Expression and secretion of proteins in E. coli
Tóm tắt
This review outlines approaches to the cloning and expression of proteins in Escherichia coli. The expression vectors described here (pIN-III derivatives) utilize the strong lipoprotein promoter, which is controlled by the lac-UV5 promoter-operator. These vectors provide the means for targeting a protein to any of the four subcellular compartments of the bacterial cell: cytoplasm, cytoplasmic membrane, periplasm, and outer membrane. Of particular importance is that secretion of proteins into the E. coli periplasm (using the OmpA signal peptide) is applicable for the production of both prokaryotic and eukaryotic proteins thereby enhancing protein activity and stability.
Tài liệu tham khảo
Methods in Molecular Biology, vol. 62: Recombinant Gene Expression Protocols. (Tuan, R., ed.), Humana Press, Totowa, NJ.
Gennity, J.M. and Inouye, M., (1991) Protein Secretion in Bacteria. Curr. Opin. Biotechnol. 266, 661–667.
Gennity, J., Goldstein, J., and Inouye, M., (1990) Signal Peptide Mutants of Escherichia coli. J. Bioenergetics Biomembranes 22, 233–269.
Lunn, C.A., Takahara, M., and Inouye, M., (1986) Use of Secretion Cloning Vectors for Guiding the Localization of Proteins in Escherichia coli. Methods Enzymol. 125, 138–149.
Stueber, D. and Bujard, H., (1982) Transcription from Efficient Promoters can Interfere with Plasmid Replication and Diminish Expression of Plasmid Specified Genes. EMBO J. 1, 1399–1404.
Inouye, M. and Halegoua, S., (1980) Secretion and Membrane Localization of Proteins in Escherichia coli. CRC Crit. Rev. Biochem. 7, 339–371.
Lunn, C.A., Takahara, M., and Inouye, M., (1986) Secretion Cloning Vectors for Guiding the Localization of Proteins in vivo. Curr. Topics Microbiolo. Immunol. 125, 59–74.
Masui, Y., Mizuno, T., and Inouye, M., (1984) Novel High Level Expression Cloning Vehicles: 104-fold Amplification of E., coli Minor Proteins. Bio/Technology 2, 81–85.
Masui, Y., Coleman, J., and Inouye, M., (1983) Multipurpose Expression Cloning Vehicles in E. coli, in Experimental Manipulation of Gene Expression (Inouye, M., ed.), Academic Press, New York, pp. 15–32.
Ghrayeb, J., Kimura, H., Takahara, M., Hsiung, H., Masui, Y., and Inouye, M., (1984) Secretion Cloning Vectors in Escherichia coli. EMBO J. 3, 2437–2442.
Wickner, W., (1983) M13 Coat Protein as a Model of Membrane Assembly. TIBS 8, 90–94.
Shine, J. and Dalgarno, L., (1975) Determination of Cistron Specificity in Bacterial Ribosomes. Nature 254, 34–38.
Ghrayeb, J., and Inouye, M., (1984) Nine Amino Acid Residues at the Amino Terminal of Lipoprotein are Sufficient for its Modification, Processing and Localization in the Outer Membrane of Escherichia coli. J. Biol. Chem. 259, 463–467.
Inouye, M., Nakamura, K., Inouye, S., and Masui, Y., (1983) Versatile Expression Cloning Vehicles using the Lipoprotein Gene of the Escherichia coli and Their Application, in The Future in Nucleic Acid Research (Watanabe, I., ed.), Academic Japan, Tokyo, pp. 419–436.
Koshland, D. and Botstein, D., (1980) Secretion of b-lactamase requires the carboxy end of the protein. Cell 20, 749–760.
Yu, F., Furukawa, H., Nakamura, K., and Mizushima, S., (1984) Mechanism of localization of major outer membrane lipoprotein in E., coli. J. Biol. Chem. 259, 6013–6018.
Pollitt, S., and Zalkin, H., (1983) Role of primary structure and disulfide bond formation in b-lactamase secretion. J. Bacteriol. 153, 27–32.
Takahara, M., Hibler, D.W., Barr, P.J., Gerlt, J.,A., and Inouye, M., (1985) OmpA signal peptide directed secretion of Staphylococcal nuclease A by Escherichia coli. J. Biol. Chem. 260, 2670–2674.
Hsuing, H.M., Mayne, N.G., and Becker, G.W., (1986) High level expression, efficient secretion and folding of human growth hormone in E. coli. Bio/Technology 4, 991–995.
Barthelemy, I., Gonzalez de Buitrago, G., Carreiro, C., Roncal, F., Perez-Aranda, A., Marquez, G., and Barbero, J.L., (1993) Production and secretion of human interleukin-6 into the periplasm of E. coli: Efficient processing of N-terminal variants of hIL-6 by the E., coli signal peptidase. J. Biotechnol. 27, 307–316.
Perez-Perez, J., Marquez, G., Barbero, J.L., and Gutierrez, J., (1994) Increasing the efficiency of protein export in E. coli. Bio/Technology 12, 178–180.
Takahara, M., Sagai, H., Inouye, S., and Inouye, M., (1988) Secretion of human superoxide dismutase in E. coli. Bio/Technology 6, 195–198.
Jabush, J.R., Farb, P.F., Kerschensteiner, D.,A., and Deutsh, H.,F., (1980) Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase. Biochemistry 19, 2310–2316.
Beauchamp, C. and Fridovich, I., (1971) Superoxide dismutase: Improved assays and an assay applicable to polyacrylamide gels. Annal. Biochem. 44, 276–287.
Meerman, H.J., and Georgiou, G., (1994) Construction and characterization of a set of E.,coli strains deficient in all known loci affecting the proteolytic stability of secreted recombinant proteins. Bio/Technology 12, 1107–1110.
Hoedemaeker, F.JU., Signorelli, T., Johns, K., Kuntz, D.A., and Rose, D.R., (1997) A single chain Fv fragment of P-glycoprotein-specific monoclonal antibody C219. Design, expression, and crystal structure at 2.4 A resolution. J. Biol. Chem. 272, 29,784–29,789.
Tudyka, T. and Skerra, A. (1997) Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli. Protein Sci. 6, 2180–2187.
Pritchard, M.P., Ossetian, R., Li, D.N., Henderson, C.J., Burchell, B., Wolf, C.R., and Friedberg, T., (1997) A general strategy for the expression of recombinant human cytochrome P450s in Escherichia coli using bacterial signal peptides: expression of CYP3A4, CYP2A6, and CYP2E1. Arch. Biochem. Biophys. 345, 342–254.
Rathore, D., Nayak, S.K., and Batra, J.K., (1997) Overproduction of fungal ribotoxin alpha-sarcin in Escherichia coli: generation of an active immunotoxin. Gene 190, 31–35.
Bardwell, J.C.A., and Beckwith, J., (1993) The bonds that tie: Catalyzed disulfide bond formation. Cell 74, 769–771.