The archaeal division protein CdvB1 assembles into polymers that are depolymerized by CdvC.

The archaeal division protein CdvB1 assembles into polymers that are depolymerized by CdvC.
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DOI:
10.1002/1873-3468.14324
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发表时间:
2022-04
期刊:
影响因子:
3.5
通讯作者:
Dekker, Cees
Dekker, Cees
中科院分区:
生物学3区
文献类型:
--
作者:
Blanch Jover, Alberto;De Franceschi, Nicola;Fenel, Daphna;Weissenhorn, Winfried;Dekker, Cees

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Cdv蛋白构成了泉古菌的细胞分裂系统,这是一种与真核生物的ESCRT系统密切相关的机制。使用TEM成像和生化分析的组合,我们在这里提出了一个在体外研究的Metallosphaera sedula CdvB1,Cdv蛋白,被认为是发挥了重要作用的收缩环,驱动细胞分裂的Crenarchea。我们发现CdvB1自组装成细丝,这些细丝被Vps4同源物ATP酶CdvC解聚。此外,我们发现,CdvB1结合带负电荷的脂质膜,并可以脱离膜的CdvC的作用。我们的研究结果提供了新的洞察古细菌细胞分裂机制的主要组成部分之一。这项研究表明,古细菌细胞分裂蛋白CdvB1可以在体外形成细丝,以及这些细丝如何被AAA ATP酶CdvC解聚。我们发现,CdvB1可以结合到脂质膜,并可以脱离他们的CdvC,古菌Cdv系统的蛋白质相互作用提供了新的见解。
The Cdv proteins constitute the cell division system of the Crenarchaea, a machinery closely related to the ESCRT system of eukaryotes. Using a combination of TEM imaging and biochemical assays, we here present an in vitro study of Metallosphaera sedula CdvB1, the Cdv protein that is believed to play a major role in the constricting ring that drives cell division in the Crenarchaea. We show that CdvB1 self‐assembles into filaments that are depolymerized by the Vps4‐homolog ATPase CdvC. Furthermore, we find that CdvB1 binds to negatively charged lipid membranes and can be detached from the membrane by the action of CdvC. Our findings provide novel insight into one of the main components of the archaeal cell division machinery. This study shows that the archaeal cell division protein CdvB1 can form filaments in vitro, and how these filaments are depolymerized by the AAA ATPase CdvC. We show that CdvB1 can bind to lipid membranes and can be detached from them by CdvC, providing new insights on the protein interactions of the archaeal Cdv system.
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