ArticleThe Journal of biological chemistry2015
The Cell Division Protein FtsZ from Streptococcus pneumoniae Exhibits a GTPase Activity Delay.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Targeting Bacterial Cell Division with Benzodioxane-Benzamide FtsZ Inhibitors as a Novel Strategy to Fight Gram-Positive Ovococcal Pathogens.International journal of molecular sciences · 2025Article
- A key bacterial cytoskeletal cell division protein FtsZ as a novel therapeutic antibacterial drug target.Bosnian journal of basic medical sciences · 2020Review
- Structural features of the interaction of MapZ with FtsZ and membranes in Streptococcus pneumoniae.Scientific reports · 2020Article
- Assembly properties of the bacterial tubulin homolog FtsZ from the cyanobacteriumThe Journal of biological chemistry · 2019Article
- Movement dynamics of divisome proteins and PBP2x:FtsW in cells ofProceedings of the National Academy of Sciences of the United States of America · 2019Article
- An essentialeLife · 2018Article
- Unite to divide: Oligomerization of tubulin and actin homologs regulates initiation of bacterial cell division.F1000Research · 2018Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cell division protein FtsZ assembles in vitro by a mechanism of cooperative association dependent on GTP, monovalent cations, and Mg(2+). We have analyzed the GTPase activity and assembly dynamics of Streptococcus pneumoniae FtsZ (SpnFtsZ). SpnFtsZ assembled in an apparently cooperative process, with a higher critical concentration than values reported for other FtsZ proteins. It sedimented in the presence of GTP as a high molecular mass polymer with a well defined size and tended to form double-stranded filaments in electron microscope preparations. GTPase activity depended on K(+) and Mg(2+) and was inhibited by Na(+). GTP hydrolysis exhibited a delay that included a lag phase followed by a GTP hydrolysis activation step, until reaction reached the GTPase rate. The lag phase was not found in polymer assembly, suggesting a transition from an initial non-GTP-hydrolyzing polymer that switches to a GTP-hydrolyzing polymer, supporting models that explain FtsZ polymer cooperativity.
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