Enhancing functional expression of heterologous proteins through random substitution of genetic codes in the 5' coding region

Biotechnology and Bioengineering

Volumn 112, Issue 4, 2015, Pages 822-826

  Cheong, Dae Eun ^a   Ko, Kyong Cheol ^a   Han, Yunjon ^a   Jeon, Ho Geun ^a   Sung, Bong Hyun ^a   Kim, Geun Joong ^b   Choi, Jong Hyun ^a   Song, Jae Jun ^a  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^b Chonnam National University   (South Korea)

Author keywords

Aggregation prone protein; Escherichia coli; Functional expression; Synonymous codon

Indexed keywords

AMINO ACIDS; BIOINFORMATICS; ESCHERICHIA COLI; FLUORESCENCE;

5'-UNTRANSLATED REGIONS; AMINO ACID SUBSTITUTION; BIOINFORMATICS TOOLS; FUNCTIONAL EXPRESSION; HETEROLOGOUS PROTEINS; RANDOM SUBSTITUTION; SECONDARY STRUCTURES; SYNONYMOUS CODON;

PROTEINS;

CELLULASE; EXOCELLULASE; HYBRID PROTEIN; MESSENGER RNA; PROTEIN CELEDX SF301; RED FLUORESCENT PROTEIN; UNCLASSIFIED DRUG; MUTANT PROTEIN; RECOMBINANT PROTEIN;

5' UNTRANSLATED REGION; ARTICLE; CODON; CONTROLLED STUDY; ESCHERICHIA COLI; GENETIC CODE; NONHUMAN; POLYMERASE CHAIN REACTION; PROTEIN EXPRESSION; RNA STRUCTURE; BIOSYNTHESIS; GENE EXPRESSION; GENETICS; MUTAGENESIS; POINT MUTATION;

ESCHERICHIA COLI;

CELLULASES; ESCHERICHIA COLI; GENE EXPRESSION; MUTAGENESIS; MUTANT PROTEINS; POINT MUTATION; POLYMERASE CHAIN REACTION; RECOMBINANT PROTEINS;

EID: 84924081704     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.25478     Document Type: Article

References (12)

1. Edgar RC. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32(5):1792-1797.
2. Espah Borujeni A, Channarasappa AS, Salis HM. 2014. Translation rate is controlled by coupled trade-offs between site accessibility, selective RNA unfolding and sliding at upstream standby sites. Nucleic Acids Res 42(4):2646-2659.
3. Goltermann L, Borch Jensen, Bentin M. 2011. Tuning protein expression using synonymous codon libraries targeted to the 5′ mRNA coding region. Protein Eng Des Sel. 24(1-2):123-129.
4. Gonzalez de Valdivia, Isaksson EI. 2004. 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(17):5198-5205.
5. Goodman DB, Church GM, Kosuri S. 2013. Causes and effects of N-terminal codon bias in bacterial genes. Science 342(6157):475-479.
6. Gopal GJ, Kumar A. 2013. Strategies for the production of recombinant protein in Escherichia coli. Protein J 32(6):419-425.
7. Ko K-C, Han Y, Cheong D-E, Choi JH, Song JJ. 2013. Strategy for screening metagenomic resources for exocellulase activity using a robotic, high-throughput screening system. J Microbiol Methods 94(3):311-316.
8. Kozak M. 2005. Regulation of translation via mRNA structure in prokaryotes and eukaryotes. Gene 361(0):13-37.
9. Kucharova V, Skancke J, Brautaset T, Valla S. 2013. Design and optimization of short DNA sequences that can be used as 5′ fusion partners for high-level expression of heterologous genes in Escherichia coli. Appl Environ Microbiol 79(21):6655-6664.
10. Peng J, Wang W, Jiang Y, Liu M, Zhang H, Shao W. 2011. Enhanced soluble expression of a thermostable cellulase from clostridium thermocellum in Escherichia coli. Curr Microbiol 63(6):523-530.
11. Rouillard JM, Zuker M, Gulari E. 2003. OligoArray 2.0: design of oligonucleotide probes for DNA microarrays using a thermodynamic approach. Nucleic Acids Res 31(12):3057-3062.
12. Weber W, Fussenegger M. 2012. Emerging biomedical applications of synthetic biology. Nat Rev Genet 13 1:21-35.