期刊
BIOTECHNOLOGY JOURNAL
卷 6, 期 6, 页码 686-699出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/biot.201000335
关键词
Cysteine; Kunitz inhibitors; Oxidative protein folding; Redox compartmentalization; Thiols
资金
- Universidad de la Republica [CSIC-I+D_407]
- Agencia Nacional de Investigacion e Innovacion [BE_INI_2008_462, BE_POS_2009_1206]
Disulfide-bond formation is a major post-translational modification and is essential for protein folding, stability, and function. This is especially true for secreted proteins, many of which possess great potential for biotechnological applications. Focusing on the use of Escherichia coli for the production of this class of proteins, we describe the mechanisms that maintain redox compartmentalization in the cell, with an emphasis on those that promote the formation and isomerization of disulfide bonds in the bacterial periplasm, while presenting parallel pathways in the eukaryotic endoplasmic reticulum. Based on these concepts, we review the use of E. coli as a cell factory for the production of heterologous disulfide-containing proteins using either peri-or cytoplasmic expression and, in particular, how these compartments can be tuned to improve the yield of correctly folded recombinant proteins. Finally, we describe a few examples of the production of small disulfide-rich proteins (protease inhibitors) to illustrate how soluble, active, and fully oxidized recombinants may be successfully obtained upon peri-or cytoplasmic expression in E. coli.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据