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Yeast Signaling

Yeast Signaling

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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High Throughput Yeast Strain Phenotyping with Droplet-Based RNA Sequencing

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Hydrophobin-Based Surface Engineering for Sensitive and Robust Quantification of Yeast Pheromones.

Stefan Hennig¹, Gerhard Rödel², Kai Ostermann³

¹Institute of Genetics, Technische Universität Dresden, 01062 Dresden, Germany. Stefan.Hennig1@tu-dresden.de.

Sensors (Basel, Switzerland)

|April 30, 2016

Summary

We developed a sensitive assay using recombinant hydrophobins to quantify yeast alpha-factor pheromone. This method offers high robustness and reusability, enabling precise detection for various yeast strains.

Keywords:

analyte detection biosensor hydrophobin surface functionalization whole-cell biosensor yeast pheromone

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Area of Science:

Biochemistry
Biotechnology
Analytical Chemistry

Background:

Quantifying small peptides like yeast pheromones presents significant analytical challenges.
Recombinant hydrophobins are amphipathic proteins known for forming stable monolayers at interfaces.
Existing methods for pheromone detection may lack sensitivity or robustness.

Purpose of the Study:

To develop a highly sensitive and robust affinity-assay for quantifying the alpha-factor pheromone from Saccharomyces cerevisiae.
To leverage recombinant hydrophobins for creating a novel detection platform.
To enable precise control over assay sensitivity and investigate its application in studying yeast pheromone secretion.

Main Methods:

Functionalization of solid supports with recombinant hydrophobins, some exposing alpha-factor.
Utilizing pheromone-specific antibodies that bind to the functionalized surface.
Competitive detachment of antibodies by increasing concentrations of the target pheromone for quantification.
Employing an inverse assay setup to enhance sensitivity and lower the limit of detection.

Main Results:

The developed assay demonstrated high sensitivity and robustness against sample matrix variations.
Hydrophobin layers proved stable, allowing for repeated use of functionalized surfaces without loss of sensitivity.
An inverse assay configuration achieved a three-orders-of-magnitude increase in sensitivity, setting a new low limit of detection for yeast pheromone.
The assay successfully studied alpha-factor secretion in diverse yeast strains, including a whole-cell biosensor.

Conclusions:

Recombinant hydrophobins provide a versatile platform for developing sensitive and robust affinity-assays.
The developed assay offers a significant advancement in yeast pheromone quantification, with potential applications in microbial research and biotechnology.
The novel biosensor design achieved unprecedented detection limits for yeast pheromones.