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A favorable solubility partner for the recombinant expression of streptavidin

机译：链霉亲和素重组表达的良好溶解性伴侣

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摘要

Recombinant streptavidin is extremely difficult to express at high levels in the cytoplasm of Escherichia coli without the formation of inclusion bodies. Fusing a solubility enhancing partner to an aggregation prone protein is a widely used tool to circumvent inclusion body formation. Here, we use streptavidin as a target protein to test the properties of N-terminal fragments of translation initiation factor IF2 from E coli as a solubility partner. Domain I (residue 1-158) of IF2 is superior to the well-established solubility partners maltose-binding protein (MBP) and NusA for soluble expression of active streptavidin. The number of active streptavidin molecules isolated by chromatography is increased threefold when domain I is used as solubility partner as compared to MBP or NusA. The relatively small size, high expressivity, and extreme solubility make domain I of IF2 an ideal partner for streptavidin and may also prevent other recombinant proteins such as ScFv antibodies from being expressed as insoluble aggregates in the cytoplasm of E coli. (C) 2003 Elsevier Inc. All rights reserved. [References: 20]
机译：重组链霉亲和素在不形成包涵体的情况下很难在大肠杆菌的细胞质中高水平表达。将易溶性增强伴侣与易于聚集的蛋白质融合在一起是一种广泛使用的工具，可避免包涵体的形成。在这里，我们使用链霉亲和素作为靶蛋白来测试作为可溶性伴侣的大肠杆菌翻译起始因子IF2的N末端片段的特性。 IF2的结构域I（残基1-158）在可溶性链霉亲和素的表达方面优于公认的溶解性伴侣麦芽糖结合蛋白（MBP）和NusA。与MBP或NusA相比，将结构域I用作溶解性伴侣时，通过色谱法分离的活性链霉亲和素分子的数量增加了三倍。相对较小的尺寸，高表达性和极高的溶解度使IF2的结构域I成为抗生蛋白链菌素的理想伴侣，还可能阻止其他重组蛋白（例如ScFv抗体）在大肠杆菌的细胞质中表达为不溶性聚集体。 （C）2003 Elsevier Inc.保留所有权利。 [参考：20]

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