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Generating new prions by targeted mutation or segment duplication.

Kacy R Paul1, Connor G Hendrich1, Aubrey Waechter1

  • 1Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523.

Proceedings of the National Academy of Sciences of the United States of America
|June 24, 2015
PubMed
Summary
This summary is machine-generated.

New yeast prion domains can evolve through mutations in glutamine/asparagine (Q/N)-rich regions or by repeating aggregation-prone segments. These mechanisms demonstrate how genetic variation can rapidly generate novel prion activities.

Keywords:
Sup35amyloidprionyeast

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Yeast prions are protein-based genetic elements formed by self-propagating amyloid structures.
  • Prion activity in yeast is primarily driven by glutamine/asparagine (Q/N)-rich prion domains.
  • The evolutionary pathways for new prion domains are not fully understood.

Purpose of the Study:

  • To investigate two potential mechanisms for the evolution of new yeast prion domains.
  • To determine if non-prion Q/N-rich domains can acquire prion-forming ability.
  • To assess if repeating aggregation-prone segments can induce prion activity.

Main Methods:

  • Rational design of mutations in non-prion Q/N-rich yeast domains.
  • Testing aggregation propensity and prion formation in engineered proteins.
  • Introducing tandem repeats of aggregation-prone segments into non-prion domains.

Main Results:

  • A small number of mutations were sufficient to induce aggregation and prion activity in previously non-prionogenic Q/N-rich domains.
  • Repeating aggregation-prone segments within non-prion Q/N-rich domains was sufficient to create prion activity.
  • These findings suggest generic mechanisms for prion domain evolution.

Conclusions:

  • The evolution of new yeast prion domains can occur through mutation and repeat expansion.
  • Genetic variation, such as DNA duplication, may facilitate the rapid emergence of prion activity.
  • Q/N-rich domains possess an inherent propensity for aggregation that can be unlocked by evolutionary pressures.