ArticleThe Journal of biological chemistry2012
Structural mechanism of ATP-induced polymerization of the partition factor ParF: implications for DNA segregation.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- 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
- Kinetic principles of ParA2-ATP cycling guide dynamic subcellular localizations in Vibrio cholerae.Nucleic acids research · 2023Article
- Multiple ParA/MinD ATPases coordinate the positioning of disparate cargos in a bacterial cell.Nature communications · 2023Article
- Catching a Walker in the Act-DNA Partitioning by ParA Family of Proteins.Frontiers in microbiology · 2022Review
- Dissection of the ATPase active site of McdA reveals the sequential steps essential for carboxysome distribution.Molecular biology of the cell · 2021Article
- Identification of a Potential Membrane-Targeting Sequence in the C-Terminus of the F Plasmid Segregation Protein SopA.The Journal of membrane biology · 2021Article
- ParC, a New Partitioning Protein, Is Necessary for the Active Form of ParA FromFrontiers in microbiology · 2020Article
- Genome Segregation by the Venus Flytrap Mechanism: Probing the Interaction Between the ParF ATPase and the ParG Centromere Binding Protein.Frontiers in molecular biosciences · 2020Article
- Structures of maintenance of carboxysome distribution Walker-box McdA and McdB adaptor homologs.Nucleic acids research · 2019Article
- Plasmid Localization and Partition inEcoSal Plus · 2019Review
- Crystal structures of HpSoj-DNA complexes and the nucleoid-adaptor complex formation in chromosome segregation.Nucleic acids research · 2019Article
- Intrinsic disorder in the partitioning protein KorB persists after co-operative complex formation with operator DNA and KorA.The Biochemical journal · 2017Article
- A three-dimensional ParF meshwork assembles through the nucleoid to mediate plasmid segregation.Nucleic acids research · 2017Article
- Structures of partition protein ParA with nonspecific DNA and ParB effector reveal molecular insights into principles governing Walker-box DNA segregation.Genes & development · 2017Article
- Driving Apart and Segregating Genomes in Archaea.Trends in microbiology · 2016Review
- Segrosome Complex Formation during DNA Trafficking in Bacterial Cell Division.Frontiers in molecular biosciences · 2016Review
- Structures of archaeal DNA segregation machinery reveal bacterial and eukaryotic linkages.Science (New York, N.Y.) · 2015Article
- Molecular Anatomy of ParA-ParA and ParA-ParB Interactions during Plasmid Partitioning.The Journal of biological chemistry · 2015Article
- Breaking and restoring the hydrophobic core of a centromere-binding protein.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Segregation of the bacterial multidrug resistance plasmid TP228 requires the centromere-binding protein ParG, the parH centromere, and the Walker box ATPase ParF. The cycling of ParF between ADP- and ATP-bound states drives TP228 partition; ATP binding stimulates ParF polymerization, which is essential for segregation, whereas ADP binding antagonizes polymerization and inhibits DNA partition. The molecular mechanism involved in this adenine nucleotide switch is unclear. Moreover, it is unknown how any Walker box protein polymerizes in an ATP-dependent manner. Here, we describe multiple ParF structures in ADP- and phosphomethylphosphonic acid adenylate ester (AMPPCP)-bound states. ParF-ADP is monomeric but dimerizes when complexed with AMPPCP. Strikingly, in ParF-AMPPCP structures, the dimers interact to create dimer-of-dimer "units" that generate a specific linear filament. Mutation of interface residues prevents both polymerization and DNA segregation in vivo. Thus, these data provide insight into a unique mechanism by which a Walker box protein forms polymers that involves the generation of ATP-induced dimer-of-dimer building blocks.
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Registered trials
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.