Related Experiment Videos
Heritable activity: a prion that propagates by covalent autoactivation.
B Tibor Roberts1, Reed B Wickner
1Laboratory of Biochemistry and Genetics, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA.
Genes & Development
|August 19, 2003
Summary
Yeast protease B can act as a prion, a self-propagating protein conformation, termed [beta]. This infectious [beta] prion is essential for yeast survival during starvation and sporulation.
Area of Science:
- Biochemistry
- Molecular Biology
- Yeast Genetics
Background:
- Prions are infectious proteins known to propagate via altered conformations.
- The theoretical possibility exists for enzymes essential for their own activation to function as prions.
Purpose of the Study:
- To investigate if yeast protease B can function as a prion.
- To characterize the properties and biological role of this potential prion.
Main Methods:
- Induction of de novo prion generation through pro-protease overexpression.
- Assessing prion infectivity, curability, and biological function in yeast.
Main Results:
- Yeast protease B was identified as a prion, designated [beta].
- [beta] prions are infectious, can be reversibly cured, and their formation is triggered by pro-protease overexpression.
- [beta] is advantageous under starvation and essential for yeast sporulation, despite being masked by protease A in normal conditions.
Conclusions:
- Yeast protease B acts as a prion ([beta]), demonstrating a novel class of prion behavior.
- This [beta] prion plays a crucial role in yeast adaptation to starvation and reproduction.
- The study suggests other enzymes requiring self-modification for activation may also form prions.