Amyloids assemble as part of recognizable structures during oogenesis in Xenopus

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 norm...

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Main Authors: Michael H. Hayes, Daniel L. Weeks
Format: Article
Language:English
Published: The Company of Biologists 2016-06-01
Series:Biology Open
Subjects:
Online Access:http://bio.biologists.org/content/5/6/801
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spelling doaj-a59d9cf172a64c78a33a1c480a89e5632021-06-02T14:40:31ZengThe Company of BiologistsBiology Open2046-63902016-06-015680180610.1242/bio.017384017384Amyloids assemble as part of recognizable structures during oogenesis in XenopusMichael H. Hayes0Daniel L. Weeks1 Molecular and Cellular Biology Program, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA Molecular and Cellular Biology Program, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA 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.http://bio.biologists.org/content/5/6/801XenopusAmyloidGerminal vesicleNuclear particlesOogenesis
collection DOAJ
language English
format Article
sources DOAJ
author Michael H. Hayes
Daniel L. Weeks
spellingShingle Michael H. Hayes
Daniel L. Weeks
Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
Biology Open
Xenopus
Amyloid
Germinal vesicle
Nuclear particles
Oogenesis
author_facet Michael H. Hayes
Daniel L. Weeks
author_sort Michael H. Hayes
title Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
title_short Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
title_full Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
title_fullStr Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
title_full_unstemmed Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
title_sort amyloids assemble as part of recognizable structures during oogenesis in xenopus
publisher The Company of Biologists
series Biology Open
issn 2046-6390
publishDate 2016-06-01
description 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.
topic Xenopus
Amyloid
Germinal vesicle
Nuclear particles
Oogenesis
url http://bio.biologists.org/content/5/6/801
work_keys_str_mv AT michaelhhayes amyloidsassembleaspartofrecognizablestructuresduringoogenesisinxenopus
AT daniellweeks amyloidsassembleaspartofrecognizablestructuresduringoogenesisinxenopus
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