Protein Condensate Formation via Controlled Multimerization of Intrinsically Disordered Sequences.

ABSTRACT: Many proteins harboring low complexity or intrinsically disordered sequences (IDRs) are capable of undergoing liquid-liquid phase separation to form mesoscale condensates that function as biochemical niches with the ability to concentrate or sequester macromolecules and regulate cellular activity. Engineered disordered proteins have been used to generate programmable synthetic membraneless organelles in cells. Phase separation is governed by the strength of interactions among polypeptides with multivalency enhancing phase separation at lower concentrations. Previously, we and others demonstrated enzymatic control of IDR valency from multivalent precursors to dissolve condensed phases. Here, we develop noncovalent strategies to multimerize an individual IDR, the RGG domain of LAF-1, using p

SUBMITTER: Garabedian MV 

PROVIDER: S-EPMC9669173 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature