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一种独特的细胞分裂蛋白,对细菌分裂体的组装至关重要。

A unique cell division protein critical for the assembly of the bacterial divisome.

机构信息

Department of Respiratory Medicine, Infectious Diseases and Pathogen Biology Center State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, The First Hospital of Jilin University, Changchun, China.

Bioinformatics Laboratory, The First Hospital of Jilin University, Changchun, China.

出版信息

Elife. 2024 Oct 3;12:RP87922. doi: 10.7554/eLife.87922.

DOI:10.7554/eLife.87922
PMID:39361022
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11449484/
Abstract

Identification of unique essential bacterial genes is important for not only the understanding of their cell biology but also the development of new antimicrobials. Here, we report a previously unrecognized core component of the divisome. Our results reveal that the protein, termed Aeg1 interacts with multiple cell division proteins, including FtsN, which is required for components of the divisome to localize to the midcell. We demonstrate that the FtsA and FtsB mutants effectively bypassed the need of Aeg1 by , as did the activation variants FtsW and FtsW. Our results suggest that Aeg1 is a cell division protein that arrives at the division site to initiate cell division by recruiting FtsN, which activates FtsQLB and FtsA to induce the septal peptidoglycan synthase FtsWI. The discovery of the new essential cell division protein has provided a new target for the development of antibacterial agents.

摘要

鉴定独特的必需细菌基因不仅对了解其细胞生物学很重要,而且对开发新的抗菌药物也很重要。在这里,我们报告了一个以前未被识别的分裂体核心成分。我们的结果表明,这种被称为 Aeg1 的蛋白质与多种细胞分裂蛋白相互作用,包括 FtsN,FtsN 是将分裂体组件定位到细胞中部所必需的。我们证明,FtsA 和 FtsB 突变体有效地通过 FtsW 和 FtsW 的激活变体绕过了对 Aeg1 的需求。我们的结果表明,Aeg1 是一种细胞分裂蛋白,通过招募 FtsN 到达分裂部位,激活 FtsQLB 和 FtsA 诱导隔膜肽聚糖合酶 FtsWI,从而启动细胞分裂。新的必需细胞分裂蛋白的发现为抗菌剂的开发提供了一个新的靶点。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/915591cfe4db/elife-87922-fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/338573d18381/elife-87922-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/c75c53f995c2/elife-87922-fig1-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/22e69c107e41/elife-87922-fig1-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/694e5fb1fb44/elife-87922-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/602a300dc542/elife-87922-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/83cdd824c9d2/elife-87922-fig3-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/5dc40d682c71/elife-87922-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/a9a0037826c9/elife-87922-fig4-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/3d980b82c151/elife-87922-fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/4ece36213f51/elife-87922-fig5-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/5c7f4907c562/elife-87922-fig5-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/915591cfe4db/elife-87922-fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/338573d18381/elife-87922-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/c75c53f995c2/elife-87922-fig1-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/22e69c107e41/elife-87922-fig1-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/694e5fb1fb44/elife-87922-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/602a300dc542/elife-87922-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/83cdd824c9d2/elife-87922-fig3-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/5dc40d682c71/elife-87922-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/a9a0037826c9/elife-87922-fig4-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/3d980b82c151/elife-87922-fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/4ece36213f51/elife-87922-fig5-figsupp1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/5c7f4907c562/elife-87922-fig5-figsupp2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e28b/11449484/915591cfe4db/elife-87922-fig6.jpg

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本文引用的文献

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FtsN maintains active septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthases in E. coli.FtsN 通过与大肠杆菌中特定于隔膜的肽聚糖合成酶形成一个连续的复合物来维持活跃的隔膜细胞壁合成。
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