Functional Advantages of Conserved Intrinsic Disorder in RNA-Binding Proteins.

TitleFunctional Advantages of Conserved Intrinsic Disorder in RNA-Binding Proteins.
Publication TypeJournal Article
Year of Publication2015
AuthorsVaradi, M., Zsolyomi F., Guharoy M., and Tompa P.
JournalPLoS One
Volume10
Issue10
Paginatione0139731
Date Published2015
ISSN1932-6203
KeywordsAmino Acid Sequence, Models, Molecular, Protein Conformation, RNA-Binding Proteins
Abstract

Proteins form large macromolecular assemblies with RNA that govern essential molecular processes. RNA-binding proteins have often been associated with conformational flexibility, yet the extent and functional implications of their intrinsic disorder have never been fully assessed. Here, through large-scale analysis of comprehensive protein sequence and structure datasets we demonstrate the prevalence of intrinsic structural disorder in RNA-binding proteins and domains. We addressed their functionality through a quantitative description of the evolutionary conservation of disordered segments involved in binding, and investigated the structural implications of flexibility in terms of conformational stability and interface formation. We conclude that the functional role of intrinsically disordered protein segments in RNA-binding is two-fold: first, these regions establish extended, conserved electrostatic interfaces with RNAs via induced fit. Second, conformational flexibility enables them to target different RNA partners, providing multi-functionality, while also ensuring specificity. These findings emphasize the functional importance of intrinsically disordered regions in RNA-binding proteins.

DOI10.1371/journal.pone.0139731
Alternate JournalPLoS ONE
PubMed ID26439842
PubMed Central IDPMC4595337
Research group: