ArticleProceedings of the National Academy of Sciences of the United States of America2014
Condensation and localization of the partitioning protein ParB on the bacterial chromosome.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 115 citations in OpenAlex.
- Unlocking the bacterial condensome: from "dark matter" to design.Molecular biology of the cell · 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
- Protein-DNA co-condensation is prewetting to a collapsed polymer.Biophysical journal · 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
- Article
- Remote Regulation by VirB, the Transcriptional Anti-Silencer of Shigella Virulence Genes, Provides Mechanistic Information.Molecular microbiology · 2025Article
- Physical models of bacterial chromosomes.Molecular microbiology · 2025Review
- 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
- Interplay of condensation and chromatin binding underlies BRD4 targeting.Molecular biology of the cell · 2024Article
- Bridging DNA contacts allow Dps from E. coli to condense DNA.Nucleic acids research · 2024Article
- Direct observation of a crescent-shape chromosome in expanded Bacillus subtilis cells.Nature communications · 2024Article
- Bridging DNA contacts allow Dps frombioRxiv : the preprint server for biology · 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
- VirB, a key transcriptional regulator ofmBio · 2023Article
- Partition complex structure can arise from sliding and bridging of ParB dimers.Nature communications · 2023Article
- VirB, a key transcriptional regulator ofbioRxiv : the preprint server for biology · 2023Article
- Diverse Partners of the Partitioning ParB Protein in Pseudomonas aeruginosa.Microbiology spectrum · 2023Article
- Simulating the chromatin-mediated phase separation of model proteins with multiple domains.Biophysical journal · 2022Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
Abstract
The ParABS system mediates chromosome segregation and plasmid partitioning in many bacteria. As part of the partitioning mechanism, ParB proteins form a nucleoprotein complex at parS sites. The biophysical basis underlying ParB-DNA complex formation and localization remains elusive. Specifically, it is unclear whether ParB spreads in 1D along DNA or assembles into a 3D protein-DNA complex. We show that a combination of 1D spreading bonds and a single 3D bridging bond between ParB proteins constitutes a minimal model for a condensed ParB-DNA complex. This model implies a scaling behavior for ParB-mediated silencing of parS-flanking genes, which we confirm to be satisfied by experimental data from P1 plasmids. Furthermore, this model is consistent with experiments on the effects of DNA roadblocks on ParB localization. Finally, we show experimentally that a single parS site is necessary and sufficient for ParB-DNA complex formation in vivo. Together with our model, this suggests that ParB binding to parS triggers a conformational switch in ParB that overcomes a nucleation barrier. Conceptually, the combination of spreading and bridging bonds in our model provides a surface tension ensuring the condensation of the ParB-DNA complex, with analogies to liquid-like compartments such as nucleoli in eukaryotes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.