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Codon optimization of genes for efficient protein expression in mammalian cells by selection of only preferred human codons

Inouye, Satoshi, Sahara-Miura, Yuiko, Sato, Jun-ichi, Suzuki, Takahiro·2015·Protein Expression and Purification
DOI 10.1016/j.pep.2015.02.002
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Abstract

A simple design method for codon optimization of genes to express a heterologous protein in mammalian cells is described. Codon optimization was performed by choosing only codons preferentially used in humans and with over 60% GC content, and the method was named the "preferred human codon-optimized method." To test our simple rule for codon optimization, the preferred human codon-optimized genes for six proteins containing photoproteins (aequorin and clytin II) and luciferases (Gaussia luciferase, Renilla luciferase, and firefly luciferases from Photinus pyralis and Luciola cruciata) were chemically synthesized and transiently expressed in Chinese hamster ovary-K1 cells. All preferred human codon-optimized genes showed higher luminescence activity than the corresponding wild-type genes. Our simple design method could be used to improve protein expression in mammalian cells efficiently.

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  • Elements including relative frequencies of codon use, local and global GC composition, mRNA secondary structure stability, and presence of cryptic termination signals or splice sites are significant factors impacting protein expression.

    “elements including the relative frequencies of codon use for each amino acid, local and global GC composition, mRNA secondary structure stability, and the presence of cryptic termination signals or splice sites are significant factors impacting the degree of protein expression”

    From Codon optimization is an essential parameter for the efficient allotopic expression of mtDNA genes (2020) · cites this paper as [62]

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Research works printed but not linked: 19

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  2. Burgess-Brown, 2008, Codon optimization can improve expression of human genes in Escherichia coli: a multi-gene study, Protein Expr. Purif., 59, 94, 10.1016/j.pep.2008.01.008 · DOI
  3. Raab, 2010, The GeneOptimizer algorithm: using a sliding window approach to cope with the vast sequence space in multiparameter DNA sequence optimization, Syst. Synth. Biol., 4, 215, 10.1007/s11693-010-9062-3 · DOI
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  6. Inouye, 1985, Cloning and sequence analysis of cDNA for the luminescent protein aequorin, Proc. Natl. Acad. Sci. U.S.A., 82, 3154, 10.1073/pnas.82.10.3154 · DOI
  7. Inouye, 2008, Cloning, expression, purification and characterization of an isotype of clytin, a calcium-binding photoprotein from the luminous hydromedusa Clytia gregarium, J. Biochem., 143, 711, 10.1093/jb/mvn024 · DOI
  8. Lorenz, 1991, Isolation and expression of a cDNA encoding Renilla reniformis luciferase, Proc. Natl. Acad. Sci. U.S.A., 88, 4438, 10.1073/pnas.88.10.4438 · DOI
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  10. Tannous, 2005, Codon-optimized Gaussia luciferase cDNA for mammalian gene expression in culture and in vivo, Mol. Ther., 11, 435, 10.1016/j.ymthe.2004.10.016 · DOI
  11. Inouye, 2000, Secretional luciferase of the luminous shrimp Oplophorus gracilirostris: cDNA cloning of a novel imidazopyrazinone luciferase, FEBS Lett., 481, 19, 10.1016/S0014-5793(00)01963-3 · DOI
  12. Hall, 2012, Engineered luciferase reporter from a deep sea shrimp utilizing a novel imidazopyrazinone substrate, ACS Chem. Biol., 7, 1848, 10.1021/cb3002478 · DOI
  13. Inouye, 2013, C6-Deoxy coelenterazine analogues as an efficient substrate for glow luminescence reaction of nanoKAZ: the mutated catalytic 19kDa component of Oplophorus luciferase, Biochem. Biophys. Res. Commun., 437, 23, 10.1016/j.bbrc.2013.06.026 · DOI
  14. de Wet, 1987, Firefly luciferase gene: structure and expression in mammalian cells, Mol. Cell. Biol., 7, 725, 10.1128/MCB.7.2.725 · DOI
  15. Masuda, 1989, Cloning and sequence analysis of cDNA for luciferase of a Japanese firefly, Luciola cruciata, Gene, 77, 265, 10.1016/0378-1119(89)90074-7 · DOI
  16. Inouye, 2014, Luminescence enhancement of the catalytic 19kDa protein (KAZ) of Oplophorus luciferase by three amino acid substitutions, Biochem. Biophys. Res. Commun., 445, 157, 10.1016/j.bbrc.2014.01.133 · DOI
  17. Inouye, 2014, Unconventional secretion of the mutated 19kDa protein of Oplophorus luciferase (nanoKAZ) in mammalian cells, Biochem. Biophys. Res. Commun., 450, 1313, 10.1016/j.bbrc.2014.06.140 · DOI
  18. Suzuki, 2011, Video rate bioluminescence imaging of secretory proteins in living cells: localization, secretory frequency, and quantification, Anal. Biochem., 415, 182, 10.1016/j.ab.2011.03.039 · DOI
  19. Suzuki, 2011, Video-rate bioluminescence imaging of matrix metalloproteinase-2 secreted from a migrating cell, PLoS ONE, 6, e25243, 10.1371/journal.pone.0025243 · DOI

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Metadata

Authors
Inouye, S., Sahara-Miura, Y., Sato, J.-I., & Suzuki, T.
Venue
Protein Expression and Purification
Publisher
Elsevier BV
Published
2015-05
Volume
109
Pages
47-54
ISSN
1046-5928
DOI
10.1016/j.pep.2015.02.002
Cited by
49
References
1
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Funders
  • JSPS KAKENHI (26462828)
  • Research Foundation for Opto-Science and Technology
  • Aichi-Gakuin University

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