ArticleThe Journal of biological chemistry2008
In vitro assembly studies of FtsZ/tubulin-like proteins (TubZ) from Bacillus plasmids: evidence for a capping mechanism.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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Who cites it
25 citing papers in PubMed, 47 citations in OpenAlex.
- Cinnamaldehyde derivatives act as antimicrobial agents againstFrontiers in microbiology · 2022Article
- Catching a Walker in the Act-DNA Partitioning by ParA Family of Proteins.Frontiers in microbiology · 2022Review
- The Phage Nucleus and Tubulin Spindle Are Conserved among Large Pseudomonas Phages.Cell reports · 2017Article
- The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red AlgaThe Journal of biological chemistry · 2017Article
- TubZ filament assembly dynamics requires the flexible C-terminal tail.Scientific reports · 2017Article
- 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
- Article
- 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
- Rapid in vitro assembly of Caulobacter crescentus FtsZ protein at pH 6.5 and 7.2.The Journal of biological chemistry · 2013Article
- Structure of the tubulin/FtsZ-like protein TubZ from Pseudomonas bacteriophage ΦKZ.Journal of molecular biology · 2013Article
- Crystallization and preliminary X-ray data analysis of the pXO1 plasmid-partitioning factor TubZ from Bacillus cereus.Acta crystallographica. Section F, Structural biology and crystallization communications · 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
- Filament formation of the FtsZ/tubulin-like protein TubZ from the Bacillus cereus pXO1 plasmid.The Journal of biological chemistry · 2012Article
- Article
- Tubulin homolog TubZ in a phage-encoded partition system.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- SulA inhibits assembly of FtsZ by a simple sequestration mechanism.Biochemistry · 2012Article
- Bacterial plasmid partition machinery: a minimalist approach to survival.Current opinion in structural biology · 2012Review
- Filament structure of bacterial tubulin homologue TubZ.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- One-way ticket to the cell pole: plasmid transport by the prokaryotic tubulin homolog TubZ.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Proteins with a weak sequence similarity to tubulin and FtsZ are expressed from large plasmids of Bacillus anthracis and Bacillus thuringiensis and are probably involved in plasmid segregation. Previously designated RepX and TubZ, we designate them here as TubZ-Ba and TubZ-Bt. We have expressed and purified the proteins for in vitro studies. TubZ-Ba and TubZ-Bt share only 21% amino acid identity, but they have remarkably similar biochemical properties. They both assemble into two-stranded filaments and larger bundles above a critical concentration, and they hydrolyze GTP at a very high rate, approximately 20 GTP min(-1) TubZ(-1). Assembly is also supported by GTPgammaS. A tiny amount of GTPgammaS stabilizes polymers assembled in GTP and inhibits the GTPase by a mechanism involving cooperativity. The nucleotide in the polymers is almost 100% GDP, which is similar to microtubules but very different from the 20-30% GDP in FtsZ polymers. This suggests that the TubZ polymers have a capping mechanism that may be related to the GTP cap that produces dynamic instability of microtubules.
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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.