4.2 Article

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

Journal

PROTEIN EXPRESSION AND PURIFICATION
Volume 109, Issue -, Pages 47-54

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2015.02.002

Keywords

Codon optimization; Synthetic gene; Luciferase; Photoprotein; Reporter gene

Funding

  1. JSPS KAKENHI Grant [26462828]
  2. Research Foundation for Opto-Science and Technology
  3. Aichi-Gakuin University
  4. Grants-in-Aid for Scientific Research [26462828] Funding Source: KAKEN

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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. (c) 2015 Elsevier Inc. All rights reserved.

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