메뉴 건너뛰기




Volumn 17, Issue 4, 2006, Pages 347-352

Finding one of a kind: advances in single-protein production

Author keywords

[No Author keywords available]

Indexed keywords

BIOREACTORS; CELLS; ESCHERICHIA COLI; RNA; SYNTHESIS (CHEMICAL);

EID: 33746740015     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.copbio.2006.06.007     Document Type: Review
Times cited : (8)

References (39)
  • 2
    • 0019800517 scopus 로고
    • Bacterial production of human insulin
    • Riggs A.D. Bacterial production of human insulin. Diabetes Care 4 (1981) 64-68
    • (1981) Diabetes Care , vol.4 , pp. 64-68
    • Riggs, A.D.1
  • 3
    • 8344271025 scopus 로고    scopus 로고
    • Advances in the production of human therapeutic proteins in yeasts and filamentous fungi
    • Gerngross T.U. Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nat Biotechnol 22 (2004) 1409-1414
    • (2004) Nat Biotechnol , vol.22 , pp. 1409-1414
    • Gerngross, T.U.1
  • 4
    • 0036447573 scopus 로고    scopus 로고
    • Expression and purification of homogenous proteins in Saccharomyces cerevisiae based on ubiquitin-FLAG fusion
    • Einhauer A., Schuster M., Wasserbauer E., and Jungbauer A. Expression and purification of homogenous proteins in Saccharomyces cerevisiae based on ubiquitin-FLAG fusion. Protein Expr Purif 24 (2002) 497-504
    • (2002) Protein Expr Purif , vol.24 , pp. 497-504
    • Einhauer, A.1    Schuster, M.2    Wasserbauer, E.3    Jungbauer, A.4
  • 5
    • 14744285206 scopus 로고    scopus 로고
    • Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production
    • Daly R., and Hearn M.T. Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production. J Mol Recognit 18 (2005) 119-138
    • (2005) J Mol Recognit , vol.18 , pp. 119-138
    • Daly, R.1    Hearn, M.T.2
  • 6
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • Macauley-Patrick S., Fazenda M.L., McNeil B., and Harvey L.M. Heterologous protein production using the Pichia pastoris expression system. Yeast 22 (2005) 249-270
    • (2005) Yeast , vol.22 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 7
    • 0030629552 scopus 로고    scopus 로고
    • Production of heterologous proteins using the baculovirus/insect expression system
    • Griffiths C.M., and Page M.J. Production of heterologous proteins using the baculovirus/insect expression system. Methods Mol Biol 75 (1997) 427-440
    • (1997) Methods Mol Biol , vol.75 , pp. 427-440
    • Griffiths, C.M.1    Page, M.J.2
  • 8
    • 0032485534 scopus 로고    scopus 로고
    • Enhanced TGFβ1 maturation in high five cells coinfected with recombinant baculovirus encoding the convertase furin/pace: improved technology for the production of recombinant proproteins in insect cells
    • Laprise M.H., Grondin F., and Dubois C.M. Enhanced TGFβ1 maturation in high five cells coinfected with recombinant baculovirus encoding the convertase furin/pace: improved technology for the production of recombinant proproteins in insect cells. Biotechnol Bioeng 58 (1998) 85-91
    • (1998) Biotechnol Bioeng , vol.58 , pp. 85-91
    • Laprise, M.H.1    Grondin, F.2    Dubois, C.M.3
  • 9
    • 15744403561 scopus 로고
    • High level, stable production of recombinant proteins in mammalian cell culture using the herpesvirus VP16 transactivator
    • Hippenmeyer P., and Highkin M. High level, stable production of recombinant proteins in mammalian cell culture using the herpesvirus VP16 transactivator. Biotechnology (NY) 11 (1993) 1037-1041
    • (1993) Biotechnology (NY) , vol.11 , pp. 1037-1041
    • Hippenmeyer, P.1    Highkin, M.2
  • 10
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant protein therapeutics in cultivated mammalian cells
    • Wurm F.M. Production of recombinant protein therapeutics in cultivated mammalian cells. Nat Biotechnol 22 (2004) 1393-1398
    • (2004) Nat Biotechnol , vol.22 , pp. 1393-1398
    • Wurm, F.M.1
  • 11
    • 33644814737 scopus 로고    scopus 로고
    • Advances in genome-wide protein expression using the wheat germ cell-free system
    • Endo Y., and Sawasaki T. Advances in genome-wide protein expression using the wheat germ cell-free system. Methods Mol Biol 310 (2005) 145-167
    • (2005) Methods Mol Biol , vol.310 , pp. 145-167
    • Endo, Y.1    Sawasaki, T.2
  • 12
    • 33644810868 scopus 로고    scopus 로고
    • The wheat germ cell-free expression system: methods for high-throughput materialization of genetic information
