The abundant nuclear RNA binding protein FUS binds the C-terminal domain (CTD) of RNA polymerase II inan RNA-dependent manner, affecting Ser2 phosphorylation and transcription. Here, we examine the mechanism of this process and find that RNA binding nucleates the formation of higher-order FUS ribonucleoprotein assemblies that bind the CTD. Both the low-complexity domain and the arginine-glycine rich domain of FUS contribute to assembly. The assemblies appear fibrous by electron microscopy and have characteristics of β zipper structures. These results support the emerging view that the pathologic protein aggregation seen in neurodegenerative diseases such as amyotrophic lateral sclerosis may occur via the exaggeration of functionally important assemblies of RNA binding proteins.
|Original language||English (US)|
|Number of pages||8|
|State||Published - Nov 27 2013|
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)