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Processes of fungal proteome evolution and gain of function: gene duplication and domain rearrangement
- Source :
- Physical Biology. 8:035009
- Publication Year :
- 2011
- Publisher :
- IOP Publishing, 2011.
-
Abstract
- During evolution, organisms have gained functional complexity mainly by modifying and improving existing functioning systems rather than creating new ones ab initio. Here we explore the interplay between two processes which during evolution have had major roles in the acquisition of new functions: gene duplication and protein domain rearrangements. We consider four possible evolutionary scenarios: gene families that have undergone none of these event types; only gene duplication; only domain rearrangement, or both events. We characterize each of the four evolutionary scenarios by functional attributes. Our analysis of ten fungal genomes indicates that at least for the fungi clade, species significantly appear to gain complexity by gene duplication accompanied by the expansion of existing domain architectures via rearrangements. We show that paralogs gaining new domain architectures via duplication tend to adopt new functions compared to paralogs that preserve their domain architectures. We conclude that evolution of protein families through gene duplication and domain rearrangement is correlated with their functional properties. We suggest that in general, new functions are acquired via the integration of gene duplication and domain rearrangements rather than each process acting independently.
- Subjects :
- Genetics
Fungal protein
Concerted evolution
Proteome
Protein family
Genes, Fungal
Protein domain
Fungi
Biophysics
Cell Biology
Computational biology
Biology
Biological Evolution
Article
Domain (software engineering)
Fungal Proteins
Structural Biology
Gene Duplication
Databases, Genetic
Gene Order
Gene duplication
Gene family
Molecular Biology
Functional divergence
Subjects
Details
- ISSN :
- 14783975
- Volume :
- 8
- Database :
- OpenAIRE
- Journal :
- Physical Biology
- Accession number :
- edsair.doi.dedup.....2506d228314a25110288d70de590bace