1. Rapid evolutionary dynamics of structural disorder as a potential driving force for biological divergence in flaviviruses
- Author
-
Jessica Siltberg-Liberles, Juan Felipe Ortiz, Patrick Masterson, Vladimir N. Uversky, and Madolyn L. MacDonald
- Subjects
conformational flexibility ,Mutation rate ,Molecular Sequence Data ,Sequence alignment ,comparative genomics ,Biology ,Divergence ,Evolution, Molecular ,03 medical and health sciences ,Viral Proteins ,Protein structure ,Mutation Rate ,Phylogenetics ,Genetics ,Amino Acid Sequence ,Evolutionary dynamics ,Ecology, Evolution, Behavior and Systematics ,Phylogeny ,030304 developmental biology ,Flexibility (engineering) ,0303 health sciences ,Flavivirus ,030302 biochemistry & molecular biology ,Biological Evolution ,Evolutionary biology ,structural disorder ,Sequence Alignment ,divergence ,Function (biology) ,Research Article - Abstract
Protein structure is commonly regarded to be conserved and to dictate function. Most proteins rely on conformational flexibility to some degree. Are regions that convey conformational flexibility conserved over evolutionary time? Can changes in conformational flexibility alter protein function? Here, the evolutionary dynamics of structurally ordered and disordered (flexible) regions are investigated genome-wide in flaviviruses, revealing that the amount and location of structural disorder fluctuates highly among related proteins. Some regions are prone to shift between structured and flexible states. Increased evolutionary dynamics of structural disorder is observed for some lineages but not in others. Lineage-specific transitions of this kind could alter the conformational ensemble accessible to the same protein in different species, causing a functional change, even if the predominant function remains conserved. Thus, rapid evolutionary dynamics of structural disorder is a potential driving force for phenotypic divergence among flaviviruses.
- Published
- 2013