Co-expression of the small heat shock protein, Lo18, with β-glucosidase in Escherichia coli improves solubilization and reveals various associations with overproduced heterologous protein, GroEL/ES
Co-expression of the small heat shock protein, Lo18, with β-glucosidase in Escherichia coli improves solubilization and reveals various associations with overproduced heterologous protein, GroEL/ES
复制标题
DOI：
10.1007/s10529-012-0854-2
复制
发表时间：
2012-01
影响因子：
2.7
通讯作者：
Florian Ronez;N. Desroche;P. Arbault;J. Guzzo
中科院分区：
文献类型：
--
作者：
Florian Ronez;N. Desroche;P. Arbault;J. Guzzo
我们开发了一个新的系统，以提高可溶性蛋白的过量生产在E。大肠杆菌中的一个质粒编码的小热休克蛋白，Lo 18，来自乳酸菌酒酒球菌。并与另一种基于E.大肠杆菌通用伴侣GroEL/ES.构建了一个编码β-葡萄糖苷酶的相容性质粒，用于该酶的过量生产和聚集。与Lo 18的共表达导致可溶性β-葡糖苷酶水平的增加，与GroEL/ES共表达系统中获得的水平相似。Lo 18被发现优先在不溶性馏分，与聚集的酶。相比之下，GroEL/ES在可溶性级分中更丰富。
We developed a new system to improve the overproduction of soluble proteins inE. colibased on a plasmid encoding the small heat-shock protein, Lo18, derived from the lactic acid bacteriumOenococcus oeni. The efficiency of this system was compared with that of another system based on production of theE. coliuniversal chaperone GroEL/ES. A compatible plasmid encoding β-glucosidase was constructed for the overproduction and aggregation of this enzyme. Co-expression with Lo18 resulted in an increase in soluble β-glucosidase levels similar to that obtained in the GroEL/ES co-expression system. Lo18 was found preferentially in the insoluble fraction, associated with aggregated enzyme. By contrast, GroEL/ES was more abundant in the soluble fraction.