Enhanced expression of the yeast Ure2 protein in Escherichia coli: The effect of synonymous codon substitutions at a selected place in the gene

Biological Chemistry

Volumn 379, Issue 10, 1998, Pages 1295-1300

  Komar, Anton A ^a   Guillemet, Elisabeth ^a   Reiss, Claude ^a   Cullin, Christophe ^a  

^a CNRS   (France)

Author keywords

Codon usage; Expression; Translation; Ure2p

Indexed keywords

EPITOPE; FUNGAL PROTEIN; RECOMBINANT PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CODON USAGE; ESCHERICHIA COLI; EXPRESSION VECTOR; IMMUNOBLOTTING; NONHUMAN; PRIORITY JOURNAL; PROTEIN SYNTHESIS; YEAST;

AMINO ACID SEQUENCE; BASE SEQUENCE; CLONING, MOLECULAR; CODON; DNA, RECOMBINANT; ESCHERICHIA COLI; FUNGAL PROTEINS; MUTAGENESIS; OPEN READING FRAMES; PLASMIDS; PRIONS; REPRESSOR PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

ESCHERICHIA COLI; UNIDENTIFIED BACTERIOPHAGE;

EID: 0031762232     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (42)

1. Apeler, H., Gottschalk, U., Guntermann, D., Hansen, J., Massen, J., Schmidt, E., Schneider, K.H., Schneidereit, M., and Rubsamen-Waigmann, H. (1997). Expression of natural and synthetic genes encoding herpes simplex virus 1 protease in Escherichia coli and purification of the protein. Eur. J. Biochem. 247, 890-895.
2. Bonekamp, F., and Jensen, K.F. (1988). The AGG codon is translated slowly in E. coli even at very low expression levels. Nucleic Acids Res. 16, 3013-3024.
3. Bossi, L., and Roth, J.R. (1980). The influence of codon context on genetic code translation. Nature 286, 123-127.
4. Buckingham, R.H. (1990). Codon context. Experientia 46, 1126-1133.
5. Chen, G.T., and Inouye, M. (1994). Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli. Genes Dev. 8, 2641-2652.
6. Coschigano, P.W., and Magasanik, B. (1991). The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases. Mol. Cell. Biol. 11, 822-832.
7. Coustou, V., Deleu, C., Saupe, S., and Begueret, J. (1997). The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc. Natl. Acad. Sci. USA 94, 9773-9778.
8. Cullin, C., and Minvielle-Sebastia, L. (1994). Multipurpose vectors designed for the fast generation of N- or C-terminal epitope-tagged proteins. Yeast 10, 105-112.
9. Donne, D.G., Viles, J.H., Groth, D., Mehlhorn, I., James, T.L, Cohen, F.E., Prusiner, S.B., Wright, P.E., and Dyson, H.J. (1997). Structure of the recornbinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc. Natl. Acad. Sci. USA, 94, 13452-13457.
10. Ford, C.F., Suominen, I., and Glatz, C.E. (1991). Fusion tails for the recovery and purification of recornbinant proteins. Protein. Expr. Purif. 2, 95-107.
11. Gietz, D., St. Jean, A., Woods, R.A., and Schiestl, R.H. (1992). Improved method for high efficiency transformation of intact yeast cells. Nucl. Acids Res. 20, 1425.
12. Gursky, Y.G., and Beabealashvilli, R.Sh. (1994). The increase in gene expression induced by introduction of rare codons into the C terminus of the template. Gene 148, 15-21.
13. Harrison, P.M., Bamborough, P., Daggett, V., Prusiner, S.B., and Cohen, F.E. (1997). The prion folding problem. Curr. Opin. Struct. Biol. 7, 53-59.
14. Hernan, R.A., Hui, H.L., Andracki, M.E., Noble, R.W., Sugar, S.G., Walder, J.A., and Walder, R.Y. (1992). Human hemoglobin expression in Escherichia coli: importance of optimal codon usage. Biochemistry 31, 8619-8628.
15. Norwich, A.L., and Weissman, J.S. (1997). Deadly conformations-protein misfolding in prion disease. Cell 89, 499-510.
16. Ikemura, T. (1981). Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes. J. Mol. Biol, 146, 1-21.
17. Irwin, B., Heck, J.D., and Hatfield, G.W. (1995). Codon pair utilization biases influence translational elongation step times. J. Biol. Chem. 270, 22801-22806.
