Institute of General Microbiology, Christian-Albrechts-Universität zu Kiel, Kiel, Germany.
Department of Microbiology, Blavatnick Institute, Harvard Medical School, Boston, MA, USA.
Sci Rep. 2020 Feb 5;10(1):1894. doi: 10.1038/s41598-020-58726-9.
Filament-forming proteins in bacteria function in stabilization and localization of proteinaceous complexes and replicons; hence they are instrumental for myriad cellular processes such as cell division and growth. Here we present two novel filament-forming proteins in cyanobacteria. Surveying cyanobacterial genomes for coiled-coil-rich proteins (CCRPs) that are predicted as putative filament-forming proteins, we observed a higher proportion of CCRPs in filamentous cyanobacteria in comparison to unicellular cyanobacteria. Using our predictions, we identified nine protein families with putative intermediate filament (IF) properties. Polymerization assays revealed four proteins that formed polymers in vitro and three proteins that formed polymers in vivo. Fm7001 from Fischerella muscicola PCC 7414 polymerized in vitro and formed filaments in vivo in several organisms. Additionally, we identified a tetratricopeptide repeat protein - All4981 - in Anabaena sp. PCC 7120 that polymerized into filaments in vitro and in vivo. All4981 interacts with known cytoskeletal proteins and is indispensable for Anabaena viability. Although it did not form filaments in vitro, Syc2039 from Synechococcus elongatus PCC 7942 assembled into filaments in vivo and a Δsyc2039 mutant was characterized by an impaired cytokinesis. Our results expand the repertoire of known prokaryotic filament-forming CCRPs and demonstrate that cyanobacterial CCRPs are involved in cell morphology, motility, cytokinesis and colony integrity.
细菌中的丝状形成蛋白在蛋白质复合物和复制子的稳定和定位中发挥作用;因此,它们对细胞分裂和生长等多种细胞过程至关重要。在这里,我们介绍了蓝细菌中的两种新型丝状形成蛋白。我们在蓝细菌基因组中调查了富含卷曲螺旋的蛋白质(CCRPs),这些蛋白质被预测为可能的丝状形成蛋白,与单细胞蓝细菌相比,丝状蓝细菌中的 CCRPs 比例更高。使用我们的预测,我们确定了九个具有中间丝(IF)特性的蛋白质家族。聚合实验表明,有四种蛋白质在体外形成聚合物,三种蛋白质在体内形成聚合物。来自 Fischerella muscicola PCC 7414 的 Fm7001 在体外聚合并在几种生物体中形成体内丝状。此外,我们在 Anabaena sp. PCC 7120 中鉴定出一种四肽重复蛋白 - All4981 -,它在体外和体内聚合形成丝状。All4981 与已知的细胞骨架蛋白相互作用,对鱼腥藻的存活是必不可少的。尽管它在体外没有形成丝状,但来自 Synechococcus elongatus PCC 7942 的 Syc2039 在体内组装成丝状,并且 Δsyc2039 突变体的细胞分裂受到损害。我们的结果扩展了已知原核丝状形成 CCRPs 的范围,并表明蓝细菌 CCRPs 参与细胞形态、运动、细胞分裂和菌落完整性。