ArticleProceedings of the National Academy of Sciences of the United States of America2015
Insights into ParB spreading from the complex structure of Spo0J and parS.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 84 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
- Versatile NTP recognition and domain fusions expand the functional repertoire of the ParB-CTPase fold beyond chromosome segregation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- SMC modulates ParB engagement in segregation complexes in streptomyces.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
- 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
- Two birds with one stone: SGI1 can stabilize itself and expel the IncC helper by hijacking the plasmid parABS system.Nucleic acids research · 2024Article
- Connecting the dots: key insights on ParB for chromosome segregation from single-molecule studies.FEMS microbiology reviews · 2024Review
- The virulence regulator VirB from Shigella flexneri uses a CTP-dependent switch mechanism to activate gene expression.Nature communications · 2024Article
- 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
- Recipient UvrD helicase is involved in single- to double-stranded DNA conversion during conjugative plasmid transfer.Nucleic acids research · 2023Article
- Programmable synthetic biomolecular condensates for cellular control.Nature chemical biology · 2023Article
- Diverse Partners of the Partitioning ParB Protein in Pseudomonas aeruginosa.Microbiology spectrum · 2023Article
- A joint-ParB interface promotes Smc DNA recruitment.Cell reports · 2022Article
- ParB proteins can bypass DNA-bound roadblocks via dimer-dimer recruitment.Science advances · 2022Article
- Catching a Walker in the Act-DNA Partitioning by ParA Family of Proteins.Frontiers in microbiology · 2022Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spo0J (stage 0 sporulation protein J, a member of the ParB superfamily) is an essential component of the ParABS (partition system of ParA, ParB, and parS)-related bacterial chromosome segregation system. ParB (partition protein B) and its regulatory protein, ParA, act cooperatively through parS (partition S) DNA to facilitate chromosome segregation. ParB binds to chromosomal DNA at specific parS sites as well as the neighboring nonspecific DNA sites. Various ParB molecules can associate together and spread along the chromosomal DNA. ParB oligomer and parS DNA interact together to form a high-order nucleoprotein that is required for the loading of the structural maintenance of chromosomes proteins onto the chromosome for chromosomal DNA condensation. In this report, we characterized the binding of parS and Spo0J from Helicobacter pylori (HpSpo0J) and solved the crystal structure of the C-terminal domain truncated protein (Ct-HpSpo0J)-parS complex. Ct-HpSpo0J folds into an elongated structure that includes a flexible N-terminal domain for protein-protein interaction and a conserved DNA-binding domain for parS binding. Two Ct-HpSpo0J molecules bind with one parS. Ct-HpSpo0J interacts vertically and horizontally with its neighbors through the N-terminal domain to form an oligomer. These adjacent and transverse interactions are accomplished via a highly conserved arginine patch: RRLR. These interactions might be needed for molecular assembly of a high-order nucleoprotein complex and for ParB spreading. A structural model for ParB spreading and chromosomal DNA condensation that lead to chromosome segregation is proposed.
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