ArticleProceedings of the National Academy of Sciences of the United States of America2010
Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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45 citing papers in PubMed, 74 citations in OpenAlex.
- Structural insights into CodY activation and DNA recognition.Nucleic acids research · 2023Article
- Molecular Analysis of pSK1 par: A Novel Plasmid Partitioning System Encoded by Staphylococcal Multiresistance Plasmids.Journal of molecular biology · 2022Article
- Catching a Walker in the Act-DNA Partitioning by ParA Family of Proteins.Frontiers in microbiology · 2022Review
- Unique Properties of the Alpha-Helical DNA-Binding Protein KfrA Encoded by the IncU Incompatibility Group Plasmid RA3 and Its Host-Dependent Role in Plasmid Maintenance.Applied and environmental microbiology · 2021Article
- 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
- β-Strand-mediated interactions of protein domains.Proteins · 2020Article
- Rules and Exceptions: The Role of Chromosomal ParB in DNA Segregation and Other Cellular Processes.Microorganisms · 2020Review
- Structures of maintenance of carboxysome distribution Walker-box McdA and McdB adaptor homologs.Nucleic acids research · 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
- Review
- Biochemical and structural characterization of a novel cooperative binding mode by Pit-1 with CATT repeats in the macrophage migration inhibitory factor promoter.Nucleic acids research · 2018Article
- Structures of partition protein ParA with nonspecific DNA and ParB effector reveal molecular insights into principles governing Walker-box DNA segregation.Genes & development · 2017Article
- TubZ filament assembly dynamics requires the flexible C-terminal tail.Scientific reports · 2017Article
- Segrosome Complex Formation during DNA Trafficking in Bacterial Cell Division.Frontiers in molecular biosciences · 2016Review
- 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
- Breaking and restoring the hydrophobic core of a centromere-binding protein.The Journal of biological chemistry · 2015Article
- Bacterial actin and tubulin homologs in cell growth and division.Current biology : CB · 2015Review
- A novel transcriptional activator, tubX, is required for the stability of Bacillus sphaericus mosquitocidal plasmid pBsph.Journal of bacteriology · 2014Article
- Amino acid residues of RegA important for interactions with the CbbR-DNA complex of Rhodobacter sphaeroides.Journal of bacteriology · 2014Article
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4 authors at 1 institution in 1 country.
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Abstract
The segregation of plasmid DNA typically requires three elements: a DNA centromere site, an NTPase, and a centromere-binding protein. Because of their simplicity, plasmid partition systems represent tractable models to study the molecular basis of DNA segregation. Unlike eukaryotes, which utilize the GTPase tubulin to segregate DNA, the most common plasmid-encoded NTPases contain Walker-box and actin-like folds. Recently, a plasmid stability cassette on Bacillus thuringiensis pBtoxis encoding a putative FtsZ/tubulin-like NTPase called TubZ and DNA-binding protein called TubR has been described. How these proteins collaborate to impart plasmid stability, however, is unknown. Here we show that the TubR structure consists of an intertwined dimer with a winged helix-turn-helix (HTH) motif. Strikingly, however, the TubR recognition helices mediate dimerization, making canonical HTH-DNA interactions impossible. Mutagenesis data indicate that a basic patch, encompassing the two wing regions and the N termini of the recognition helices, mediates DNA binding, which indicates an unusual HTH-DNA interaction mode in which the N termini of the recognition helices insert into a single DNA groove and the wings into adjacent DNA grooves. The TubZ structure shows that it is as similar structurally to eukaryotic tubulin as it is to bacterial FtsZ. TubZ forms polymers with guanine nucleotide-binding characteristics and polymer dynamics similar to tubulin. Finally, we show that the exposed TubZ C-terminal region interacts with TubR-DNA, linking the TubR-bound pBtoxis to TubZ polymerization. The combined data suggest a mechanism for TubZ-polymer powered plasmid movement.
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