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Updated: Aug 6, 2026
08:07
Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
Published on: August 2, 2015
SoPPIs: a highly parallelized protein-protein-interaction screening method in prokaryotic and eukaryotic hosts
Silvio Collani1,2, Sarah Muniz Nardeli1,3, K V S K Arjun Chowdary3
1Umeå Plant Science Centre, Department of Plant Physiology, Umeå University, Umeå SE-90187, Sweden.
Nucleic Acids Research
|July 22, 2026
Summary
We developed SoPPIs, a novel method for genome-wide protein-protein interaction (PPI) analysis. This technique uses split-Cre/loxP and DNA sequencing to efficiently identify interacting protein pairs in cells.
Area of Science:
- Molecular Biology
- Genomics
- Biochemistry
Background:
- Protein-protein interactions (PPIs) are crucial for cellular functions but analyzing them genome-wide is difficult.
- Existing methods for PPI analysis have limitations in scalability and efficiency.
Purpose of the Study:
- To develop a novel, high-throughput method for genome-wide PPI analysis.
- To enable cost-efficient and parallelized identification of interacting protein pairs.
Main Methods:
- Developed SoPPIs (sequencing of PPIs), combining the split-Cre/loxP system with high-throughput DNA sequencing.
- Utilized sequential plasmid recombination to encode PPI information in DNA sequences.
- Applied next-generation sequencing for efficient identification of interacting protein pairs.
Main Results:
- SoPPIs successfully facilitates parallelized PPI analyses.
- The method was demonstrated by analyzing the Arabidopsis thaliana LSm/Sm ring and identifying interacting proteins.
- SoPPIs is applicable to most soluble proteins and adaptable to various cell types.
Conclusions:
- SoPPIs offers a versatile and user-friendly approach for comprehensive PPI network analysis.
- This method has the potential to significantly advance the study of complex biological systems by providing insights into PPIs.
- SoPPIs is expected to become a valuable tool for biological research due to its efficiency and broad applicability.
Related Concept Videos
02:04Protein-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...
02:26Protein 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,...
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,...