Complex formation of Vipp1 depends on its α-helical PspA-like domain
Complex formation of Vipp1 depends on its α-helical PspA-like domain
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DOI：
10.1074/jbc.m401750200
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发表时间：
2004-08-20
影响因子：
4.8
通讯作者：
Vothknecht, UC
中科院分区：
文献类型：
--
作者：
Aseeva, E;Ossenbühl, F;Vothknecht, UC
Vipp1 ((v)在棒状囊泡下- (i)在棒状囊泡下诱导(p)在棒状囊泡下的蛋白质（p)在棒状囊泡下(1)在棒状囊泡下）存在于蓝藻和光合真核生物的叶绿体中，它对类囊体膜的形成至关重要。Vipp1与bar hage (s) under bar hock (p) under bar protein (A) under bar （PspA）密切相关，这是一种在不同胁迫条件下诱导的细菌蛋白。Vipp1蛋白与PspA的不同之处在于一个额外的c端结构域，这是Vipp1在类囊体生物发生中发挥作用所必需的。在蓝藻、绿藻和维管植物中，Vipp1是一个高分子质量复合体的一部分。该复合体由Vipp1的多个拷贝形成，复合体的形成涉及Vipp1和PspA蛋白共同的中心α -螺旋结构域的相互作用。在维管植物的叶绿体中，Vipp1复合体可以通过绿色荧光蛋白在内膜的离散位置融合而可视化。绿色荧光蛋白融合分析进一步揭示了复合体的形成对于Vipp1在叶绿体内膜的正确定位很重要。
Vipp1 ((v) under bar esicle- (i) under bar nducing (p) under bar rotein in (p) under bar lastids (1) under bar) is found in Cyanobacteria and chloroplasts of photosynthetic eukaryotes where it is essential for the formation of the thylakoid membrane. Vipp1 is closely related to the (p) under bar hage (s) under bar hock (p) under bar rotein (A) under bar (PspA), a bacterial protein induced under diverse stress conditions. Vipp1 proteins differ from PspA by an additional C-terminal domain that is required for Vipp1 function in thylakoid biogenesis. We show here that in Cyanobacteria, green algae, and vascular plants, Vipp1 is part of a high molecular mass complex. The complex is formed by multiple copies of Vipp1, and complex formation involves interaction of the central alpha-helical domain that is common to Vipp1 as well as to PspA proteins. In chloroplasts of vascular plants, the Vipp1 complex can be visualized by green fluorescent protein fusion in discrete locations at the inner envelope. Green fluorescent protein fusion analysis furthermore revealed that complex formation is important for proper positioning of Vipp1 at the inner envelope of chloroplasts.