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Expression of a Highly Toxic Protein Bax in Escherichia coli by Attachment of a Leader Peptide Derived from the GroES Cochaperone

机译：通过附着从GroES伴侣蛋白衍生的前导肽在大肠杆菌中表达高毒性蛋白Bax

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摘要

Attempts to express a truncated form of murine Bax in the periplasm by using an expression vector that attached the OmpA signal sequence to the protein failed to alleviate this toxicity. In contrast, attachment of a peptide based on a portion of the E. coli cochaperone GroES reduced Bax’s toxicity significantly and allowed good expression. The peptide, which was attached to the N-terminus, included the amino acid sequence of the mobile loop of GroES that has been demonstrated to interact with the chaperonin, GroEL. Under normal growth conditions, expression of this construct was still toxic, but generated a small amount of detectable recombinant Bax. However, when cells were grown in the presence of 2% ethanol, which stimulated overproduction of the molecular chaperones GroEL and DnaK, toxicity was reduced and good overexpression occurred. Two-dimensional gel electrophoresis analysis showed that approximately 15-fold more GroES-loop-Bax was produced under these conditions than under standard conditions and that GroEL and DnaK were elevated approximately 3-fold.
机译：试图通过使用将OmpA信号序列连接到蛋白质的表达载体在周质中表达截短形式的鼠Bax未能减轻这种毒性。相反，基于一部分大肠杆菌伴侣蛋白GroES的肽的附着可显着降低Bax的毒性并实现良好的表达。附着在N端的肽段包含GroES流动环的氨基酸序列，该序列已被证明与伴侣蛋白GroEL相互作用。在正常的生长条件下，该构建体的表达仍然是有毒的，但是会产生少量可检测的重组Bax。但是，当细胞在2％乙醇存在下生长时，刺激了分子伴侣分子GroEL和DnaK的过量生产，毒性降低了，并且发生了良好的过表达。二维凝胶电泳分析表明，在这些条件下产生的GroES-loop-Bax比标准条件下多大约15倍，并且GroEL和DnaK升高了大约3倍。

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