Journal article
Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
Biology open, Vol.5(6), pp.801-806
06/15/2016
DOI: 10.1242/bio.017384
PMCID: PMC4920187
PMID: 27215327
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.
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.
Details
- Title: Subtitle
- Amyloids assemble as part of recognizable structures during oogenesis in Xenopus
- Creators
- Michael H Hayes - Carver College of Medicine, University of IowaDaniel L Weeks - Carver College of Medicine, University of Iowa
- Resource Type
- Journal article
- Publication Details
- Biology open, Vol.5(6), pp.801-806
- DOI
- 10.1242/bio.017384
- PMID
- 27215327
- PMCID
- PMC4920187
- NLM abbreviation
- Biol Open
- ISSN
- 2046-6390
- eISSN
- 2046-6390
- Publisher
- The Company of Biologists Ltd
- Grant note
- ; GM069944 / ;
- Language
- English
- Date published
- 06/15/2016
- Academic Unit
- Stead Family Department of Pediatrics; Biochemistry and Molecular Biology
- Record Identifier
- 9984025258902771
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