James Richard, Penfold Christopher N, Moore Geoffrey R, Kleanthous Colin
Division of microbiology and infectious diseases, University Hospital, University of Nottingham, NG7 2UH, Nottingham, UK.
Biochimie. 2002 May-Jun;84(5-6):381-9. doi: 10.1016/s0300-9084(02)01450-5.
The process by which the endonuclease domain of colicin E9 is translocated across the outer membrane, the periplasmic space and the cytoplasmic membrane to reach the cytoplasm of E. coli cells, resulting in DNA degradation and cell death, is a unique event in prokaryotic biology. Although considerable information is known about the role of the BtuB outer membrane receptor, as well as the mostly periplasmic Tol proteins that are essential for the translocation process, the precise nature of the interactions between colicin E9 and these proteins remains to be elucidated. In this review, we consider our current understanding of the key events in this process, concentrating on recent findings concerning receptor-binding, translocation and the mechanism of cytotoxicity.
大肠杆菌素E9的核酸内切酶结构域穿过外膜、周质空间和细胞质膜到达大肠杆菌细胞的细胞质，导致DNA降解和细胞死亡，这一过程在原核生物学中是一个独特的事件。尽管关于BtuB外膜受体的作用以及转运过程所必需的主要位于周质的Tol蛋白已有大量信息，但大肠杆菌素E9与这些蛋白质之间相互作用的确切性质仍有待阐明。在这篇综述中,我们考虑了目前对这一过程中关键事件的理解，重点关注最近关于受体结合、转运和细胞毒性机制的研究发现.
