Feucht Andrea, Errington Jeffery
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Microbiology (Reading). 2005 Jun;151(Pt 6):2053-2064. doi: 10.1099/mic.0.27899-0.
A key event in cytokinesis in bacteria is the assembly of the essential division protein FtsZ into ring-like structures at the nascent division site. FtsZ is the prokaryotic homologue of tubulin, and is found in nearly all bacteria. In vitro, FtsZ polymerizes in the presence of GTP to form higher-ordered polymers. FtsZ consists of two domains, with the GTP-binding site located in the N-terminal domain. The less-conserved C-terminal domain contains residues important for GTP hydrolysis, but its overall function is still unclear. This paper reports the development of a simple strategy to generate mutations in the essential division gene ftsZ. Nine novel and viable ftsZ mutants of Bacillus subtilis are described. Eight of the mutations would affect the C-terminus of FtsZ. The collection of mutants exhibits a range of morphological phenotypes, ranging from normal to highly filamentous cells; some produce minicells, or divide in a twisted configuration; one mutation has a temperature-sensitive effect specifically impairing sporulation. The sites of the amino acid changes generated by the mutations could be informative about FtsZ function and its protein-protein interactions.
细菌胞质分裂中的一个关键事件是必需的分裂蛋白FtsZ在新生分裂位点组装成环状结构。FtsZ是微管蛋白的原核同源物，几乎存在于所有细菌中。在体外，FtsZ在GTP存在下聚合形成高阶聚合物。FtsZ由两个结构域组成，GTP结合位点位于N端结构域。保守性较低的C端结构域包含对GTP水解重要的残基，但其整体功能仍不清楚。本文报道了一种在必需分裂基因ftsZ中产生突变的简单策略的开发。描述了枯草芽孢杆菌的9个新的且可行的ftsZ突变体。其中8个突变会影响FtsZ的C端。这些突变体的集合表现出一系列形态表型，从正常细胞到高度丝状细胞；一些产生微小细胞，或以扭曲的形态分裂；一个突变具有温度敏感效应，特别损害孢子形成。由这些突变产生的氨基酸变化位点可能有助于了解FtsZ的功能及其蛋白质-蛋白质相互作用。
