Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.

Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.
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DOI:
10.1016/j.molcel.2010.12.018
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发表时间:
2011-01-21
期刊:
影响因子:
16
通讯作者:
Bell SD
Bell SD
中科院分区:
生物学1区
文献类型:
--
作者:
Samson RY;Obita T;Hodgson B;Shaw MK;Chong PL;Williams RL;Bell SD

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泉古菌王国的成员,如硫化叶菌,通过二分裂分裂,但缺乏细胞骨架蛋白的微管蛋白和肌动蛋白超家族的基因。最近的工作已经确定,硫化叶菌同源物的真核ESCRT-III和Vps 4的ESCRT机制的组成部分在硫化叶菌细胞分裂中发挥重要作用。在真核生物中,几种途径将ESCRT-III蛋白募集到其作用位点。然而,古细菌ESCRT-III的定位决定因素尚不清楚。在这里,我们确定了一种蛋白质,CdvA,负责招募硫化叶菌ESCRT-III的膜。与CdvA相互作用的分离的ESCRT-III结构域的过表达导致产生无核细胞。此外,CdvA和ESCRT-III协同作用,在体外变形古菌膜。CdvA/ESCRT-III界面的结构使我们深入了解更复杂和模块化的真核ESCRT复合物的进化。
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 synergise 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.
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