ArticleProceedings of the National Academy of Sciences of the United States of America2012
Superstructure of the centromeric complex of TubZRC plasmid partitioning systems.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Cyanobacterial membrane dynamics in the light of eukaryotic principles.Bioscience reports · 2023Article
- Molecular Analysis of pSK1 par: A Novel Plasmid Partitioning System Encoded by Staphylococcal Multiresistance Plasmids.Journal of molecular biology · 2022Article
- A general method for directly phasing diffraction data from high-solvent-content protein crystals.IUCrJ · 2022Article
- Catching a Walker in the Act-DNA Partitioning by ParA Family of Proteins.Frontiers in microbiology · 2022Review
- The C-terminal region of the plasmid partitioning protein TubY is a tetramer that can bind membranes and DNA.The Journal of biological chemistry · 2020Article
- 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
- The IntXO-PSL Recombination System Is a Key Component of the Second Maintenance System for Bacillus anthracis Plasmid pXO1.Journal of bacteriology · 2016Article
- Can I solve my structure by SAD phasing? Planning an experiment, scaling data and evaluating the useful anomalous correlation and anomalous signal.Acta crystallographica. Section D, Structural biology · 2016Article
- Can I solve my structure by SAD phasing? Anomalous signal in SAD phasing.Acta crystallographica. Section D, Structural biology · 2016Article
- Segrosome Complex Formation during DNA Trafficking in Bacterial Cell Division.Frontiers in molecular biosciences · 2016Review
- Bacterial Filament Systems: Toward Understanding Their Emergent Behavior and Cellular Functions.The Journal of biological chemistry · 2015Review
- Reconstitution of a prokaryotic minus end-tracking system using TubRC centromeric complexes and tubulin-like protein TubZ filaments.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A novel transcriptional activator, tubX, is required for the stability of Bacillus sphaericus mosquitocidal plasmid pBsph.Journal of bacteriology · 2014Article
- Identification of three noncontiguous regions on Bacillus anthracis plasmid pXO1 that are important for its maintenance.Journal of bacteriology · 2014Article
- Bacterial tubulin TubZ-Bt transitions between a two-stranded intermediate and a four-stranded filament upon GTP hydrolysis.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The internal organization of mycobacterial partition assembly: does the DNA wrap a protein core?PloS one · 2012Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Bacterial plasmid partitioning systems segregate plasmids into each daughter cell. In the well-understood ParMRC plasmid partitioning system, adapter protein ParR binds to centromere parC, forming a helix around which the DNA is externally wrapped. This complex stabilizes the growth of a filament of actin-like ParM protein, which pushes the plasmids to the poles. The TubZRC plasmid partitioning system consists of two proteins, tubulin-like TubZ and TubR, and a DNA centromere, tubC, which perform analogous roles to those in ParMRC, despite being unrelated in sequence and structure. We have dissected in detail the binding sites that comprise Bacillus thuringiensis tubC, visualized the TubRC complex by electron microscopy, and determined a crystal structure of TubR bound to the tubC repeat. We show that the TubRC complex takes the form of a flexible DNA-protein filament, formed by lateral coating along the plasmid from tubC, the full length of which is required for the successful in vitro stabilization of TubZ filaments. We also show that TubR from Bacillus megaterium forms a helical superstructure resembling that of ParR. We suggest that the TubRC DNA-protein filament may bind to, and stabilize, the TubZ filament by forming such a ring-like structure around it. The helical superstructure of this TubRC may indicate convergent evolution between the actin-containing ParMRC and tubulin-containing TubZRC systems.
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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.