Cui Jing, Wang Guangqiang, Chen Haiqin, Chen Jie, Gu Zhennan, Chen Wei, Zhang Hao
Wei Sheng Wu Xue Bao. 2015 Feb 4;55(2):198-204.
We used 50-amino acid-long peptides from the N-terminus of 4 different non-classically secreted proteins to study the secretion efficiency of Bacillus subtilis LipaseA via non-classical secretion pathway.
We amplified the coding sequences (CDs) of LipaseA and N-terminus of non-classically secreted proteins, constructed 8 fusion protein expression vectors containing both LipaseA CD and different secretion signal peptide and transformed them into B. subtilis WB800. Secretion efficiency of these fusion proteins was analyzed by enzyme activity, SDS-PAGE and Western-Blot.
Recombinant LipaseA containing coding sequences of PdhA or N-terminus of SodA and Eno as secretion signals was efficiently secreted.
Parts of non-classically secreted proteins or N-terminus (50 amino acids) could guide LipaseA protein secretion.
我们使用来自4种不同非经典分泌蛋白N端的50个氨基酸长的肽段，来研究枯草芽孢杆菌脂肪酶A通过非经典分泌途径的分泌效率。
我们扩增了脂肪酶A和非经典分泌蛋白N端的编码序列（CDs），构建了8个包含脂肪酶A编码序列和不同分泌信号肽的融合蛋白表达载体，并将它们转化到枯草芽孢杆菌WB800中。通过酶活性、SDS-PAGE和Western-Blot分析这些融合蛋白的分泌效率。
含有PdhA编码序列或SodA和Eno的N端作为分泌信号的重组脂肪酶A被有效分泌。
部分非经典分泌蛋白或N端（50个氨基酸）可以指导脂肪酶A蛋白的分泌。
