MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Curr Biol. 2021 May 24;31(10):R542-R546. doi: 10.1016/j.cub.2021.03.011.
All living cells depend on the intricate organization of molecular components in space and time. Although this notion was historically based on eukaryotic cells, with their structured intracellular architecture and cellular morphologies, it is now recognized that prokaryotes (that is, bacteria and archaea) also possess complex structures. A cytoskeleton is a network of intracellular protein filaments that play a structural or mechanical role (such as scaffolding, pushing, or pulling) in the spatiotemporal organization of cellular processes. Polymerization of protein monomers in a roughly linear fashion into filaments represents an effective means to establish long-range spatial order by bridging the gap between nanometer-sized molecules and micron-sized cells. It is now evident that bacteria and archaea possess numerous kinds of cytoskeletal proteins, including prokaryotic homologues of the eukaryotic actins, tubulins, and intermediate filaments, as well as other types that have been found primarily or exclusively in prokaryotes (Table 1). Understanding the diverse functions and mechanisms of the rapidly growing universe of prokaryotic cytoskeletal proteins will not only advance prokaryotic cell biology and reveal evolutionary principles, but also open up new avenues for the development of anti-microbial agents, de novo protein design, and the construction of minimal and synthetic cells.
所有活细胞都依赖于分子成分在空间和时间上的精细组织。尽管这一概念在历史上是基于具有结构细胞内结构和细胞形态的真核细胞,但现在已经认识到原核生物(即细菌和古菌)也具有复杂的结构。细胞骨架是细胞内蛋白丝的网络,在细胞过程的时空组织中发挥结构或机械作用(如支架、推动或拉动)。蛋白单体以大致线性的方式聚合成长丝,这是通过在纳米级分子和微米级细胞之间架起桥梁来建立长程空间秩序的有效手段。现在已经很明显,细菌和古菌拥有多种细胞骨架蛋白,包括真核生物肌动蛋白、微管蛋白和中间丝的原核同源物,以及其他主要或仅在原核生物中发现的类型(表 1)。了解快速增长的原核细胞骨架蛋白的多种功能和机制,不仅将推进原核细胞生物学并揭示进化原则,还将为开发抗菌剂、从头设计蛋白质以及构建最小和合成细胞开辟新途径。