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Yeast Signaling

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Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

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Related Experiment Video

Updated: Sep 11, 2025

Protein Engineering by Yeast Surface Display

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

Decoding Protein-Peptide Interactions Using a Large, Target-Agnostic Yeast Surface Display Library.

Joseph D Hurley¹, Irina Shlosman¹, Megha Lakshminarayan¹

¹Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, Massachusetts 02115, United States.

ACS Chemical Biology

|August 13, 2025

Summary

This summary is machine-generated.

We developed a large yeast surface display library to discover high-affinity peptide binders for target proteins. This powerful tool identifies novel peptide ligands and characterizes protein-peptide interactions for biomedical research.

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Area of Science:

Biochemistry
Molecular Biology
Biotechnology

Background:

Protein-peptide interactions are crucial for biological processes and drug discovery.
Identifying high-affinity peptide binders to target proteins is a key challenge.
Current methods for peptide discovery are often low-throughput and limited in scope.

Purpose of the Study:

To develop a high-throughput method for discovering novel peptide ligands.
To characterize sequence properties that drive peptide-protein binding.
To create a versatile tool for exploring protein-peptide interactions.

Main Methods:

Construction of a yeast surface display library with approximately 6.1 × 10^9 unique peptides.
Screening the library against diverse protein targets, including antibodies, an E3 ubiquitin ligase, and a bacterial enzyme.
Analysis of binding data to identify key sequence motifs and high-affinity peptide clones.

Main Results:

Successful identification of binding motifs for various protein targets.
Discovery of multiple novel peptide ligands with high binding affinity.
Demonstration of the library's effectiveness across different protein types.

Conclusions:

The yeast surface display library is a robust and versatile tool for peptide ligand discovery.
The library facilitates the characterization of protein-peptide binding interactions.
The library will be made available to enable further research in the field.