关键词: Actin Cell wall Cytoskeleton Division machinery Divisome Peptidoglycan Septation Tubulin

Mesh : Bacterial Proteins / metabolism genetics Cytoskeletal Proteins / metabolism genetics Cell Division Escherichia coli / metabolism genetics Escherichia coli Proteins / metabolism genetics Bacteria / metabolism genetics

来  源:   DOI:10.1007/978-3-031-58843-3_4

Abstract:
Across living organisms, division is necessary for cell survival and passing heritable information to the next generation. For this reason, cell division is highly conserved among eukaryotes and prokaryotes. Among the most highly conserved cell division proteins in eukaryotes are tubulin and actin. Tubulin polymerizes to form microtubules, which assemble into cytoskeletal structures in eukaryotes, such as the mitotic spindle that pulls chromatids apart during mitosis. Actin polymerizes to form a morphological framework for the eukaryotic cell, or cytoskeleton, that undergoes reorganization during mitosis. In prokaryotes, two of the most highly conserved cell division proteins are the tubulin homolog FtsZ and the actin homolog FtsA. In this chapter, the functions of the essential bacterial cell division proteins FtsZ and FtsA and their roles in assembly of the divisome at the septum, the site of cell division, will be discussed. In most bacteria, including Escherichia coli, the tubulin homolog FtsZ polymerizes at midcell, and this step is crucial for recruitment of many other proteins to the division site. For this reason, both FtsZ abundance and polymerization are tightly regulated by a variety of proteins. The actin-like FtsA protein polymerizes and tethers FtsZ polymers to the cytoplasmic membrane. Additionally, FtsA interacts with later stage cell division proteins, which are essential for division and for building the new cell wall at the septum. Recent studies have investigated how actin-like polymerization of FtsA on the lipid membrane may impact division, and we will discuss this and other ways that division in bacteria is regulated through FtsZ and FtsA.
摘要:
在生物体中,分裂是细胞存活和将可遗传信息传递给下一代所必需的。出于这个原因,细胞分裂在真核生物和原核生物中高度保守。真核生物中最高度保守的细胞分裂蛋白是微管蛋白和肌动蛋白。微管蛋白聚合形成微管,在真核生物中组装成细胞骨架结构,例如有丝分裂纺锤体在有丝分裂期间将染色单体分开。肌动蛋白聚合形成真核细胞的形态框架,或细胞骨架,在有丝分裂期间经历重组。在原核生物中,两种最高度保守的细胞分裂蛋白是微管蛋白同源物FtsZ和肌动蛋白同源物FtsA。在这一章中,细菌细胞分裂必需蛋白FtsZ和FtsA的功能及其在隔膜分裂体组装中的作用,细胞分裂的部位,将讨论。在大多数细菌中,包括大肠杆菌,微管蛋白同源物FtsZ在中细胞聚合,这一步对于许多其他蛋白质募集到分裂位点至关重要。出于这个原因,FtsZ丰度和聚合都受到多种蛋白质的严格调控。肌动蛋白样FtsA蛋白聚合并将FtsZ聚合物束缚到细胞质膜上。此外,FtsA与后期细胞分裂蛋白相互作用,这对于分裂和在隔膜处建立新的细胞壁至关重要。最近的研究已经调查了FtsA在脂质膜上的肌动蛋白样聚合如何影响分裂,我们将讨论通过FtsZ和FtsA调节细菌分裂的这种方式和其他方式。
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