ArticleNature communications2021
The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Plasmid-encoded host reprogramming promotes plasmid dissemination.bioRxiv : the preprint server for biology · 2026Article
- Beyond bactericidal: targeting plasmid-mediated antibiotic resistance with natural product-based plasmid curing agents.Frontiers in microbiology · 2026Review
- Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation.Nature communications · 2025Article
- Mutational analysis of the F plasmid partitioning protein ParA reveals residues required for oligomerization and plasmid maintenance.Nucleic acids research · 2025Article
- Coordinating plasmid partition with bacterial chromosome segregation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Plasmid partitioning driven by collective migration of ParA between nucleoid lobes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- To let go or not to let go: how ParA can impact the release of the chromosomal anchoring in Caulobacter crescentus.Nucleic acids research · 2023Article
- Kinetic principles of ParA2-ATP cycling guide dynamic subcellular localizations in Vibrio cholerae.Nucleic acids research · 2023Article
- 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 4 institutions in 2 countries.
Funding
Abstract
The efficient segregation of replicated genetic material is an essential step for cell division. Bacterial cells use several evolutionarily-distinct genome segregation systems, the most common of which is the type I Par system. It consists of an adapter protein, ParB, that binds to the DNA cargo via interaction with the parS DNA sequence; and an ATPase, ParA, that binds nonspecific DNA and mediates cargo transport. However, the molecular details of how this system functions are not well understood. Here, we report the cryo-EM structure of the Vibrio cholerae ParA2 filament bound to DNA, as well as the crystal structures of this protein in various nucleotide states. These structures show that ParA forms a left-handed filament on DNA, stabilized by nucleotide binding, and that ParA undergoes profound structural rearrangements upon DNA binding and filament assembly. Collectively, our data suggest the structural basis for ParA's cooperative binding to DNA and the formation of high ParA density regions on the nucleoid.
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Registered trials
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