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Related Experiment Video

Updated: Apr 11, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Amyloids or prions? That is the question.

Raimon Sabate¹, Frederic Rousseau, Joost Schymkowitz

¹a Departament de Fisicoquímica ; Facultat de Farmàcia; and Institut de Nanociència i Nanotecnologia (IN2UB); Universitat de Barcelona ; Barcelona , Spain ;

|June 4, 2015

Summary

This summary is machine-generated.

Understanding prion transmissibility requires analyzing amino acid sequences. Yeast prion domains reveal that intrinsically disordered regions rich in glutamine and asparagine are crucial for prion formation and propagation.

Keywords:

AD, Alzheimer's disease CJD, Creutzfeldt-Jakob disease PD, Parkinson's disease PFD, prion forming domain Q/N-rich domains TSE, transmissible spongiform encephalopathy amyloids fALS, familial amyotrophic lateral sclerosis neurodegenerative diseases prions protein intrinsic disorder yeast

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Published on: January 8, 2015

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Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Prion transmissibility is a poorly understood phenomenon.
Decoding sequence requirements for prion formation is an ongoing challenge.

Purpose of the Study:

To investigate the role of amino acid sequences in prion transmissibility.
To understand the sequence requirements for prion formation using yeast prion domains.

Main Methods:

Experimental analysis of yeast prion domains.
Bioinformatic analysis of intrinsically disordered sequence regions.

Main Results:

Intrinsically disordered sequence regions with high glutamine and asparagine content are essential for prion formation.
These regions balance amyloid nucleation propensity with disorder, preventing unwanted nucleation and facilitating propagation.

Conclusions:

Amino acid sequence, particularly in disordered regions, plays a critical role in prion formation and transmissibility.
Yeast prion domain studies offer insights into the molecular mechanisms of prion diseases.