    • Sawasaki T., Gouda M.D., Kawasaki T., Tsuboi T., Tozawa Y., Takai K., and Endo Y. The wheat germ cell-free expression system: methods for high-throughput materialization of genetic information. Methods Mol Biol 310 (2005) 131-144
    • (2005) Methods Mol Biol , vol.310 , pp. 131-144
    • Sawasaki, T.1    Gouda, M.D.2    Kawasaki, T.3    Tsuboi, T.4    Tozawa, Y.5    Takai, K.6    Endo, Y.7
  • 13
    • 0141975780 scopus 로고    scopus 로고
    • High-throughput, genome-scale protein production method based on the wheat germ cell-free expression system
    • This article reviews a high-throughput protein production method based on the cell-free system prepared from wheat embryos. It discusses the modifications that were performed to optimize the translation yield.
    • Endo Y., and Sawasaki T. High-throughput, genome-scale protein production method based on the wheat germ cell-free expression system. Biotechnol Adv 21 (2003) 695-713. This article reviews a high-throughput protein production method based on the cell-free system prepared from wheat embryos. It discusses the modifications that were performed to optimize the translation yield.
    • (2003) Biotechnol Adv , vol.21 , pp. 695-713
    • Endo, Y.1    Sawasaki, T.2
  • 14
    • 3543147238 scopus 로고    scopus 로고
    • Preparation of Escherichia coli cell extract for highly productive cell-free protein expression
    • Using an E. coli extract for cell-free protein synthesis, the authors developed a high-throughput pipeline for protein sample preparation for structural genomics and proteomics.
    • Kigawa T., Yabuki T., Matsuda N., Matsuda T., Nakajima R., Tanaka A., and Yokoyama S. Preparation of Escherichia coli cell extract for highly productive cell-free protein expression. J Struct Funct Genomics 5 (2004) 63-68. Using an E. coli extract for cell-free protein synthesis, the authors developed a high-throughput pipeline for protein sample preparation for structural genomics and proteomics.
    • (2004) J Struct Funct Genomics , vol.5 , pp. 63-68
    • Kigawa, T.1    Yabuki, T.2    Matsuda, N.3    Matsuda, T.4    Nakajima, R.5    Tanaka, A.6    Yokoyama, S.7
  • 15
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labeling of milligram quantities of proteins
    • Kigawa T., Yabuki T., Yoshida Y., Tsutsui M., Ito Y., Shibata T., and Yokoyama S. Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett 442 (1999) 15-19
    • (1999) FEBS Lett , vol.442 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3    Tsutsui, M.4    Ito, Y.5    Shibata, T.6    Yokoyama, S.7
  • 16
    • 0033404584 scopus 로고    scopus 로고
    • Prolonging cell-free protein synthesis with a novel ATP regeneration system
    • Kim D.M., and Swartz J.R. Prolonging cell-free protein synthesis with a novel ATP regeneration system. Biotechnol Bioeng 66 (1999) 180-188
    • (1999) Biotechnol Bioeng , vol.66 , pp. 180-188
    • Kim, D.M.1    Swartz, J.R.2
  • 17
    • 0030250637 scopus 로고    scopus 로고
    • A semicontinuous prokaryotic coupled transcription/translation system using a dialysis membrane
    • Kim D.M., and Choi C.Y. A semicontinuous prokaryotic coupled transcription/translation system using a dialysis membrane. Biotechnol Prog 12 (1996) 645-649
    • (1996) Biotechnol Prog , vol.12 , pp. 645-649
    • Kim, D.M.1    Choi, C.Y.2
  • 18
    • 0037069324 scopus 로고    scopus 로고
    • A cell-free protein synthesis system for high-throughput proteomics
    • Sawasaki T., Ogasawara T., Morishita R., and Endo Y. A cell-free protein synthesis system for high-throughput proteomics. Proc Natl Acad Sci USA 99 (2002) 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
  • 19
    • 0015871909 scopus 로고
    • In vitro synthesis of protein in microbial systems
    • Zubay G. In vitro synthesis of protein in microbial systems. Annu Rev Genet 7 (1973) 267-287
    • (1973) Annu Rev Genet , vol.7 , pp. 267-287
    • Zubay, G.1
  • 20
    • 0034613064 scopus 로고    scopus 로고
    • Expression of different coding sequences in cell-free bacterial and eukaryotic systems indicates translational pausing on Escherichia coli ribosomes
    • Ramachandiran V., Kramer G., and Hardesty B. Expression of different coding sequences in cell-free bacterial and eukaryotic systems indicates translational pausing on Escherichia coli ribosomes. FEBS Lett 482 (2000) 185-188
    • (2000) FEBS Lett , vol.482 , pp. 185-188
    • Ramachandiran, V.1    Kramer, G.2    Hardesty, B.3
  • 21
    • 23244446620 scopus 로고    scopus 로고
    • Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis
