Differences in the number of intrinsically disordered regions between yeast duplicated proteins, and their relationship with functional divergence

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Abstract

Background: Intrinsically disordered regions are enriched in short interaction motifs that play a critical role in many protein-protein interactions. Since new short interaction motifs may easily evolve, they have the potential to rapidly change protein interactions and cellular signaling. In this work we examined the dynamics of gain and loss of intrinsically disordered regions in duplicated proteins to inspect if changes after genome duplication can create functional divergence. For this purpose we used Saccharomyces cerevisiae and the outgroup species Lachancea kluyveri. Principal Findings: We find that genes duplicated as part of a genome duplication (ohnologs) are significantly more intrinsically disordered than singletons (p>2.2 e-16, Wilcoxon), reflecting a preference for retaining intrinsically disordered proteins in duplicate. In addition, there have been marked changes in the extent of intrinsic disorder following duplication. A large number of duplicated genes have more intrinsic disorder than their L. kluyveri ortholog (29% for duplicates versus 25% for singletons) and an even greater number have less intrinsic disorder than the L. kluyveri ortholog (37% for duplicates versus 25% for singletons). Finally, we show that the number of physical interactions is significantly greater in the more intrinsically disordered ohnolog of a pair (p = 0.003, Wilcoxon). Conclusion: This work shows that intrinsic disorder gain and loss in a protein is a mechanism by which a genome can also diverge and innovate. The higher number of interactors for proteins that have gained intrinsic disorder compared with their duplicates may reflect the acquisition of new interaction partners or new functional roles. © 2011 Montanari et al.

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Montanari, F., Shields, D. C., & Khaldi, N. (2011). Differences in the number of intrinsically disordered regions between yeast duplicated proteins, and their relationship with functional divergence. PLoS ONE, 6(9). https://doi.org/10.1371/journal.pone.0024989

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