Efficient expression of haloarchaeal nucleoside diphosphate kinase via strong porin promoter in moderately halophilic bacteria.
Efficient expression of haloarchaeal nucleoside diphosphate kinase via strong porin promoter in moderately halophilic bacteria.
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DOI：
10.2174/092986606777145760
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发表时间：
2006-05
影响因子：
1.6
通讯作者：
C. Nagayoshi;H. Tokunaga;Aya Hayashi;Hiroaki Harazono;K. Hamasaki;Ayumi Ando;M. Tokunaga
中科院分区：
文献类型：
--
作者：
C. Nagayoshi;H. Tokunaga;Aya Hayashi;Hiroaki Harazono;K. Hamasaki;Ayumi Ando;M. Tokunaga
来自极端嗜盐古细菌的酶需要高浓度的盐才能正确折叠，因此在大肠杆菌中表达为未折叠和无活性形式。中度嗜盐菌，积累蛋白质稳定剂，即，相容性溶质是用于重组生产异源蛋白的有吸引力的宿主细胞，因为这样的蛋白稳定剂可以帮助表达蛋白的折叠。在这里，我们成功地高效表达和纯化的重组嗜盐古菌核苷二磷酸激酶（HsNDK）的同质性在中度嗜盐菌使用新分离的强孔蛋白启动子。
Enzymes from extremely halophilic archaea require high concentration of salts for their proper folding and consequently are expressed as an unfolded and inactive form in Escherichia coli. Moderate halophile, which accumulates protein stabilizers, i.e., compatible solutes, is an attractive host cell for the recombinant production of heterologous proteins, since such protein stabilizers may help folding of expressed proteins. Here, we succeeded in efficient expression and purification to homogeneity of recombinant haloarchaeal nucleoside diphosphate kinase (HsNDK) in moderate halophile using newly isolated strong porin promoter.