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

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 resulted in a faster aggregate-to-viscous liquid transformation of the condensates. We show that the aggregate-like nature of the early-stage condensates is linked to the presence of short, double-stranded DNA. The counterintuitive formation of aggregate-like, non-spherical condensates near the critical point is attributed to stronger bending of the DNA by oppositely charged peptides as the system moves away from the critical point, deeper in the two-phase region. Overall, this work shows that enzymes can induce shape transformations of condensates, and that condensate material properties do not necessarily inform about their stability. In this collection, you can find the data underlying this study.