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Related Experiment Video

Updated: Jul 12, 2025

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

Human proteins curing yeast prions.

Songsong Wu¹, Herman K Edskes¹, Reed B Wickner¹

¹Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, MD 20892-0830.

Proceedings of the National Academy of Sciences of the United States of America

|October 30, 2023

Summary

This summary is machine-generated.

Researchers screened human genes in yeast to find anti-prion compounds. They identified 20 genes, including Bag5, that cure yeast prions [PSI+] and [URE3] by interfering with prion propagation mechanisms.

Keywords:

Bag5 DNAJA1 PRPF19 URE3 amyloid

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Last Updated: Jul 12, 2025

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Area of Science:

Molecular Biology
Biochemistry
Genetics

Background:

Human amyloidoses are increasingly recognized as prion diseases.
Saccharomyces cerevisiae prion models ([PSI+] and [URE3]) are crucial for screening anti-prion agents.
Yeast possesses intrinsic anti-prion systems that eliminate most de novo prions.

Purpose of the Study:

To screen a library of human open reading frames for compounds that cure yeast prions.
To identify novel anti-prion factors and elucidate their mechanisms of action.

Main Methods:

A yeast shuttle plasmid library of 14,913 human open reading frames was created under GAL promotion.
This library was screened for genes capable of curing the [PSI+] and [URE3] yeast prion models.
The functional domains and interactions of identified anti-prion proteins (e.g., PRPF19, DNAJA1, Bag5) were investigated.

Main Results:

Twenty human genes were identified that cure [PSI+] or [URE3] prions upon expression in yeast.
PRPF19 (E3 ubiquitin ligase) and DNAJA1 (J protein) were found to cure specific prions under certain conditions.
Human Bag5 demonstrated potent curing of both [URE3] and [PSI+], with its efficacy dependent on the number of BAG domains and interaction with Hsp70s.

Conclusions:

Human Bag5 and other identified genes represent potential therapeutic leads for prion diseases.
Bag5-mediated prion curing involves interference with the Hsp70/Hsp104/Sis1 chaperone machinery essential for prion propagation.
The yeast prion model is a powerful tool for discovering anti-prion therapeutics targeting conserved cellular pathways.