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Related Experiment Video

Updated: Jun 18, 2026

Microscopy of Fission Yeast Sexual Lifecycle

Microscopy of Fission Yeast Sexual Lifecycle

Published on: March 9, 2016

Prm1 functions as a disulfide-linked complex in yeast mating.

Valerie N Olmo¹, Eric Grote

¹Department of Biochemistry and Molecular Biology, The Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland 21205, USA.

The Journal of Biological Chemistry

|November 26, 2009

Summary

Prm1, a yeast mating protein, forms a disulfide-linked homodimer essential for plasma membrane fusion. Specific extracellular cysteines are crucial for this dimerization and fusion activity, revealing its function in cell fusion.

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Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Prm1 is a pheromone-induced glycoprotein crucial for yeast mating and plasma membrane fusion.
Previous studies suggested Prm1's role in cell fusion, but its precise structure and mechanism were unclear.

Purpose of the Study:

To elucidate the structure and topology of Prm1.
To identify the role of disulfide bonds and specific cysteine residues in Prm1 homodimerization and fusion activity.

Main Methods:

SDS-PAGE analysis under non-reducing conditions to assess Prm1 dimerization.
Co-immunoprecipitation assays to confirm Prm1 interactions.
Localization studies using GFP-Prm1 fusion proteins and protease protection assays.
Site-directed mutagenesis of cysteine residues in extracellular loops.

Main Results:

Prm1 exists as a disulfide-linked homodimer, migrating at twice its expected molecular weight.
A revised topological model shows Prm1 has four transmembrane domains and two large extracellular loops.
Mutating extracellular cysteines disrupted disulfide bond formation and homodimer stability but not localization.
Specific cysteines (Cys120 and Cys545) in extracellular loops are essential for disulfide cross-linking and fusion activity.

Conclusions:

Prm1 functions as a disulfide-linked homodimer, with extracellular cysteines critical for its structure and function in yeast plasma membrane fusion.
The extracellular loops and their disulfide bonds likely play a key role in mediating membrane fusion during mating.