Characterizing unique features of prion-like domains recruited to stress granules
type: CreativeWork
description: Upon nucleation into a cross-β-structure, a classical amyloid will elongate in a concentration-dependent manner as successive hydrogen bonds are made along each exposed β-strand. Solid-state assemblies in biomolecular condensates such as the Balbiani Body in oocytes share a similar β-sheet rich structure that contributes to low dynamicity of the interactions in this separated phase. Prion-like domains (PrLDs) are domains that compositionally resemble yeast prion domains. Some PrLDs can form solid-state assemblies; however, PrLDs have also been associated with the formation of more liquid-like biomolecular condensates. Liquid-like biomolecular condensates form upon varying stimuli, and they appear to assemble through different mechanisms of recruitment than what has been observed for solid-state assemblies. Many solid-state assemblies form via homotypic interactions between identical assembly-prone PrLDs. In contrast, liquid-like assemblies generally form through heterotypic interactions across multiple components. Both solid-state and liquid-like condensates recruit domains that are currently classified as "prion-like", but evidence is mounting that these contrasting condensates preferentially recruit functionally different types of prion-like domains. A unique feature of prion-like domains recruited to liquid-like condensates is that formation of these assemblies appears to obey a more diverse set of rules for recruitment. This diversity of recruitment of PrLDs may be largely due to the heterotypic interaction mechanism for assembly into liquid-like condensates. This mechanism of recruitment may also be partially responsible for the different compositional preferences observed for PrLDs recruited to liquid-like assemblies. PrLD manipulation is a convenient tool for analyzing the compositional elements contributing to formation of both classes of biomolecular condensates. To elucidate the divergent features of PrLDs recruited to liquid-like assemblies, we used syste…
abstract: Upon nucleation into a cross-β-structure, a classical amyloid will elongate in a concentration-dependent manner as successive hydrogen bonds are made along each exposed β-strand. Solid-state assemblies in biomolecular condensates such as the Balbiani Body in oocytes share a similar β-sheet rich structure that contributes to low dynamicity of the interactions in this separated phase. Prion-like domains (PrLDs) are domains that compositionally resemble yeast prion domains. Some PrLDs can form solid-state assemblies; however, PrLDs have also been associated with the formation of more liquid-like biomolecular condensates. Liquid-like biomolecular condensates form upon varying stimuli, and they appear to assemble through different mechanisms of recruitment than what has been observed for solid-state assemblies. Many solid-state assemblies form via homotypic interactions between identical assembly-prone PrLDs. In contrast, liquid-like assemblies generally form through heterotypic interactions across multiple components. Both solid-state and liquid-like condensates recruit domains that are currently classified as "prion-like", but evidence is mounting that these contrasting condensates preferentially recruit functionally different types of prion-like domains. A unique feature of prion-like domains recruited to liquid-like condensates is that formation of these assemblies appears to obey a more diverse set of rules for recruitment. This diversity of recruitment of PrLDs may be largely due to the heterotypic interaction mechanism for assembly into liquid-like condensates. This mechanism of recruitment may also be partially responsible for the different compositional preferences observed for PrLDs recruited to liquid-like assemblies. PrLD manipulation is a convenient tool for analyzing the compositional elements contributing to formation of both classes of biomolecular condensates. To elucidate the divergent features of PrLDs recruited to liquid-like assemblies, we used syste…
author: Baer, Matthew Henry, author
author: Ross, Eric D., advisor
author: Stasevich, Timothy J., committee member
author: Zabel, Mark D., committee member
language: eng
language: English
keywords: prion-like domains, LLPS, stress granules
date published: 2021
date modified: 2026-07-27T19:13:25Z
provider: Colorado State University
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: Colorado State University. Libraries

PropertyValue
property ID: Handle
value: https://hdl.handle.net/10217/234209

PropertyValue
property ID: DOI
value: 10.25675/3.02607