Abstract:
:Intrinsically disordered regions in proteins are known to evolve rapidly while maintaining their function. However, given their lack of structure and sequence conservation, the means through which they stay functional is not clear. Poor sequence conservation also hampers the classification of these regions into functional groups. We studied the sequence conservation of a large number of predicted and experimentally determined intrinsically disordered regions from the human proteome in 7 other eukaryotes. We determined the chemical composition of disordered regions by calculating the fraction of positive, negative, polar, hydrophobic and special (Pro, Gly) residues, and studied its maintenance in orthologous proteins. A significant number of disordered regions with low sequence conservation showed considerable similarity in their chemical composition between orthologs. Clustering disordered regions based on their chemical composition resulted in functionally distinct groups. Finally, disordered regions showed location preference within the proteins that was dependent on their chemical composition. We conclude that preserving the overall chemical composition is one of the ways through which intrinsically disordered regions maintain their flexibility and function through evolution. We propose that the chemical composition of disordered regions can be used to classify them into functional groups and, together with conservation and location, may be used to define a general classification scheme.
journal_name
Mol Biosystjournal_title
Molecular bioSystemsauthors
Moesa HA,Wakabayashi S,Nakai K,Patil Adoi
10.1039/c2mb25202csubject
Has Abstractpub_date
2012-10-30 00:00:00pages
3262-73issue
12eissn
1742-206Xissn
1742-2051journal_volume
8pub_type
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