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分裂酶是大肠杆菌和新月柄杆菌中的一种自我增强机器。

The divisome is a self-enhancing machine in Escherichia coli and Caulobacter crescentus.

机构信息

Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, Hubei, China.

Key Laboratory of Polar Environment Monitoring and Public Governance (Ministry of Education), Wuhan University, Wuhan, China.

出版信息

Nat Commun. 2024 Sep 18;15(1):8198. doi: 10.1038/s41467-024-52217-5.

Abstract

During bacterial cytokinesis, polymers of the bacterial tubulin FtsZ coalesce into the Z ring to orchestrate divisome assembly and septal cell wall synthesis. Previous studies have found that Z ring condensation and stability is critical for successful cell division. However, how FtsZ filaments condense into a Z ring remains enigmatic and whether septal cell wall synthesis can feedback to the Z ring has not been investigated. Here, we show that FtsZ-associated proteins (Zaps) play important roles in Z ring condensation and stability, and discover septal cell wall synthesis as a novel player for Z ring condensation and stabilization in Escherichia coli and Caulobacter crescentus. Moreover, we find that the interaction between the Z ring membrane anchor, FtsA, and components of the septal cell wall synthetic complex are critical for septal cell wall synthesis-mediated Z ring condensation. Altogether, these findings suggest that the divisome is a self-enhancing machine in these two gram-negative bacteria, where the Z ring and the septal cell wall synthetic complex communicate with and reinforce each other to ensure robustness of cell division.

摘要

在细菌胞质分裂过程中,细菌微管蛋白 FtsZ 的多聚体凝聚成 Z 环,以协调分裂体组装和隔膜细胞壁合成。先前的研究发现,Z 环的凝聚和稳定性对于成功的细胞分裂至关重要。然而,FtsZ 丝如何凝聚成 Z 环仍然是一个谜,以及隔膜细胞壁合成是否可以反馈到 Z 环尚未得到研究。在这里,我们表明 FtsZ 相关蛋白(Zaps)在 Z 环的凝聚和稳定性中发挥重要作用,并发现隔膜细胞壁合成是大肠杆菌和新月柄杆菌中 Z 环凝聚和稳定的一个新的参与者。此外,我们发现 Z 环膜锚定蛋白 FtsA 与隔膜细胞壁合成复合物的成分之间的相互作用对于隔膜细胞壁合成介导的 Z 环凝聚至关重要。总之,这些发现表明,在这两种革兰氏阴性菌中,分裂体是一种自我增强的机器,其中 Z 环和隔膜细胞壁合成复合物相互交流并相互加强,以确保细胞分裂的稳健性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9031/11410940/acd538ac3314/41467_2024_52217_Fig1_HTML.jpg

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