ArticleNature communications2025
Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- A dual-function regulatory element couples ParB expression and DNA substrate specificity.bioRxiv : the preprint server for biology · 2026Article
- Stable inheritance of the Streptomyces linear plasmid SCP1 by dual ParABS partition systems.Nucleic acids research · 2026Article
- Article
- 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
- Brownian ratchet mechanisms for carboxysome positioning in bacteria.Current opinion in microbiology · 2025Review
- Tuning the interaction of a ParA-type ATPase with its partner separates bacterial organelle positioning from partitioning.Research square · 2025Article
- Tuning the interaction of a ParA-type ATPase with its partner separates bacterial organelle positioning from partitioning.bioRxiv : the preprint server for biology · 2025Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
DNA segregation by bacterial ParABS systems is mediated by transient tethering interactions between nucleoid-bound dimers of the ATPase ParA and centromere (parS)-associated complexes of the clamp-forming CTPase ParB. The lifetime of these interactions is limited by the ParB-dependent activation of ParA ATPase activity. Here, we elucidate the functional interplay between ParA and ParB in the model bacterium Myxococcus xanthus. We demonstrate that the N-terminal ParA-binding motif of ParB associates with a conserved bipartite binding pocket at the ParA dimer interface, in a manner dependent on ParB clamp closure. Moreover, we show that ParB and non-specific DNA interact cooperatively with ParA and synergistically induce structural changes in its Walker A and Walker B motifs that correlate with the activation of ParA ATPase activity. These results advance our understanding of the mechanism underlying DNA transport by the ParABS system and may help to unravel the mode of action of related cargo-positioning systems.
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