ArticleNucleic acids research2022
Stochastically multimerized ParB orchestrates DNA assembly as unveiled by single-molecule analysis.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Molecular Insights on the Assembling of ParB1 and ParB1-ACS bio & med chem Au · 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
- DNA supercoiling enhances DNA condensation by ParB proteins.Nucleic acids research · 2024Article
- Phase-separated ParB enforces diverse DNA compaction modes and stabilizes the parS-centered partition complex.Nucleic acids research · 2024Article
- Insights into the molecular mechanism of ParABS system in chromosome partition by HpParA and HpParB.Nucleic acids research · 2024Article
- Connecting the dots: key insights on ParB for chromosome segregation from single-molecule studies.FEMS microbiology reviews · 2024Review
- Dynamic ParB-DNA interactions initiate and maintain a partition condensate for bacterial chromosome segregation.Nucleic acids research · 2023Article
- A model industrial workhorse: Bacillus subtilis strain 168 and its genome after a quarter of a century.Microbial biotechnology · 2023Review
- Live cell imaging of DNA and RNA with fluorescent signal amplification and background reduction techniques.Frontiers in cell and developmental biology · 2023Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tripartite ParABS system mediates chromosome segregation in a wide range of bacteria. Dimeric ParB was proposed to nucleate on parS sites and spread to neighboring DNA. However, how properly distributed ParB dimers further compact chromosomal DNA into a higher-order nucleoprotein complex for partitioning remains poorly understood. Here, using a single-molecule approach, we show that tens of Bacillus subtilis ParB (Spo0J) proteins can stochastically multimerize on and stably bind to nonspecific DNA. The introduction of CTP promotes the formation and diffusion of the multimeric ParB along DNA, offering an opportunity for ParB proteins to further forgather and cluster. Intriguingly, ParB multimers can recognize parS motifs and are more inclined to remain immobile on them. Importantly, the ParB multimer features distinct capabilities of not only bridging two independent DNA molecules but also mediating their transportation, both of which are enhanced by the presence of either CTP or parS in the DNA. These findings shed new light on ParB dynamics in self-multimerization and DNA organization and help to better comprehend the assembly of the ParB-DNA partition complex.
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Registered trials
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