    • Underwood K.A., Swartz J.R., and Puglisi J.D. Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis. Biotechnol Bioeng 91 (2005) 425-435
    • (2005) Biotechnol Bioeng , vol.91 , pp. 425-435
    • Underwood, K.A.1    Swartz, J.R.2    Puglisi, J.D.3
  • 22
    • 3543116722 scopus 로고    scopus 로고
    • High-throughput, genome-scale protein production method based on the wheat germ cell-free expression system
    • Endo Y., and Sawasaki T. High-throughput, genome-scale protein production method based on the wheat germ cell-free expression system. J Struct Funct Genomics 5 (2004) 45-57
    • (2004) J Struct Funct Genomics , vol.5 , pp. 45-57
    • Endo, Y.1    Sawasaki, T.2
  • 23
    • 0036667328 scopus 로고    scopus 로고
    • The 5′-leader of tobacco mosaic virus promotes translation through enhanced recruitment of eIF4F
    • Gallie D.R. The 5′-leader of tobacco mosaic virus promotes translation through enhanced recruitment of eIF4F. Nucleic Acids Res 30 (2002) 3401-3411
    • (2002) Nucleic Acids Res , vol.30 , pp. 3401-3411
    • Gallie, D.R.1
  • 25
    • 33645395535 scopus 로고    scopus 로고
    • An efficient mammalian cell-free translation system supplemented with translation factors
    • The authors examined whether cell-free protein synthesis using HeLa cells was enhanced if supplemented with translational initiation factors or translational regulators.
    • Mikami S., Masutani M., Sonenberg N., Yokoyama S., and Imataka H. An efficient mammalian cell-free translation system supplemented with translation factors. Protein Expr Purif 46 (2006) 348-357. The authors examined whether cell-free protein synthesis using HeLa cells was enhanced if supplemented with translational initiation factors or translational regulators.
    • (2006) Protein Expr Purif , vol.46 , pp. 348-357
    • Mikami, S.1    Masutani, M.2    Sonenberg, N.3    Yokoyama, S.4    Imataka, H.5
  • 26
    • 0030454053 scopus 로고    scopus 로고
    • General RNA binding proteins render translation cap dependent
    • Svitkin Y.V., Ovchinnikov L.P., Dreyfuss G., and Sonenberg N. General RNA binding proteins render translation cap dependent. EMBO J 15 (1996) 7147-7155
    • (1996) EMBO J , vol.15 , pp. 7147-7155
    • Svitkin, Y.V.1    Ovchinnikov, L.P.2    Dreyfuss, G.3    Sonenberg, N.4
  • 27
    • 0035674431 scopus 로고    scopus 로고
    • Poly(A)-binding protein interaction with elF4G stimulates picornavirus IRES-dependent translation
    • Svitkin Y.V., Imataka H., Khaleghpour K., Kahvejian A., Liebig H.D., and Sonenberg N. Poly(A)-binding protein interaction with elF4G stimulates picornavirus IRES-dependent translation. RNA 7 (2001) 1743-1752
    • (2001) RNA , vol.7 , pp. 1743-1752
    • Svitkin, Y.V.1    Imataka, H.2    Khaleghpour, K.3    Kahvejian, A.4    Liebig, H.D.5    Sonenberg, N.6
  • 28
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • A protocol is described where high protein expression is induced in a lac operon-derived expression system by auto-induction without using IPTG.
    • Studier F.W. Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41 (2005) 207-234. A protocol is described where high protein expression is induced in a lac operon-derived expression system by auto-induction without using IPTG.
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 30
    • 0035913735 scopus 로고    scopus 로고
    • Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy
    • This article describes an in-cell NMR method that was developed to enable one to observe protein conformations inside living cells. Rifampicin was used to suppress bacterial protein synthesis and to allow expression of the protein of interest that was under the control of a T7 promoter.
    • Serber Z., Ledwidge R., Miller S.M., and Dotsch V. Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy. J Am Chem Soc 123 (2001) 8895-8901. This article describes an in-cell NMR method that was developed to enable one to observe protein conformations inside living cells. Rifampicin was used to suppress bacterial protein synthesis and to allow expression of the protein of interest that was under the control of a T7 promoter.
    • (2001) J Am Chem Soc , vol.123 , pp. 8895-8901
    • Serber, Z.1    Ledwidge, R.2    Miller, S.M.3    Dotsch, V.4
  • 31
    • 0031105797 scopus 로고    scopus 로고
    • Mathematical model of the lac operon: inducer exclusion, catabolite repression, and diauxic growth on glucose and lactose
