Bramhill D
Department of Enzymology, Merck Research Laboratories, Rahway, New Jersey 07065-0900, USA.
Annu Rev Cell Dev Biol. 1997;13:395-424. doi: 10.1146/annurev.cellbio.13.1.395.
Bacteria usually divide by building a central septum across the middle of the cell. This review focuses on recent results indicating that the tubulin-like FtsZ protein plays a central role in cytokinesis as a major component of a contractile cytoskeleton. Assembly of this cytoskeletal element abutting the membrane is a key point for regulation. The characterization of FtsZ homologues in Mycoplasmas, Archaea, and chloroplasts implies that the constriction mechanism is conserved and that FtsZ can constrict in the absence of peptidoglycan synthesis. In most Eubacteria, the internal cytoskeleton must also regulate synthesis of septal peptidoglycan. The Escherichia coli septum-specific penicillin-binding protein 3 (PBP3) forms a complex with other enzymes involved in murein metabolism, suggesting a centrally located transmembrane complex capable of splicing multiple new strands of peptidoglycan into the cell wall. Important questions remain about the spatial and temporal control of bacterial division.
细菌通常通过在细胞中部构建一个中央隔膜来进行分裂。本综述重点关注近期的研究结果，这些结果表明，微管蛋白样FtsZ蛋白作为收缩性细胞骨架的主要成分，在胞质分裂中起着核心作用。这种与膜相邻的细胞骨架元件的组装是调控的关键环节。对支原体、古细菌和叶绿体中FtsZ同源物的表征表明，收缩机制是保守的，并且FtsZ在没有肽聚糖合成的情况下也能收缩。在大多数真细菌中，内部细胞骨架还必须调节隔膜肽聚糖的合成。大肠杆菌隔膜特异性青霉素结合蛋白3（PBP3）与其他参与胞壁质代谢的酶形成复合物，这表明存在一个位于中央的跨膜复合物，能够将多条新的肽聚糖链拼接进细胞壁。关于细菌分裂的空间和时间控制，仍存在重要问题。
