An efficient translational termination of human erythropoietin in Escherichia coli by altering the base following the stop codon |
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Authors: | Sang Hyeon Kang Sang Taek Jung Taek Jin Kang Ryang Guk Kim Sang Hyuk Suh Ji Hyoung Woo Eun Yeol Lee Cha Yong Choi |
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Institution: | (1) School of Chemical Engineering, Korea;(2) Interdisciplinary Program for Biochemical Engineering and Biotechnology, College of Engineering, Seoul National University, Seoul, 151-742, Korea;(3) Department of Food Science and Technology, College of Engineering, Kyungsung University, Pusan, 608-736, Korea |
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Abstract: | Each of the four nucleotides (A, C, G and T) was introduced as the base following the stop codon to investigate the effect of this fourth base on translational termination efficiency during the heterologous expression of human erythropoietin (hEPO) in E. coli. The efficiency of peptide chain termination in E. coli was markedly dependent on the fourth base. The choice of the fourth base was crucial to prevent the expression of undesirable proteins due to the translational infidelity such as frameshifting and stop codon read-through, and translational termination efficiency could be improved with adenosine as the fourth base. |
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Keywords: | erythropoietin Escherichia coli termination efficiency translational stop codon |
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