Abstract
Protein misfolding and aggregation are associated with human diseases and aging. However, microorganisms widely exploit the self-propagating properties of misfolded infectious protein particles, prions, as epigenetic information carriers that drive various phenotypic adaptations and encode molecular information. Microbial prion research has faced a paradigm shift in recent years, with breakthroughs that demonstrate the great functional and structural diversity of these agents. Here, we outline unorthodox examples of microbial prions in yeast and other microorganisms, focusing on their noncanonical functions. We discuss novel molecular mechanisms for the inheritance of conformationally-encoded epigenetic information and the evolutionary advantages they confer. Lastly, in light of recent advancements in the field of molecular self-assembly, we present a hypothesis regarding the existence of non-proteinaceous prion-like entities.
Original language | English |
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Pages (from-to) | 391-405 |
Number of pages | 15 |
Journal | Trends in Biochemical Sciences |
Volume | 46 |
Issue number | 5 |
DOIs | |
State | Published - May 2021 |
Keywords
- amyloids
- metions
- microorganisms
- prions
- self-assembly
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Biochemistry