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Related Concept Videos

Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Related Experiment Video

Updated: May 22, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
08:38

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells

Published on: March 3, 2015

Predicting the fission yeast protein interaction network.

Vera Pancaldi, Omer S Saraç, Charalampos Rallis

    G3 (Bethesda, Md.)
    |April 28, 2012
    PubMed
    Summary

    Researchers predicted fission yeast protein interactions using computational methods, creating a valuable resource for biological exploration. This in silico interactome provides a foundation for understanding cellular processes and guiding future experiments.

    Keywords:
    Cbf11Mak1/2/3TORrandom forestsupport vector machine

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    Area of Science:

    • Molecular Biology
    • Systems Biology
    • Genomics

    Background:

    • Understanding cellular information flow necessitates mapping protein-protein interactions (PPIs).
    • Fission yeast (Schizosaccharomyces pombe) lacks comprehensive PPI data, hindering systems-level analysis.
    • PPIs are crucial for deciphering biological processes and cellular functions.

    Purpose of the Study:

    • To develop and validate an in silico method for predicting PPIs in fission yeast.
    • To create a comprehensive protein-interaction network for Schizosaccharomyces pombe.
    • To identify key protein hubs and pathways within the fission yeast interactome.

    Main Methods:

    • Utilized gene/protein properties, genome-wide regulation data, and cross-species conservation (budding vs. fission yeast) for in silico prediction.
    • Validated predictions through high-confidence test sets (70-80% accuracy), known complexes (SAGA), and mass spectrometry (Cbf11).
    • Explored subnetworks involving Tor1/2 kinases and identified potential hubs in stress response (Mak1/2/3) and gene silencing (argonaute 1).

    Main Results:

    • Developed a predictive model for fission yeast PPIs with high accuracy.
    • Successfully recapitulated known interactions and identified novel ones, with 73% of newly discovered interactions present in predictions.
    • Identified potential key regulators in stress response and gene silencing pathways.

    Conclusions:

    • The generated in silico fission yeast interactome provides a valuable resource for biological research.
    • The predicted network can guide experimental design and accelerate the discovery of cellular mechanisms.
    • The PInt online resource offers freely accessible predicted protein interactions for Schizosaccharomyces pombe.