Rapid Evolution of Virus Sequences in Intrinsically Disordered Protein Regions

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Proteins often contain regions with defined structures that enable their function. While important for maintaining the overall architecture of the protein, structural conservation adds constraints on the ability of the protein to mutate, and thus evolve. Viruses of eukaryotes, however, often encode for proteins with unstructured regions. As these regions are less constrained, they are more likely to accumulate mutations, which in turn can facilitate the appearance of novel functions during the evolution of the virus. Even though it has been known that such “disordered protein regions” have been particularly malleable in evolution, their functions and their ability to withstand extensive mutations have not been explored in detail. Here, we discovered that a disordered part of the Nodamura Virus polymerase is both required for replication of the viral genome, and extremely variable among different nodaviruses. We examined the tolerance of this protein region to mutations and found an unexpected ability to accommodate very diverse protein sequences. We propose that disordered protein regions can be a reservoir for evolutionary innovation that can play important roles in virus adaptation to new environments.

Vyšlo v časopise: Rapid Evolution of Virus Sequences in Intrinsically Disordered Protein Regions. PLoS Pathog 10(12): e32767. doi:10.1371/journal.ppat.1004529
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004529

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