General Microbiology Laboratory, Biology Department, University Tor Vergata Rome, Italy.
N Biotechnol. 2010 Dec 31;27(6):870-81. doi: 10.1016/j.nbt.2010.05.002. Epub 2010 May 9.
FtsQ is a highly conserved component of the divisome that plays a central role in the assembly of early and late cell division proteins. The biological activity of this protein is still largely unknown, but its ability to interact with many components of the divisome was described by both two-hybrid assays and co-immunoprecipitation experiments. This paper describes the behaviour of ftsQ point mutants, created by random mutagenesis without regard to their phenotype, in which FtsQ is impaired in its ability to interact with its Escherichia coli division partners. Our results allow the identification of FtsQ residues involved in the interaction with other partner proteins and the determination of the biological significance of these interactions. The knowledge derived by this study could constitute not only the basis for understanding how these proteins assemble in the divisome, but also a starting point for the design of new antibacterial drugs that disrupt the bacterial division machinery.
FtsQ 是分裂体的高度保守成分,在早期和晚期细胞分裂蛋白的组装中发挥核心作用。该蛋白的生物学活性在很大程度上仍然未知,但通过双杂交测定和共免疫沉淀实验都描述了它与分裂体许多成分相互作用的能力。本文描述了随机诱变创建的 ftsQ 点突变体的行为,这些突变体的表型没有得到关注,其中 FtsQ 与其大肠杆菌分裂伙伴相互作用的能力受损。我们的结果允许鉴定与其他伙伴蛋白相互作用的 FtsQ 残基,并确定这些相互作用的生物学意义。通过这项研究获得的知识不仅可以为了解这些蛋白质如何在分裂体中组装提供基础,还可以为设计破坏细菌分裂机制的新型抗菌药物提供起点。