ArticleGenes & development2017
Structures of partition protein ParA with nonspecific DNA and ParB effector reveal molecular insights into principles governing Walker-box DNA segregation.
Article in Genes & development, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 64 citations in OpenAlex.
- A dual-function regulatory element couples ParB expression and DNA substrate specificity.bioRxiv : the preprint server for biology · 2026Article
- OT-Curtains: an approach for studying protein interactions with DNA ends using optical tweezers and confocal fluorescence microscopy.Nucleic acids research · 2026Article
- SMC ensures efficient chromosome replication and oriC positioning during Streptomyces spore germination.Scientific reports · 2026Article
- SMC modulates ParB engagement in segregation complexes in streptomyces.Nature communications · 2025Article
- Article
- Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation.Nature communications · 2025Article
- Expanding the diversity of bacterial DNA partitioning: A CTP-independent ParABProceedings of the National Academy of Sciences of the United States of America · 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
- Mutational analysis of the F plasmid partitioning protein ParA reveals residues required for oligomerization and plasmid maintenance.Nucleic acids research · 2025Article
- DNA supercoiling enhances DNA condensation by ParB proteins.Nucleic acids research · 2024Article
- TPGPred: A Mixed-Feature-Driven Approach for Identifying Thermophilic Proteins Based on GradientBoosting.International journal of molecular sciences · 2024Article
- Unraveling the structure and function of a novel SegC protein interacting with the SegAB chromosome segregation complex in Archaea.Nucleic acids research · 2024Article
- Insights into the molecular mechanism of ParABS system in chromosome partition by HpParA and HpParB.Nucleic acids research · 2024Article
- Positioning of cellular components by the ParA/MinD family of ATPases.Current opinion in microbiology · 2024Review
- Connecting the dots: key insights on ParB for chromosome segregation from single-molecule studies.FEMS microbiology reviews · 2024Review
- Kinetic principles of ParA2-ATP cycling guide dynamic subcellular localizations in Vibrio cholerae.Nucleic acids research · 2023Article
- A new role for monomeric ParA/Soj in chromosome dynamics in Bacillus subtilis.MicrobiologyOpen · 2023Article
- Strain-Specific Gifsy-1 Prophage Genes Are Determinants for Expression of the RNA Repair Operon during the SOS Response in Salmonella enterica Serovar Typhimurium.Journal of bacteriology · 2023Article
- Molecular Analysis of pSK1 par: A Novel Plasmid Partitioning System Encoded by Staphylococcal Multiresistance Plasmids.Journal of molecular biology · 2022Article
- Chromosome remodelling by SMC/Condensin inProceedings of the National Academy of Sciences of the United States of America · 2022Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Walker-box partition systems are ubiquitous in nature and mediate the segregation of bacterial and archaeal DNA. Well-studied plasmid Walker-box partition modules require ParA, centromere-DNA, and a centromere-binding protein, ParB. In these systems, ParA-ATP binds nucleoid DNA and uses it as a substratum to deliver ParB-attached cargo DNA, and ParB drives ParA dynamics, allowing ParA progression along the nucleoid. How ParA-ATP binds nonspecific DNA and is regulated by ParB is unclear. Also under debate is whether ParA polymerizes on DNA to mediate segregation. Here we describe structures of key ParA segregation complexes. The ParA-β,γ-imidoadenosine 5'-triphosphate (AMPPNP)-DNA structure revealed no polymers. Instead, ParA-AMPPNP dimerization creates a multifaceted DNA-binding surface, allowing it to preferentially bind high-density DNA regions (HDRs). DNA-bound ParA-AMPPNP adopts a dimer conformation distinct from the ATP sandwich dimer, optimized for DNA association. Our ParA-AMPPNP-ParB structure reveals that ParB binds at the ParA dimer interface, stabilizing the ATPase-competent ATP sandwich dimer, ultimately driving ParA DNA dissociation. Thus, the data indicate how harnessing a conformationally adaptive dimer can drive large-scale cargo movement without the requirement for polymers and suggest a segregation mechanism by which ParA-ATP dimers equilibrate to HDRs shown to be localized near cell poles of dividing chromosomes, thus mediating equipartition of attached ParB-DNA substrates.
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