Fahnestock S R, Fisher K E
J Bacteriol. 1986 Mar;165(3):796-804. doi: 10.1128/jb.165.3.796-804.1986.
Gene fusions of DNA sequences encoding protein A from Staphylococcus aureus (spa) with expression elements from an alpha-amylase gene from Bacillus amyloliquefaciens (amyEBamP) directed the synthesis and efficient secretion of protein A in Bacillus subtilis. The fusions were established on multicopy pUB110-based plasmid vectors, in contrast to the intact spa gene, which could not be stably established on plasmids in B. subtilis. Some of the resulting B. subtilis strains secreted protein A at levels in excess of 1 g/liter, demonstrating that a foreign protein encoded by an engineered gene can be secreted by B. subtilis at levels comparable to endogenous exoproteins.
编码来自金黄色葡萄球菌的蛋白A（spa）的DNA序列与来自解淀粉芽孢杆菌的α-淀粉酶基因（amyEBamP）的表达元件的基因融合，指导了枯草芽孢杆菌中蛋白A的合成和有效分泌。与完整的spa基因不同，这些融合体是在基于多拷贝pUB110的质粒载体上构建的，完整的spa基因无法在枯草芽孢杆菌的质粒上稳定构建。一些所得的枯草芽孢杆菌菌株分泌蛋白A的水平超过1克/升，这表明工程基因编码的外源蛋白可以被枯草芽孢杆菌以与内源性外分泌蛋白相当的水平分泌。
