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Updated: May 13, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
Published on: August 8, 2017
Blessings in disguise: biological benefits of prion-like mechanisms
Gregory A Newby1, Susan Lindquist
1Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Abstract:
Prions and amyloids are often associated with disease, but related mechanisms provide beneficial functions in nature. Prion-like mechanisms (PriLiMs) are found from bacteria to humans, where they alter the biological and physical properties of prion-like proteins. We have proposed that prions can serve as heritable bet-hedging devices for diversifying microbial phenotypes. Other, more dynamic proteinaceous complexes may be governed by similar self-templating conformational switches. Additional PriLiMs continue to be identified and many share features of self-templating protein structure (including amyloids) and dependence on chaperone proteins. Here, we discuss several PriLiMs and their functions, intending to spur discussion and collaboration on the subject of beneficial prion-like behaviors.
Insights
Prion-like mechanisms (PriLiMs) offer beneficial functions beyond disease. These self-templating protein structures can diversify microbial phenotypes, acting as heritable bet-hedging devices.
Area of Science:
- Molecular Biology
- Biochemistry
- Evolutionary Biology
Background:
- Prions and amyloids are typically linked to diseases.
- However, similar self-templating protein mechanisms, termed prion-like mechanisms (PriLiMs), exist in nature.
- These PriLiMs can confer beneficial functions across diverse organisms.
Purpose of the Study:
- To discuss the beneficial roles of PriLiMs.
- To highlight their presence from bacteria to humans.
- To encourage research and collaboration on these functional prion-like behaviors.
Main Methods:
- Review and discussion of existing literature on PriLiMs.
- Identification of common features, such as self-templating protein structures and chaperone dependence.
- Exploration of proposed functions, including phenotypic diversification.
Main Results:
- PriLiMs are widespread, found in various organisms.
- They exhibit self-templating conformational switches, similar to amyloids.
- PriLiMs can function as heritable bet-hedging devices, promoting microbial adaptation.
Conclusions:
- Prion-like mechanisms are not solely pathogenic but play crucial beneficial roles.
- Understanding PriLiMs can reveal novel biological strategies for adaptation and survival.
- Further investigation into PriLiMs is warranted to explore their full functional spectrum.
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