Abstract

BackgroundThere is increasing interest in the evolution of protein-protein interactions because this should ultimately be informative of the patterns of evolution of new protein functions within the cell. One model proposes that the evolution of new protein-protein interactions and protein complexes proceeds through the duplication of self-interacting genes. This model is supported by data from yeast. We examined the relationship between gene duplication and self-interaction in the human genome.ResultsWe investigated the patterns of self-interaction and duplication among 34808 interactions encoded by 8881 human genes, and show that self-interacting proteins are encoded by genes with higher duplicability than genes whose proteins lack this type of interaction. We show that this result is robust against the system used to define duplicate genes. Finally we compared the presence of self-interactions amongst proteins whose genes have duplicated either through whole-genome duplication (WGD) or small-scale duplication (SSD), and show that the former tend to have more interactions in general. After controlling for age differences between the two sets of duplicates this result can be explained by the time since the gene duplication.ConclusionsGenes encoding self-interacting proteins tend to have higher duplicability than proteins lacking self-interactions. Moreover these duplicate genes have more often arisen through whole-genome rather than small-scale duplication. Finally, self-interacting WGD genes tend to have more interaction partners in general in the PIN, which can be explained by their overall greater age. This work adds to our growing knowledge of the importance of contextual factors in gene duplicability.

Highlights

  • There is increasing interest in the evolution of protein-protein interactions because this should be informative of the patterns of evolution of new protein functions within the cell

  • We show a greater enrichment of self-interacting genes among whole genome duplication (WGD) duplicates than small-scale duplication (SSD) duplicates and relate this to an overall higher connectivity of WGD genes in the proteininteraction network

  • We observed greater duplicability of human self-interacting genes and that WGD duplicate genes tend to be selfinteracting more often than SSD duplicate genes. This latter observation probably relates to the higher overall connectivity of WGD genes in protein interaction networks

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Summary

Introduction

There is increasing interest in the evolution of protein-protein interactions because this should be informative of the patterns of evolution of new protein functions within the cell. One model proposes that the evolution of new protein-protein interactions and protein complexes proceeds through the duplication of self-interacting genes. This model is supported by data from yeast. One special category of PPI is the interaction between identical copies of a protein produced from the same gene (self-interaction) forming homomers. These comprise a significant fraction of the protein interaction network (PIN) due to genetic factors: the interacting partners are translated from the same mRNA and so are ipso facto co-regulated and co-localized in the cell; as well. The duplicability of genes differs between smallscale (SSD) and whole genome duplication (WGD) [7,8]

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