Article

Abstract

• The abundant nuclear RNA binding protein FUS binds the C-terminal domain (CTD) of RNApolymerase II in an RNA-dependent manner, affecting Ser2 phosphorylation and transcription. Here, we examine the mechanism of this process and find that RNA binding nucleates the formation ofhigher-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 ofRNA binding proteins.

Creator

• Schwartz, Jacob V.
• Cech, Thomas R.
• Wang, Xueyin
• Podell, Elaine R.

Date Issued

• 2013-11-27

Academic Affiliation

• Chemical and Biological Engineering

Journal Title

• Cell Reports

Journal Issue/Number

• 4

Journal Volume

• 5

File Extent

• 918-925

Última modificação

• 2019-12-05

Resource Type

• Article

Declaração de direitos

• In Copyright

DOI

• 10.1016/j.celrep.2013.11.017

Language

• English [eng]

Relações

Itens

Miniatura	Título	Data de carga	Acesso	Ações
	rnaSeedsHigherOrderAssemblyOfFusProtein.pdf	2019-12-05	Público	Baixar