Phase-separated ParB enforces diverse DNA compaction modes and stabilizes the parS-centered partition complex.

ABSTRACT: The tripartite ParABS system mediates chromosome segregation in the majority of bacterial species. Typically, DNA-bound ParB proteins around the parS sites condense the chromosomal DNA into a higher-order multimeric nucleoprotein complex for the ParA-driven partition. Despite extensive studies, the molecular mechanism underlying the dynamic assembly of the partition complex remains unclear. Herein, we demonstrate that Bacillus subtilis ParB (Spo0J), through the multimerization of its N-terminal domain, forms phase-separated condensates along a single DNA molecule, leading to the concurrent organization of DNA into a compact structure. Specifically, in addition to the co-condensation of ParB dimers with DNA, the engagement of well-established ParB condensates with DNA allows for the compres

SUBMITTER: Zhao Y 

PROVIDER: S-EPMC11317135 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature