ArticleProceedings of the National Academy of Sciences of the United States of America2014
Bacterial tubulin TubZ-Bt transitions between a two-stranded intermediate and a four-stranded filament upon GTP hydrolysis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- Article
- Identifying the core genome of the nucleus-forming bacteriophage family and characterization of Erwinia phage RAY.Cell reports · 2023Article
- 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
- 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
- Prokaryotic cytoskeletons: protein filaments organizing small cells.Nature reviews. Microbiology · 2018Review
- The Phage Nucleus and Tubulin Spindle Are Conserved among Large Pseudomonas Phages.Cell reports · 2017Article
- TubZ filament assembly dynamics requires the flexible C-terminal tail.Scientific reports · 2017Article
- Novel actin filaments from Bacillus thuringiensis form nanotubules for plasmid DNA segregation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- 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
- X-ray crystallography over the past decade for novel drug discovery - where are we heading next?Expert opinion on drug discovery · 2015Review
- A novel transcriptional activator, tubX, is required for the stability of Bacillus sphaericus mosquitocidal plasmid pBsph.Journal of bacteriology · 2014Article
- Article
- Inside out: tubulin cytomotive filaments versus microtubules.Structure (London, England : 1993) · 2014Article
- Plasmid segregation by a moving ATPase gradient.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Cytoskeletal filaments form diverse superstructures that are highly adapted for specific functions. The recently discovered TubZ subfamily of tubulins is involved in type III plasmid partitioning systems, facilitating faithful segregation of low copy-number plasmids during bacterial cell division. One such protein, TubZ-Bt, is found on the large pBtoxis plasmid in Bacillus thuringiensis, and interacts via its extended C terminus with a DNA adaptor protein TubR. Here, we use cryo-electron microscopy to determine the structure of TubZ-Bt filaments and light scattering to explore their mechanism of polymerization. Surprisingly, we find that the helical filament architecture is remarkably sensitive to nucleotide state, changing from two-stranded to four-stranded depending on the ability of TubZ-Bt to hydrolyze GTP. We present pseudoatomic models of both the two- and four-protofilament forms based on cryo-electron microscopy reconstructions (10.8 Å and 6.9 Å, respectively) of filaments formed under different nucleotide states. These data lead to a model in which the two-stranded filament is a necessary intermediate along the pathway to formation of the four-stranded filament. Such nucleotide-directed structural polymorphism is to our knowledge an unprecedented mechanism for the formation of polar filaments.
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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.