Arginine-Enriched Mixed-Charge Domains Provide Cohesion for Nuclear Speckle Condensation.

ABSTRACT: Low-complexity protein domains promote the formation of various biomolecular condensates. However, in many cases, the precise sequence features governing condensate formation and identity remain unclear. Here, we investigate the role of intrinsically disordered mixed-charge domains (MCDs) in nuclear speckle condensation. Proteins composed exclusively of arginine-aspartic acid dipeptide repeats undergo length-dependent condensation and speckle incorporation. Substituting arginine with lysine in synthetic and natural speckle-associated MCDs abolishes these activities, identifying a key role for multivalent contacts through arginine's guanidinium ion. MCDs can synergize with a speckle-associated RNA recognition motif to promote speckle specificity and residence. MCD behavior is tunable throug

SUBMITTER: Greig JA 

PROVIDER: S-EPMC10715173 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature