Earticle

초록

영어

Recombinant protein is often expressed as non-functional and aggregated form by protein misfolding in E. coli. Protein folding occurs co-translational and reaches a thermodynamically metastable conformation through guiding partially folded intermediates during translation process. Protein folding structure is related with protein synthesis rate regulated by translation initiation rate and elongation rate. To functional heterologous expression of recombinant proteins, ribosome traffic could be controlled to optimize for expression of functional recombinant protein. We constructed a genetic circuit to control translation initiation and elongation rates and consequently ribosome traffic can be controlled during translation process. Using this genetic circuit controlling ribosome traffic, wild type GFP and human granulocyte colony-stimulating factor (G-CSF) were functionally and solubly expressed in E. coli without modifying the primary structure. It indicates that controlling the ribosome traffic is useful for functionally expressing the recombinant protein by guiding them into native folding states and can be universal approach for functional expression of various recombinant proteins.

키워드

저자

• Byung Eun MIN [ School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, San 31, Hyoja-dong, Nam-gu, Pohang, Gyeongbuk, Korea, 790-784. ]
• Sang Woo SEO [ Department of Chemical Engineering, Pohang University of Science and Technology, San 31, Hyoja-dong, Nam-gu, Pohang, Gyeongbuk, Korea, 790-784. ]
• Gyoo Yeol JUNG [ School of Interdisciplinary Bioscience and Bioengineering and Department of Chemical Engineering, Pohang University of Science and Technology, San 31, Hyoja-dong, Nam-gu, Pohang, Gyeongbuk, Korea, 790-784. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576