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Amyloids assemble as part of recognizable structures during oogenesis in Xenopus

By Michael H. Hayes and Daniel L. Weeks

Abstract

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

Topics: Xenopus, Amyloid, Germinal vesicle, Nuclear particles, Oogenesis, Science, Q, Biology (General), QH301-705.5
Publisher: The Company of Biologists
Year: 2016
DOI identifier: 10.1242/bio.017384
OAI identifier: oai:doaj.org/article:a59d9cf172a64c78a33a1c480a89e563
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