Intrinsically disordered sequences enable modulation of protein phase separation through distributed tyrosine motifs.

ABSTRACT: Liquid-liquid phase separation (LLPS) is thought to contribute to the establishment of many biomolecular condensates, eukaryotic cell structures that concentrate diverse macromolecules but lack a bounding membrane. RNA granules control RNA metabolism and comprise a large class of condensates that are enriched in RNA-binding proteins and RNA molecules. Many RNA granule proteins are composed of both modular domains and intrinsically disordered regions (IDRs) having low amino acid sequence complexity. Phase separation of these molecules likely plays an important role in the generation and stability of RNA granules. To understand how folded domains and IDRs can cooperate to modulate LLPS, we generated a series of engineered proteins. These were based on fusions of an IDR derived from the RNA g

SUBMITTER: Lin Y 

PROVIDER: S-EPMC5704491 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature