古菌细胞分裂过程中 ESCRT-III 膜招募的分子和结构基础。
Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.
机构信息
Sir William Dunn School of Pathology, South Parks Road, Oxford OX1 3RE, UK.
出版信息
Mol Cell. 2011 Jan 21;41(2):186-96. doi: 10.1016/j.molcel.2010.12.018.
Members of the crenarchaeal kingdom, such as Sulfolobus, divide by binary fission yet lack genes for the otherwise near-ubiquitous tubulin and actin superfamilies of cytoskeletal proteins. Recent work has established that Sulfolobus homologs of the eukaryotic ESCRT-III and Vps4 components of the ESCRT machinery play an important role in Sulfolobus cell division. In eukaryotes, several pathways recruit ESCRT-III proteins to their sites of action. However, the positioning determinants for archaeal ESCRT-III are not known. Here, we identify a protein, CdvA, that is responsible for recruiting Sulfolobus ESCRT-III to membranes. Overexpression of the isolated ESCRT-III domain that interacts with CdvA results in the generation of nucleoid-free cells. Furthermore, CdvA and ESCRT-III synergize to deform archaeal membranes in vitro. The structure of the CdvA/ESCRT-III interface gives insight into the evolution of the more complex and modular eukaryotic ESCRT complex.
泉古菌门的成员，如 Sulfolobus，通过二分分裂进行繁殖，但缺乏细胞骨架蛋白中普遍存在的微管蛋白和肌动蛋白超家族的基因。最近的研究表明，泉古菌门中真核生物 ESCRT-III 和 Vps4 成分的同源物在 Sulfolobus 细胞分裂中发挥重要作用。在真核生物中，有几种途径将 ESCRT-III 蛋白募集到其作用部位。然而，尚未确定古菌 ESCRT-III 的定位决定因素。在这里，我们鉴定出一种名为 CdvA 的蛋白质，它负责将 Sulfolobus ESCRT-III 招募到膜上。过表达与 CdvA 相互作用的分离 ESCRT-III 结构域会导致无核体细胞的产生。此外，CdvA 和 ESCRT-III 在体外协同作用使古菌膜变形。CdvA/ESCRT-III 界面的结构深入了解了更复杂和模块化的真核 ESCRT 复合物的进化。
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