Influence of the second amino acid on recombinant protein expression

Protein Expression and Purification

Volumn 74, Issue 2, 2010, Pages 248-256

  Bivona, Louis ^a   Zou, Zhongcheng ^a   Stutzman, Nicole ^a   Sun, Peter D ^a  

^a NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

Author keywords

Codon usage; Escherichia coli expression system; Ig ; MRNa structure; Mutational analysis; Recombinant expression; Recombinant protein production; Second codon position

Indexed keywords

CXCL10 PROTEIN, HUMAN; GAMMA INTERFERON INDUCIBLE PROTEIN 10; IMMUNOGLOBULIN A; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; ESCHERICHIA COLI; GENETICS; HUMAN; METABOLISM; PROTEIN SYNTHESIS; START CODON;

AMINO ACID SEQUENCE; CHEMOKINE CXCL10; CODON, INITIATOR; ESCHERICHIA COLI; HUMANS; IMMUNOGLOBULIN A; PROTEIN BIOSYNTHESIS; RECOMBINANT PROTEINS;

ESCHERICHIA COLI;

EID: 77957750717     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.06.005     Document Type: Article

References (20)

1. J. Shine, and L. Dalgarno Terminal-sequence analysis of bacterial ribosomal RNA. Correlation between the 3′-terminal-polypyrimidine sequence of 16-S RNA and translational specificity of the ribosome Eur. J. Biochem. 57 1975 221 230
2. M. Kozak Initiation of translation in prokaryotes and eukaryotes Gene 234 1999 187 208
3. H. Chen, M. Bjerknes, R. Kumar, and E. Jay Determination of the optimal aligned spacing between the Shine-Dalgarno sequence and the translation initiation codon of Escherichia coli mRNAs Nucleic Acids Res. 22 1994 4953 4957
4. E.J. Gren Recognition of messenger RNA during translational initiation in Escherichia coli Biochimie 66 1984 1 29
5. S.M. O'Donnell, and G.R. Janssen The initiation codon affects ribosome binding and translational efficiency in Escherichia coli of cI mRNA with or without the 5′ untranslated leader J. Bacteriol. 183 2001 1277 1283
6. C.M. Stenström, E. Holmgren, and L.A. Isaksson Cooperative effects by the initiation codon and its flanking regions on translation initiation Gene 273 2001 259 265
7. G.D. Stormo, T.D. Schneider, and L.M. Gold Characterization of translational initiation sites in E. coli Nucleic Acids Res. 10 1982 2971 2996
8. A.C. Looman, J. Bodlaender, L.J. Comstock, D. Eaton, H.A. De Boer, and P.H. van Knippenberg Influence of the codon following the AUG initiation codon on the expression of a modified lacZ gene in Escherichia coli EMBO J. 6 1987 2489 2492
9. C.M. Stenström, H. Jin, L.L. Major, W.P. Tate, and L.A. Isaksson Codon bias at the 3′-side of the initiation codon is correlated with translation initiation efficiency in Escherichia coli Gene 263 2001 273 284
10. E. Zamora-Romo, L.R. Cruz-Vera, S. Vivanco-Domínguez, M.A. Magos-Castro, and G. Guarneros Efficient expression of gene variants that harbour AGA codons next to the initiation codon Nucleic Acids Res. 35 2007 5966 5974
11. G. Gutiérrez, L. Márquez, and A. Marín Preference for guanosine at first codon position in highly expressed Escherichia coli genes. A relationship with translational efficiency Nucleic Acids Res. 24 1996 2525 2527
12. E.I. Gonzalez de Valdivia, and L.A. Isaksson A codon window in mRNA downstream of the initiation codon where NGG codons give strongly reduced gene expression in Escherichia coli Nucleic Acids Res. 32 2004 5198 5205
13. Y. Ishihama, T. Schmidt, J. Rappsilber, M. Mann, F.U. Hartl, M.J. Kerner, and D. Frishman Protein abundance profiling of the Escherichia coli cytosol BMC Genomics 9 2008
14. I.M. Keseler, C. Bonavides-Martinez, J. Collado-Vides, S. Gama-Castro, R.P. Gunsalus, D.A. Johnson, M. Krummenacker, L.M. Nolan, S. Paley, I.T. Paulsen, M. Peralta-Gil, A. Santos-Zavaleta, A.G. Shearer, and P.D. Karp EcoCyc: a comprehensive view of Escherichia coli biology Nucleic Acids Res. 37 2009 464 470
15. H. Tegel, S. Tourle, J. Ottonson, and A. Persson Increased levels of recombinant human proteins with the Escherichia coli strain Rosetta (DE3) Protein Expr. Purif. 69 2010 159 167
16. W. Zhang, W. Xiao, H. Wei, J. Zhang, and Z. Tian MRNA secondary structure at start AUG codon is a key limiting factor for human protein expression in Escherichia coli Biochem. Biophys. Res. Commun. 349 2006 69 78
17. A.G. Nackley, S.A. Shabalina, I.E. Tchivileva, K. Satterfield, O. Korchynskyi, S.S. Makarov, W. Maixner, and L. Diatchenko Human catechol-O-methyltransferase haplotypes modulate protein expression by altering mRNA secondary structure Science 314 2006 1930 1933
18. A. Tats, M. Remm, and T. Tenson Highly expressed proteins have an increased frequency of alanine in the second amino acid position BMC Genomics 7 2006
19. A. Bachmair, D. Finley, and A. Varshavsky In vivo half life of a protein is a function of its amino terminal residue Science 234 1986 179 186
20. A. Varshavsky The N-end rule: functions, mysteries, uses Proc. Natl. Acad. Sci. 93 1996 12142 12149