Shape transformations in peptide-DNA coacervates driven by enzyme-catalyzed deacetylation.

ABSTRACT: Biomolecular condensates formed by liquid-liquid phase separation (LLPS) are important organizers of biochemistry in living cells. Condensate formation can be dynamically regulated, for example, by protein binding or enzymatic processes. However, how enzymatic reactions can influence condensate shape and control shape transformations is less well understood. Here, we design a model condensate that can be formed by the enzymatic deacetylation of a small peptide by sirtuin-3 in the presence of DNA. Interestingly, upon nucleation condensates initially form gel-like aggregates that gradually transform into spherical droplets, displaying fusion and wetting. This process is governed by sirtuin-3 concentration, as more enzyme results in a faster aggregate-to-liquid transformation of the condensat

SUBMITTER: van Haren MHI 

PROVIDER: S-EPMC11582960 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature