Polymer compaction and bridging-induced clustering of protein-inspired patchy particles

TL;DR

This study uses simulations to explore how protein-like particles with multiple binding sites induce DNA compaction and clustering through bridging, revealing the influence of protein valence and shape on these processes.

Contribution

It extends previous models by incorporating detailed patchy particles to analyze polymer compaction and bridging-induced clustering mechanisms.

Findings

Protein valence affects compaction and clustering.

Protein shape influences bridging ability.

Bridging-induced attraction occurs without explicit protein-protein attraction.

Abstract

There are many proteins or protein complexes which have multiple DNA binding domains. This allows them to bind to multiple points on a DNA molecule (or chromatin fibre) at the same time. There are also many proteins which have been found to be able to compact DNA in vitro, and many others have been observed in foci or puncta when fluorescently labelled and imaged in vivo. In this work we study, using coarse-grained Langevin dynamics simulations, the compaction of polymers by simple model proteins and a phenomenon known as the "bridging-induced attraction". The latter is a mechanism observed in previous simulations [Brackley et al., Proc. Natl. Acad. Sci. USA 110 (2013)], where proteins modelled as spheres form clusters via their multivalent interactions with a polymer, even in the absence of any explicit protein-protein attractive interactions. Here we extend this concept to consider more detailed model proteins, represented as simple "patchy particles" interacting with a semi-flexible bead-and-spring polymer. We find that both the compacting ability and the effect of the bridging-induced attraction depend on the valence of the model proteins. These effects also depend on the shape of the protein, which determines its ability to form bridges.