ArticleNucleic acids research2024
Phase-separated ParB enforces diverse DNA compaction modes and stabilizes the parS-centered partition complex.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Bacterial ribonucleoprotein bodies maintain an acidic pH environment as a mechanism of enzyme regulation.Nature communications · 2026Article
- Molecular Insights on the Assembling of ParB1 and ParB1-ACS bio & med chem Au · 2026Article
- Fast assembly and in vivo coalescence of ParBF biocondensates involved in bacterial DNA partition.Nucleic acids research · 2026Article
- Dual and opposing roles of the EXD2 exonuclease in the resolution of RNA-DNA hybrids.Nucleic acids research · 2026Article
- Bacillus subtilis ParB C-terminal lysine residues are essential for dimerization and in vivo function, indicating their roles in DNA sliding.Nucleic acids research · 2026Article
- Beyond bactericidal: targeting plasmid-mediated antibiotic resistance with natural product-based plasmid curing agents.Frontiers in microbiology · 2026Review
- SMC modulates ParB engagement in segregation complexes in streptomyces.Nature communications · 2025Article
- Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation.Nature communications · 2025Article
- The ParB-CTP cycle activates phase separation in bacterial DNA segregation.Nucleic acids research · 2025Article
- Coupling chromosome organization to genome segregation in Archaea.Nature communications · 2025Article
- Significance of the CTP-binding motif for the interactions of S. coelicolor ParB with DNA, chromosome segregation, and sporogenic hyphal growth.Nucleic acids research · 2025Article
Corrections and comments
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Authors and funding
12 authors.
Funding
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 compression of adjacent DNA and the looping of distant DNA. Notably, the presence of CTP promotes the formation of condensates by a low amount of ParB at parS sites, triggering two-step DNA condensation. Remarkably, parS-centered ParB-DNA co-condensate constitutes a robust nucleoprotein architecture capable of withstanding disruptive forces of tens of piconewton. Overall, our findings unveil diverse modes of DNA compaction enabled by phase-separated ParB and offer new insights into the dynamic assembly and maintenance of the bacterial partition complex.
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