Translocation of alkaline phosphatase via the Tat pathway in Escherichia coli

• Main Authors: Guan-Jie Huang, 黃冠傑
• Other Authors: 林松池
• Format: Others
• Language: zh-TW
• Published: 2006
• Online Access: http://ndltd.ncl.edu.tw/handle/17488048907740295783

碩士 === 國立中興大學 === 化學工程學系所 === 94 === Twin-arginine translocation pathway is a novel system for the secretion of proteins into the periplasm of Gram-negative bacteria such as Escherichia coli. Sec pathway has long been exploited for protein secretion due to its well studied mechanism and high translocation efficiency. However, it is not capable of translocating folded proteins. On the contrary, it has recently been shown that the twin-arginine translocation (TAT) pathway is capable of translocating fully folded, disulfided proteins. In light of the potential applications of protein secretion for the production of recombinant proteins on industrial scales, a systematic study comparing the Sec pathway and Tat pathway for the secretion of a dimeric, disulfided protein, alkaline phosphatase, was conducted. In this study, it is demonstrated the Sec pathway is a superior system for the secretion of the model protein. It is also shown that the co-expression of TorD does not enhance the translocation of alkaline phosphatase via the Tat pathway in Escherichia coli.