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Updated: May 26, 2026

A Yeast 2-Hybrid Screen in Batch to Compare Protein Interactions

A Yeast 2-Hybrid Screen in Batch to Compare Protein Interactions

Published on: June 6, 2018

High-throughput yeast two-hybrid screening.

George G Roberts¹, Jodi R Parrish, Bernardo A Mangiola

¹Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, MI, USA.

Methods in Molecular Biology (Clifton, N.J.)

|January 6, 2012

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This study introduces two high-throughput yeast two-hybrid screening methods to efficiently map protein interactions. These protocols maximize coverage for selected proteins or entire proteomes, advancing biological systems research.

Area of Science:

Proteomics
Molecular Biology
Systems Biology

Background:

Protein interactions are crucial for understanding biological processes.
The yeast two-hybrid system is a scalable technology for detecting these interactions.
Current protein interaction maps are incomplete due to screening limitations.

Purpose of the Study:

To develop high-throughput screening protocols for yeast two-hybrid systems.
To efficiently maximize coverage of protein interactions for selected proteins or entire proteomes.
To provide adaptable methods for various yeast two-hybrid system versions.

Main Methods:

Two distinct high-throughput yeast two-hybrid screening protocols are presented.
Protocol 1 is suitable for screening libraries of activation domain (AD) clones.

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Last Updated: May 26, 2026

A Yeast 2-Hybrid Screen in Batch to Compare Protein Interactions

A Yeast 2-Hybrid Screen in Batch to Compare Protein Interactions

Published on: June 6, 2018

Unravelling the Function of a Bacterial Effector from a Non-cultivable Plant Pathogen Using a Yeast Two-hybrid Screen

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Informatic Analysis of Sequence Data from Batch Yeast 2-Hybrid Screens

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Published on: June 28, 2018

Protocol 2 uses a two-phase scheme to screen arrays of individual AD clones.

Main Results:

The developed methods enable efficient screening of numerous protein pairs.
These protocols significantly enhance the coverage of detectable protein interactions.
The methods are designed to identify interactors for bait proteins fused to a DNA-binding domain (BD).

Conclusions:

The presented high-throughput yeast two-hybrid methods offer efficient strategies for comprehensive protein interaction mapping.
These protocols address the economic and technical challenges of large-scale proteome analysis.
The adaptable methods facilitate broader application in biological research.