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Yeast Signaling01:28

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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Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
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Published on: May 30, 2025

Yeast proteome map (update 2006).

Michel Perrot1, Anne-Laure Guieysse-Peugeot, Aurélie Massoni

  • 1Institut de Biochemie et Génétique Cellulaires, UMR CNRS 5095, Bordeaux, France.

Proteomics
|March 14, 2007
PubMed
Summary

Researchers identified 187 new protein spots in yeast using mass spectrometry and gene inactivation. This brings the total identified spots on the yeast proteome map to 602, significantly advancing proteomic investigations.

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Last Updated: Jul 16, 2026

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Identification of protein complexes with quantitative proteomics in S. cerevisiae
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Area of Science:

  • Proteomics
  • Yeast Biology
  • Molecular Biology

Background:

  • Two-dimensional gel electrophoresis (2-D PAGE) is crucial for proteomic studies.
  • Systematic protein identification is needed to enhance the utility of 2-D PAGE in yeast research.

Purpose of the Study:

  • To systematically identify Saccharomyces cerevisiae proteins separated by 2-D gels.
  • To expand the existing yeast 2-D proteome map.

Main Methods:

  • Mass spectrometry for protein identification.
  • Gene inactivation (knockout) studies to confirm protein identities.

Main Results:

  • Identification of 187 novel protein spots.
  • The yeast 2-D proteome map now includes 602 identified spots, representing 417 distinct proteins.
  • Approximately half of the detectable spots on the proteome map have been identified.

Conclusions:

  • The study significantly enhances the yeast 2-D proteome map.
  • The identified proteins and reference map are available via the Yeast Protein Map server.
  • This work improves the potential of 2-D PAGE for comprehensive yeast proteomic investigations.