Amyloids assemble as part of recognizable structures during oogenesis in Xenopus.
Amyloids assemble as part of recognizable structures during oogenesis in Xenopus.
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DOI：
10.1242/bio.017384
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发表时间：
2016-06-15
期刊：
影响因子：
2.4
通讯作者：
Weeks DL
中科院分区：
文献类型：
--
作者：
Hayes MH;Weeks DL
阿尔茨海默病、亨廷顿病和类似疾病的一个标志是蛋白质组装成淀粉样蛋白，而不是折叠成它们的天然状态。越来越多的人认识到，淀粉样蛋白在特定条件下可能是非致病性的。在这里，我们表明，淀粉样蛋白的形式作为一个正常的一部分，非洲爪蟾卵母细胞的发展。使用淀粉样蛋白结合染料和识别淀粉样蛋白结构的抗体，可以在胞质溶胶和细胞核中检测到淀粉样蛋白。在胞质溶胶中，卵黄血小板是淀粉样蛋白反应性的，因为是一些尚未被表征的颗粒。在细胞核中，我们发现与RNA聚合酶I、II和III的转录和RNA加工相关的颗粒含有淀粉样蛋白。核淀粉样蛋白在分离后数小时内保持完整;然而，RNA酶处理迅速破坏核淀粉样蛋白。总结：非洲爪蟾卵母细胞中负责RNA转录、修饰和加工的非膜结合核颗粒含有作为正常发育的一部分组装成淀粉样蛋白的蛋白质。
A hallmark of Alzheimer's, Huntington's and similar diseases is the assembly of proteins into amyloids rather than folding into their native state. There is an increasing appreciation that amyloids, under specific conditions, may be non-pathogenic. Here we show that amyloids form as a normal part of Xenopus oocyte development. Amyloids are detectable in the cytosol and the nucleus using an amyloid binding dye and antibodies that recognize amyloid structure. In the cytosol, yolk platelets are amyloid reactive, as are a number of yet to be characterized particles. In the nucleus, we find particles associated with transcription by RNA polymerase I, II and III and RNA processing contain amyloids. Nuclear amyloids remain intact for hours following isolation; however, RNase treatment rapidly disrupts nuclear amyloids. Summary: Non-membrane-bound nuclear particles in Xenopus oocytes responsible for RNA transcription, modification and processing contain proteins assembled into amyloids as part of normal development.