Abstract
BackgroundIntrinsically 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 FindingsWe find that genes duplicated as part of a genome duplication (ohnologs) are significantly more intrinsically disordered than singletons (p<2.2e-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).ConclusionThis 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.
Highlights
Disordered proteins are biologically active proteins containing sequences without stable secondary and/or tertiary structure [1,2,3]
We set out to investigate if the proteins that were retained in duplicate after whole genome duplication (WGD) have a higher or lower number of intrinsically disordered regions than singleton proteins
We found that 29% (154) of ohnologs in S. cerevisiae have gained at least one intrinsically disordered region compared to their orthologs in L. kluyveri, while the figure is only 25% (1027) for Number of proteins having at least 1 intrinsically disordered region
Summary
Disordered proteins are biologically active proteins containing sequences without stable secondary and/or tertiary structure [1,2,3]. Disordered regions typically evolve rapidly compared to ordered regions [14]. There are several possible mechanisms explaining how genes encoding intrinsically disordered proteins have arisen. These include de novo generation [15,16], lateral and horizontal gene transfer, and gene duplication [17]. 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
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
