Bacterial Division Proteins FtsZ and ZipA Induce Vesicle Shrinkage and Cell Membrane Invagination
Bacterial Division Proteins FtsZ and ZipA Induce Vesicle Shrinkage and Cell Membrane Invagination
复制标题
DOI：
10.1074/jbc.m113.491688
复制
发表时间：
2013-09-13
影响因子：
4.8
通讯作者：
Vicente, Miguel
中科院分区：
文献类型：
--
作者：
Cabre, Elisa J.;Sanchez-Gorostiaga, Alicia;Vicente, Miguel
当主要的细胞分裂蛋白FtsZ在GTP存在下聚合时，含有原环锚定ZipA蛋白的可渗透小泡缩小。收缩，类似于细胞质膜的收缩，在ZipA浓度高于细胞中发现的浓度时发生，并受FtsZ聚合物的动态调节。在体内，过量的ZipA会在细胞质内产生多层膜包涵体，并导致膜作为通透性屏障的功能丧失。在阻止分隔的水平上过量生产ZipA伴随着FtsZ和另外两个分裂蛋白FTSA和FtsN从潜在的分隔位置转移到与ZipA共同定位在膜附近的簇。结果表明，在细菌和囊泡中都可以观察到参与细胞分裂的特定元件介导的基本收缩事件。
Permeable vesicles containing the proto-ring anchoring ZipA protein shrink when FtsZ, the main cell division protein, polymerizes in the presence of GTP. Shrinkage, resembling the constriction of the cytoplasmic membrane, occurs at ZipA densities higher than those found in the cell and is modulated by the dynamics of the FtsZ polymer. In vivo, an excess of ZipA generates multilayered membrane inclusions within the cytoplasm and causes the loss of the membrane function as a permeability barrier. Overproduction of ZipA at levels that block septation is accompanied by the displacement of FtsZ and two additional division proteins, FtsA and FtsN, from potential septation sites to clusters that colocalize with ZipA near the membrane. The results show that elementary constriction events mediated by defined elements involved in cell division can be evidenced both in bacteria and in vesicles.