Protein compactness and interaction valency define the architecture of a biomolecular condensate across scales.

ABSTRACT: Non-membrane-bound biomolecular condensates have been proposed to represent an important mode of subcellular organization in diverse biological settings. However, the fundamental principles governing the spatial organization and dynamics of condensates at the atomistic level remain unclear. The Saccharomyces cerevisiae Lge1 protein is required for histone H2B ubiquitination and its N-terminal intrinsically disordered fragment (Lge1_1-80) undergoes robust phase separation. This study connects single- and multi-chain all-atom molecular dynamics simulations of Lge1_1-80 with the in vitro behavior of Lge1_1-80 condensates. Analysis of modeled protein-protein interactions elucidates the key determinants of Lge1_1-80 condensate formation and links c

SUBMITTER: Polyansky AA 

PROVIDER: S-EPMC10406433 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature