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Updated: Jul 20, 2026
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A Yeast 2-Hybrid Screen in Batch to Compare Protein Interactions
Published on: June 6, 2018
Preferential duplication in the sparse part of yeast protein interaction network
Li Li1, Yingwu Huang, Xuefeng Xia
1MOE Key Laboratory of Bioinformatics, State Key Laboratory of Biomembrane and Membrane Biotechnology, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing, China.
Molecular Biology and Evolution
|September 19, 2006
Summary
Gene duplication, a key evolutionary driver, is constrained by protein interaction networks. Genes in highly connected network modules are less likely to duplicate, favoring duplication in sparser network regions.
Area of Science:
- Systems Biology
- Evolutionary Biology
- Bioinformatics
Background:
- Gene duplication is a fundamental mechanism driving the evolution of biomolecular networks.
- A strong relationship is expected between a gene's duplicability and its protein product's interactions within the network.
Purpose of the Study:
- To investigate the relationship between gene duplicability and protein interaction network properties in Saccharomyces cerevisiae.
- To determine how network structure, modularity, and hub characteristics influence gene duplication rates.
Main Methods:
- Analysis of the protein interaction network (PIN) of Saccharomyces cerevisiae.
- Calculation of clustering coefficient (CC) and modularity (Q(n)) for proteins.
- Utilizing functional annotation data and high-throughput experimental data for protein complexes.
Main Results:
- Duplicate genes exhibit significantly lower clustering coefficients (CC) than singletons.
- The proportion of duplicates (PD) decreases with increasing CC and is negatively correlated with mean CC across functional categories.
- Intramodular hubs show lower PD, while intermodular hubs have PD comparable to or higher than the network average.
Conclusions:
- High clustering coefficient (CC) and modularity impose evolutionary constraints on gene duplicability.
- Gene duplication is favored in less constrained, sparser regions of protein interaction networks.
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