IM30 IDPs form a membrane-protective carpet upon super-complex disassembly.

IM30 IDPs form a membrane-protective carpet upon super-complex disassembly.
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DOI:
10.1038/s42003-020-01314-4
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发表时间:
2020-10-21
影响因子:
5.9
通讯作者:
Schneider D
Schneider D
中科院分区:
生物学2区
文献类型:
--
作者:
Junglas B;Orru R;Axt A;Siebenaller C;Steinchen W;Heidrich J;Hellmich UA;Hellmann N;Wolf E;Weber SAL;Schneider D

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噬菌体休克蛋白A(PspA)家族的成员,包括30 kDa的内膜相关蛋白(IM30),被认为是稳定应激细胞膜。此外,IM30在含有类囊体膜的叶绿体和蓝细菌中是必不可少的,在那里它参与膜生物发生和/或重塑。虽然众所周知PspA和顶30与膜结合,但膜稳定化的机制仍然是谜。在这里,我们报告说,环形IM30超复合物在膜上分解,导致形成膜保护蛋白地毯。在环解离后,IM30的C-末端结构域展开,并且原聚体在膜上自组装。IM30在膜上的组装在体内已经被观察到,并且与蓝藻和叶绿体中的应激反应相关。这些组件可能对应于这里识别的毯状结构。我们的研究定义了迄今为止IM30和相关蛋白(包括PspA)生理功能的神秘结构基础,并强调了迄今为止尚未认识到的内在无序蛋白质膜稳定的概念。Junalton等人通过30 kDa的内膜相关蛋白(IM30)(噬菌体休克蛋白A(PspA)家族的一个成员)探索膜稳定化的机制,并报道了环状IM30超复合物在与带负电荷的膜表面结合时分解,涉及单体的部分解折叠和膜保护毯的形成。这项研究强调了内在无序蛋白质在膜稳定中的结构作用。
Members of the phage shock protein A (PspA) family, including the inner membrane-associated protein of 30 kDa (IM30), are suggested to stabilize stressed cellular membranes. Furthermore, IM30 is essential in thylakoid membrane-containing chloroplasts and cyanobacteria, where it is involved in membrane biogenesis and/or remodeling. While it is well known that PspA and IM30 bind to membranes, the mechanism of membrane stabilization is still enigmatic. Here we report that ring-shaped IM30 super-complexes disassemble on membranes, resulting in formation of a membrane-protecting protein carpet. Upon ring dissociation, the C-terminal domain of IM30 unfolds, and the protomers self-assemble on membranes. IM30 assemblies at membranes have been observed before in vivo and were associated with stress response in cyanobacteria and chloroplasts. These assemblies likely correspond to the here identified carpet structures. Our study defines the thus far enigmatic structural basis for the physiological function of IM30 and related proteins, including PspA, and highlights a hitherto unrecognized concept of membrane stabilization by intrinsically disordered proteins. Junglas et al. probe into the mechanism of membrane stabilization by the inner membrane-associated protein of 30 kDa (IM30), a member of the phage shock protein A (PspA) family, and report that ring-shaped IM30 super-complexes disassemble upon binding to negatively charged membrane surfaces, involving partly unfolding of the monomers and formation of a membrane-protecting carpet. This study highlights the structural role of intrinsically disordered proteins in membrane stabilization.
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