Hale C A, de Boer P A
Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106-4960, USA.
Cell. 1997 Jan 24;88(2):175-85. doi: 10.1016/s0092-8674(00)81838-3.
FtsZ is a soluble, tubulin-like GTPase that forms a membrane-associated ring at the division site of bacterial cells. While this ring is thought to drive cell constriction, it is not well understood how it is assembled or how it affects cell wall invagination. Here we report that FtsZ binds directly to a novel integral inner membrane protein in E. coli that we call ZipA. We present genetic and morphological evidence indicating that this interaction is required for cell division, and show that a fluorescent ZipA-Gfp fusion protein is located in a ring structure at the division site, both before and during cell wall invagination. ZipA is an essential component of the division machinery, and, by binding to both FtsZ and the cytoplasmic membrane, is likely to be directly involved in the assembly and/or function of the FtsZ ring.
FtsZ是一种可溶性的、类似于微管蛋白的GTP酶，它在细菌细胞的分裂位点形成一个与膜相关的环。虽然这个环被认为驱动细胞收缩，但目前还不清楚它是如何组装的，以及它如何影响细胞壁内陷。在这里，我们报告FtsZ直接与大肠杆菌中一种新的整合内膜蛋白结合，我们将其称为ZipA。我们提供了遗传和形态学证据，表明这种相互作用是细胞分裂所必需的，并表明荧光ZipA-Gfp融合蛋白在细胞壁内陷之前和期间都位于分裂位点的环状结构中。ZipA是分裂机制的一个重要组成部分，通过与FtsZ和细胞质膜结合，可能直接参与FtsZ环的组装和/或功能。
