ArticleThe EMBO journal2007
Structural analysis of the ParR/parC plasmid partition complex.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 79 citations in OpenAlex.
- DNA Segregation in Enterobacteria.EcoSal Plus · 2023Review
- Article
- Chromosome segregation in Archaea: SegA- and SegB-DNA complex structures provide insights into segrosome assembly.Nucleic acids research · 2021Article
- The structure of a 15-stranded actin-like filament from Clostridium botulinum.Nature communications · 2019Article
- Plasmid Localization and Partition inEcoSal Plus · 2019Review
- The TubR-centromere complex adopts a double-ring segrosome structure in Type III partition systems.Nucleic acids research · 2018Article
- Segrosome Complex Formation during DNA Trafficking in Bacterial Cell Division.Frontiers in molecular biosciences · 2016Review
- Conjugative DNA Transfer Is Enhanced by Plasmid R1 Partitioning Proteins.Frontiers in molecular biosciences · 2016Article
- Bacterial Filament Systems: Toward Understanding Their Emergent Behavior and Cellular Functions.The Journal of biological chemistry · 2015Review
- Structures of actin-like ParM filaments show architecture of plasmid-segregating spindles.Nature · 2015Article
- Replication and Active Partition of Integrative and Conjugative Elements (ICEs) of the SXT/R391 Family: The Line between ICEs and Conjugative Plasmids Is Getting Thinner.PLoS genetics · 2015Article
- A model for the evolution of biological specificity: a cross-reacting DNA-binding protein causes plasmid incompatibility.Journal of bacteriology · 2014Article
- Bacterial actins and their diversity.Biochemistry · 2013Review
- Structure of the ParM filament at 8.5Å resolution.Journal of structural biology · 2013Article
- A bipolar spindle of antiparallel ParM filaments drives bacterial plasmid segregation.Science (New York, N.Y.) · 2012Article
- Superstructure of the centromeric complex of TubZRC plasmid partitioning systems.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Bacterial actin homolog ParM: arguments for an apolar, antiparallel double helix.Journal of molecular biology · 2012Article
- Structural mechanism of ATP-induced polymerization of the partition factor ParF: implications for DNA segregation.The Journal of biological chemistry · 2012Article
- Alp7R regulates expression of the actin-like protein Alp7A in Bacillus subtilis.Journal of bacteriology · 2012Article
- Bacterial plasmid partition machinery: a minimalist approach to survival.Current opinion in structural biology · 2012Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Accurate DNA partition at cell division is vital to all living organisms. In bacteria, this process can involve partition loci, which are found on both chromosomes and plasmids. The initial step in Escherichia coli plasmid R1 partition involves the formation of a partition complex between the DNA-binding protein ParR and its cognate centromere site parC on the DNA. The partition complex is recognized by a second partition protein, the actin-like ATPase ParM, which forms filaments required for the active bidirectional movement of DNA replicates. Here, we present the 2.8 A crystal structure of ParR from E. coli plasmid pB171. ParR forms a tight dimer resembling a large family of dimeric ribbon-helix-helix (RHH)2 site-specific DNA-binding proteins. Crystallographic and electron microscopic data further indicate that ParR dimers assemble into a helix structure with DNA-binding sites facing outward. Genetic and biochemical experiments support a structural arrangement in which the centromere-like parC DNA is wrapped around a ParR protein scaffold. This structure holds implications for how ParM polymerization drives active DNA transport during plasmid partition.
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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.