Designing Expression Plasmid Vectors in E. coli

  • Paulina Balbás
Part of the Methods in Molecular Biology book series (MIMB, volume 62)


The production of proteins is one of the main applications of genetic engineering in biotechnology. Even though standard cloning procedures are now routine and a large variety of host-vector systems for gene expression are available, difficulties are encountered when theoretical strategies are put into practice, so gene expression is still quite empirical. E. coli remains an important host system for the industrial production of proteins from cloned genes, and considerable lore has accumulated since the pioneering gene expression experiments. The extensive knowledge about E. coli’s physiology and genetics accounts for its preferential use as a host for gene expression. The inability of this organism to exert certain posttranslational modifications of proteins that lead to correct folding and activity represents its major drawback as a production organism.


Transcription Initiation Ribosome Binding Site mRNA Synthesis Replicative Plasmid Strain Genotype 
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  1. 1.
    Balbás, P. and Bolivar, F. (1990) Design and construction of expression plasmid vectors in E. coli. Methods. Enzymol. 185, 14–37.PubMedCrossRefGoogle Scholar
  2. 2.
    Balbás, P., Soberón, X., Merino, M., Zurita, M., Lomelí, H., Valle, F., Flores, N., and Bolivar, F. (1986) Plasmid pBR322 and its Special Purpose Derivatives—a Review. Gene 50, 3–40.PubMedCrossRefGoogle Scholar
  3. 3.
    Gerhardt, P., Murray, R. G. E., Wood, W. A., and Krieg, N. R. (1994) Methods for General and Molecular Bacteriology American Society for Microbiology, ASM Press, Washington, DC.Google Scholar
  4. 4.
    Schwab, H. (1993) Principles of Genetic Engineering for E. coli, in Genetic Engineering of Microorganisms (Pulher, A., ed.), VCH Publishers, New York, pp. 1–53.Google Scholar
  5. 5.
    Rosenbaum, V., Klahn, T., Lundberg, U., Holmgren, E., von Gabain, A., and Riesner, D. (1993) Co-existing structures of an mRNA stability determinant. J. Mol. Biol. 229, 656–670.PubMedCrossRefGoogle Scholar
  6. 6.
    Goeddel, D. V. (1990) Systems for heterologous gene expression. Methods Enzymol. 185, 3–7.PubMedCrossRefGoogle Scholar
  7. 7.
    Georgiou, G. and Bowden, G. A. (1991) Inclusion body formation and the recovery of aggregated recombinant proteins, in Recombinant DNA Technology and Applications (Prokop, A., Bajpai, R. K., and Ho, C., eds.), McGraw Hill, New York, pp. 333–356.Google Scholar
  8. 8.
    Bogosian, G., Kane, J. F., Obukowicz, M. G., and Olins, P. O. (1991) Optimizing protein production in recombinant strains of E. coli, in Recombinant DNA Technology and Applications (Prokop, A., Bajpai, R. K., and Ho, C., eds.), McGraw Hill, New York, pp. 285–315.Google Scholar
  9. 9.
    Shuler, M. L. and Kargi, F. (1992) Bioprocess Engineering Basic Concepts Prentice Hall, Englewood Cliffs, NJ.Google Scholar

Copyright information

© Humana Press Inc. 1997

Authors and Affiliations

  • Paulina Balbás
    • 1
  1. 1.Centro de Investigación en BiotechnologiaUniversidad Autónoma del Estado de MorelosCuernavacaMexico

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