    • Wong P., Gladney S., and Keasling J.D. Mathematical model of the lac operon: inducer exclusion, catabolite repression, and diauxic growth on glucose and lactose. Biotechnol Prog 13 (1997) 132-143
    • (1997) Biotechnol Prog , vol.13 , pp. 132-143
    • Wong, P.1    Gladney, S.2    Keasling, J.D.3
  • 32
    • 0035206064 scopus 로고    scopus 로고
    • The organization of metabolic reaction networks. III. Application for diauxic growth on glucose and lactose
    • Kremling A., Bettenbrock K., Laube B., Jahreis K., Lengeler J.W., and Gilles E.D. The organization of metabolic reaction networks. III. Application for diauxic growth on glucose and lactose. Metab Eng 3 (2001) 362-379
    • (2001) Metab Eng , vol.3 , pp. 362-379
    • Kremling, A.1    Bettenbrock, K.2    Laube, B.3    Jahreis, K.4    Lengeler, J.W.5    Gilles, E.D.6
  • 33
    • 17044408749 scopus 로고    scopus 로고
    • Single protein production in living cells facilitated by an mRNA interferase
    • The authors designed a single-protein production system in living E. coli cells that exploits the unique properties of MazF, a bacterial toxin that is a single-stranded RNA- and ACA-specific endoribonuclease.
    • Suzuki M., Zhang J., Liu M., Woychik N.A., and Inouye M. Single protein production in living cells facilitated by an mRNA interferase. Mol Cell 18 (2005) 253-261. The authors designed a single-protein production system in living E. coli cells that exploits the unique properties of MazF, a bacterial toxin that is a single-stranded RNA- and ACA-specific endoribonuclease.
    • (2005) Mol Cell , vol.18 , pp. 253-261
    • Suzuki, M.1    Zhang, J.2    Liu, M.3    Woychik, N.A.4    Inouye, M.5
  • 34
    • 0242361323 scopus 로고    scopus 로고
    • MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli
    • The first report to demonstrate that MazF toxin encoded by the 'mazE-mazF addiction module' is a sequence-specific (ACA) endoribonuclease functional only for single-stranded RNA.
    • Zhang Y., Zhang J., Hoeflich K.P., Ikura M., Qing G., and Inouye M. MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli. Mol Cell 12 (2003) 913-923. The first report to demonstrate that MazF toxin encoded by the 'mazE-mazF addiction module' is a sequence-specific (ACA) endoribonuclease functional only for single-stranded RNA.
    • (2003) Mol Cell , vol.12 , pp. 913-923
    • Zhang, Y.1    Zhang, J.2    Hoeflich, K.P.3    Ikura, M.4    Qing, G.5    Inouye, M.6
  • 35
    • 3042825336 scopus 로고    scopus 로고
    • Cold-shock induced high-yield protein production in Escherichia coli
    • The authors apply the unique features of the cspA gene to develop a series of expression vectors, termed pCold vectors, which drive the high expression of cloned genes upon induction by cold shock.
    • Qing G., Ma L.C., Khorchid A., Swapna G.V., Mal T.K., Takayama M.M., Xia B., Phadtare S., Ke H., Acton T., et al. Cold-shock induced high-yield protein production in Escherichia coli. Nat Biotechnol 22 (2004) 877-882. The authors apply the unique features of the cspA gene to develop a series of expression vectors, termed pCold vectors, which drive the high expression of cloned genes upon induction by cold shock.
    • (2004) Nat Biotechnol , vol.22 , pp. 877-882
    • Qing, G.1    Ma, L.C.2    Khorchid, A.3    Swapna, G.V.4    Mal, T.K.5    Takayama, M.M.6    Xia, B.7    Phadtare, S.8    Ke, H.9    Acton, T.10
  • 36
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublie S. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol 276 (1997) 523-530
    • (1997) Methods Enzymol , vol.276 , pp. 523-530
    • Doublie, S.1
  • 37
    • 11144247743 scopus 로고    scopus 로고
    • Accurate multiplex gene synthesis from programmable DNA microchips
    • Tian J., Gong H., Sheng N., Zhou X., Gulari E., Gao X., and Church G. Accurate multiplex gene synthesis from programmable DNA microchips. Nature 432 (2004) 1050-1054
    • (2004) Nature , vol.432 , pp. 1050-1054
    • Tian, J.1    Gong, H.2    Sheng, N.3    Zhou, X.4    Gulari, E.5    Gao, X.6    Church, G.7
  • 39
    • 10844238943 scopus 로고    scopus 로고
    • Unattended high-density cell growth and induction of protein expression with the Overnight Express Autinduction System
    • Grabski A., Mehler M., and Drott D. Unattended high-density cell growth and induction of protein expression with the Overnight Express Autinduction System. InNovations 17 (2003) 3-6
    • (2003) InNovations , vol.17 , pp. 3-6
    • Grabski, A.1    Mehler, M.2    Drott, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.