MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.
Curr Opin Microbiol. 2013 Dec;16(6):745-51. doi: 10.1016/j.mib.2013.09.003. Epub 2013 Oct 1.
The divisome and elongasome are bacterial protein complexes responsible for peptidoglycan (PG) synthesis during cell division and elongation, respectively. We review several lines of evidence, arguing for a shared evolutionary past of the divisome and elongasome. Both integrate closely related penicillin-binding proteins (PBPs) for PG synthesis, use proteins of the RodA/FtsW (SEDS, shape, elongation, division and sporulation) family for Lipid II export and interact with MraY/Mur proteins for Lipid II synthesis. It was recently shown that the actin-like protein FtsA of the divisome polymerises on membranes, adding another parallel, since membrane-associated filaments of the bacterial actin MreB guide the elongasome. Given these similarities, it seems plausible to conclude that the elongasome is a modified version of the divisome, without the membrane-constricting FtsZ-ring and its associated machinery on the inside.
分裂体和伸长体是细菌蛋白复合物，分别负责细胞分裂和伸长过程中的肽聚糖（PG）合成。我们回顾了几条证据，认为分裂体和伸长体具有共同的进化史。两者都整合了密切相关的青霉素结合蛋白（PBPs）用于 PG 合成，使用 RodA/FtsW（SEDS，形状，伸长，分裂和孢子形成）家族的蛋白质进行脂质 II 输出，并与 MraY/Mur 蛋白相互作用进行脂质 II 合成。最近的研究表明，分裂体中的肌动蛋白样蛋白 FtsA 在膜上聚合，增加了另一个平行现象，因为细菌肌动蛋白 MreB 的膜相关丝状体指导伸长体。鉴于这些相似之处，似乎可以合理地得出结论，即伸长体是分裂体的一种修饰形式，内部没有限制膜的 FtsZ 环及其相关机制。
