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Updated: Jun 4, 2026

Protein Engineering by Yeast Surface Display

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

Construction of yeast surface-displayed cDNA libraries.

Scott Bidlingmaier¹, Bin Liu

¹UCSF Comprehensive Cancer Center, University of California at San Francisco, San Francisco, CA, USA.

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

|March 3, 2011

Summary

This study presents a method for displaying protein fragments on yeast cells for screening. This technique enables the efficient identification of proteins with specific binding properties from large libraries.

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Area of Science:

Biotechnology
Molecular Biology
Protein Engineering

Background:

Yeast display is a powerful technique for expressing heterologous proteins on the surface of Saccharomyces cerevisiae.
It allows for high-copy-level display and efficient screening of large protein libraries.
Previous applications have successfully identified binding proteins for various targets.

Purpose of the Study:

To describe protocols for constructing and validating yeast surface-displayed cDNA libraries.
To leverage existing yeast two-hybrid cDNA libraries as a starting point for display library construction.
To enable the selection of functional protein fragments with specific binding affinities.

Main Methods:

Utilizing yeast display technology to express protein fragments on the Saccharomyces cerevisiae cell wall.

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Protein Engineering by Yeast Surface Display

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

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Competitive Genomic Screens of Barcoded Yeast Libraries

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Constructing yeast surface-displayed cDNA libraries from existing yeast two-hybrid libraries.

Employing fluorescence-activated cell sorting (FACS) for selection of binding proteins.

Main Results:

Demonstrated efficient display of heterologous protein fragments at high copy levels on yeast cells.
Validated protocols for the construction and characterization of yeast surface-displayed cDNA libraries.
Showcased the potential for selecting protein fragments with specific binding properties.

Conclusions:

Yeast display provides an efficient platform for screening protein libraries for specific binding properties.
The described protocols facilitate the construction of functional yeast surface-displayed cDNA libraries.
This method, combined with FACS, offers a robust approach for identifying novel protein binders.