Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein
Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein
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DOI：
10.1006/jmbi.1999.3055
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发表时间：
1999-09-10
影响因子：
5.6
通讯作者：
Saibil, HR
中科院分区：
文献类型：
--
作者：
Al-Khayat, HA;Bhella, D;Saibil, HR
酵母Ty反转录转座子产生的病毒样颗粒(VLP)在结构和功能上与逆转录病毒核心相关。利用低温电子显微镜(Cryo-EM)和三维重建(3D)，我们研究了由全长和截短形式的衣壳结构蛋白组装而成的VLP的结构。VLP在其半径分布上具有高度的多分散性。我们发现，衣壳结构蛋白C-末端区域的长度决定了组装颗粒的T数，从而决定了颗粒的大小。每个被研究的结构似乎组装成至少两到三个大小的类别，较短的C末端产生较小的颗粒。这种组装特性为理解逆转录病毒核心蛋白的可变组装提供了一个模型。这些颗粒是由三聚体聚集的单元组装而成，衣壳上有孔。(C)1999年学术出版社。
The virus-like particles (VLPs) produced by the yeast Ty retrotransposons are structurally and functionally related to retroviral cores. Using cryoelectron microscopy (cryo-EM) and three-dimensional (3D) reconstruction, we have examined the structures of VLPs assembled from full-length and truncated forms of the capsid structural protein. The VLPs are highly polydisperse in their radius distribution. We have found that the length of the C-terminal region of the capsid structural protein dictates the T-number, and thus the size, of the assembled particles. Each construct studied appears to assemble into at least two or three size classes, with shorter C termini giving rise to smaller particles. This assembly property provides a model for understanding the variable assembly of retroviral core proteins. The particles are assembled from trimer-clustered units and there are holes in the capsid shells. (C) 1999 Academic Press.