RT Journal Article
SR Electronic
T1 Intrinsically disordered regions contribute promiscuous interactions to RNP granule assembly
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 147561
DO 10.1101/147561
A1 David S. W. Protter
A1 Bhalchandra S. Rao
A1 Briana Van Treeck
A1 Yuan Lin
A1 Laura Mizoue
A1 Michael K. Rosen
A1 Roy Parker
YR 2017
UL http://biorxiv.org/content/early/2017/06/12/147561.abstract
AB Eukaryotic cells contain large RNA-protein assemblies referred to as RNP granules, whose assembly is promoted by both traditional protein interactions and intrinsically disordered protein domains. Using RNP granules as an example, we provide evidence for an assembly mechanism of large cellular structures wherein specific protein-protein or protein-RNA interactions act together with promiscuous interactions of intrinsically disordered regions (IDRs). This synergistic assembly mechanism illuminates RNP granule assembly, and explains why many components of RNP granules, and other large dynamic assemblies, contain IDRs linked to specific protein-protein or protein-RNA interaction modules. We suggest assemblies based on combinations of specific interactions and promiscuous IDRs are common features of eukaryotic cells.