18. Kane, J.F. (1995). Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 6, 494-500.
19. Kurland, C. (1996). Errors of heterologous protein expression. Curr. Opin. Biotechnol. 7, 489-493.
20. Lacroute, F. (1971). Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast. J. Bacteriol. 106, 519-522.
21. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
22. LaVallie, E.R., and McCoy, J.M. (1995). Gene fusion expression systems in Escherichia coli. Curr. Opin. Biotechnol. 6, 501-506.
23. Ledent, P., Duez, C., Vanhove, M., Lejeune, A., Fonze, E., Charlier, P., Rhazi-Filali, F., Thamm, I., Guillaume, G., Samyn, B., Devreese, B., Van Beeumen, J., Lamotte-Brasseur, J., and Frere, J.M. (1997). Unexpected influence of a C-terminal-fused Histag on the processing of an enzyme and on the kinetic and folding parameters. FEBS Letters 413, 194-196.
24. Lindquist, S. (1997). Mad cows meet psi-chotic yeast: the expansion of the prion hypothesis. Cell 89, 495-498.
25. Lipman, D.J., and Wilbur, W.J. (1983). Contextual constraints on synonymous codon choice. J. Mol. Biol. 163, 363-376.
26. Nilsson, B., and Anderson, S. (1991). Proper and improper folding of proteins in the cellular environment. Annu. Rev. Microbiol. 45, 607-635.
27. Maniatis, T., Fritsch, E.F., and Sambrook, J. (1982). Molecular Cloning: A Laboratory Manual. (Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press).
28. Makrides, S.C. (1996). Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60, 512-538.
29. Masison, D.C., Maddelein, M.L., and Wickner, R.B. (1997). The prion model for [URE3] of yeast; spontaneous generation and requirements for propagation. Proc. Natl. Acad. Sci. USA 94, 12503-12508.
30. Misra, R., and Reeves, P. (1985). Intermediates in the synthesis of TolC protein include an incomplete peptide stalled at a rare Arg codon. Eur J. Biochem. 152, 151-155.
31. Perlak, F.J., Fuchs, R.L., Dean, D.A., McPherson, S.L., and Fischhoff, D.A. (1991). Modification of the coding sequence enhances plant expression of insect control protein genes. Proc. Natl. Acad, Sci. USA 88, 3324-3328.
32. Prusiner, S.B. (1996). Molecular biology and pathogenesis of prion diseases. Trends Biochem. Sci. 21, 482-487.
33. Prusiner, S.B., Scott, M.R., DeArmond, S.J. and Cohen, F.E. (1998). Prion protein biology. Cell 93, 337-348.
34. Riek, R. Hornemann, S., Wider, G., Glockshuber, R., and Wüthrich, K. (1997). NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Letters 413, 282-288.
35. Rose, D.M., Winston, F., and Bieter, P. (1990). Methods in Yeast Genetics. A Laboratory Course Manual. (Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press).
36. Rouwendal, G.J., Mendes, O., Wolbert, E.J., and Douwe de Boer, A. (1997). Enhanced expression in tobacco of the gene encod- ing green fluorescent protein by modification of its codon usage. Plant. Mol. Biol. 33, 989-999.
37. Sharp, P.M., Tuohy, T.M., and Mosurski, K.R. (1986). Codon usage in yeast: cluster analysis clearly differentiates highly and lowly expressed genes. Nucleic Acids Res. 14, 5125-5143.
38. Shpaer, E.G. (1986). Constraints on codon context in Escherichia coli genes. Their possible role in modulating the efficiency of translation. J. Mol. Biol. 188, 555-564.
39. Smith, D.W. (1996). Problems of translating heterofogous genes in expression systems: the role of tRNA. Biotechnol. Prog. 12, 417-422.
40. Spanjaard, R.A., and van Duin, J. (1988). Translation of the sequence AGG-AGG yields 50% ribosomal frameshift. Proc. Natl. Acad. Sci. USA 85, 7967-7971.
41. Weissmann, C. (1996). Molecular biology of transmissible spongiform encephalopathies. FEBS Letters. 389, 3-11.
42. Wickner, R.B. (1996). Prions and RNA viruses of Saccharomyces cerevisiae. Annu. Rev. Genet. 30, 109-139.