Dalbey R E, Kuhn A, von Heijne G
Dept of Chemistry, Ohio State University, Columbus 43210, USA.
Trends Cell Biol. 1995 Oct;5(10):380-3. doi: 10.1016/s0962-8924(00)89079-0.
Protein translocation normally starts from an N-terminal signal peptide and proceeds in an N-to-C-terminal direction. However, in certain integral membrane proteins an N-terminal tail is translocated even though it is not preceded by a signal peptide. In eukaryotic cells this process involves the normal Sec-machinery. In contrast, recent studies in Escherichia coli show that translocation of such N-terminal tails occurs by a mechanism that does not appear to involve the Sec proteins and is most efficient for short tails lacking positively charged residues. These novel observations suggest that the Sec-machinery has an inherent N-to-C-terminal directionality and cannot work 'in reverse'.
蛋白质转运通常从N端信号肽开始,并沿N端到C端的方向进行。然而,在某些整合膜蛋白中,即使N端尾部之前没有信号肽,它也会发生转运。在真核细胞中,这个过程涉及正常的Sec机制。相比之下,最近对大肠杆菌的研究表明,这种N端尾部的转运是通过一种似乎不涉及Sec蛋白的机制发生的,并且对于缺乏带正电荷残基的短尾部最为有效。这些新的观察结果表明,Sec机制具有固有的N端到C端方向性,不能“反向”工作。