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Evolutionary behaviour of bacterial prion-like proteins
1Department of Biology, McGill University, Montreal, QC, Canada.
Plos One
|March 6, 2019
Summary
Bacterial prion-like domains, like Rho, are widespread across diverse phyla but found in few species. This sporadic evolutionary pattern is common for these protein domains, impacting evolutionary studies.
Area of Science:
- Evolutionary biology
- Microbial genetics
- Protein science
Background:
- Prions in eukaryotes are associated with diseases and biological functions.
- Bacterial prion-forming proteins, such as Clostridium botulinum Rho, are emerging research areas.
- The evolutionary distribution of bacterial prions is not well understood.
Purpose of the Study:
- To analyze the evolutionary distribution of the Rho prion-forming domain across bacteria.
- To determine if wide-ranging evolutionary sporadicity is typical for bacterial prion-like domains.
- To assess the prevalence and distribution of prion-like protein domains in bacteria.
Main Methods:
- Bioinformatic analysis of the Rho prion-forming domain's conservation across bacterial species.
- Derivation of a 'coverage' metric (C) to quantify domain prevalence within its evolutionary range.
- Comparative analysis of >60 prion-like protein domain families across multiple bacterial phyla.
Main Results:
- The Rho prion-forming domain exhibits sporadic conservation across the Clostridium genus and bacteria generally.
- This domain spans at least eight different bacterial phyla, demonstrating wide evolutionary reach.
- Bacterial prion-like domains frequently occur across multiple phyla but sample a low fraction of species within their range.
- The Rho family is among the top three most widely distributed prion-like domain families by phyla count.
Conclusions:
- Wide-ranging evolutionary sporadicity is a common characteristic of bacterial prion-like protein domains.
- These findings have implications for understanding bacterial evolution and prion protein research.
- Further experimental investigation into bacterial prion-forming proteins is warranted.
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