
    • F. Hoffmann U. Rinas 2004 Role of heat shock protein in the production of recombinant proteins in Escherichia coli Advances in Biochemical Engineering and Biotecnology 89 143 161
    • (2004) Advances in Biochemical Engineering and Biotecnology , vol.89 , pp. 143-161
    • Hoffmann, F.1    Rinas, U.2
  • 39
    • 0033662220 scopus 로고    scopus 로고
    • DNA microarray detection of metabolic responces to protein over production in Escherichia coli
    • M. K. Oh J. C. Liao 2000 DNA microarray detection of metabolic responces to protein over production in Escherichia coli Metabolic Engineering 2 201 209
    • (2000) Metabolic Engineering , vol.2 , pp. 201-209
    • Oh, M.K.1    Liao, J.C.2
  • 40
    • 0035808168 scopus 로고    scopus 로고
    • Genomic analysis of high cell density recombinant Escherichia coli fermentation and "cell conducting" for improved recombinant protein yield
    • R. Gill M. Delisa J. Valdes W. Bentlay 2000 Genomic analysis of high cell density recombinant Escherichia coli fermentation and "cell conducting" for improved recombinant protein yield Biotechnology and.Bioengineering 72 85 95
    • (2000) Biotechnology and .Bioengineering , vol.72 , pp. 85-95
    • Gill, R.1    Delisa, M.2    Valdes, J.3    Bentlay, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.