ArticleExtremophiles : life under extreme conditions2011
Identification and characterization of a unique, zinc-containing transport ATPase essential for natural transformation in Thermus thermophilus HB27.
Article in Extremophiles : life under extreme conditions, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- The PulE ATPase is required for twitching motility and DNA donation during Thermus thermophilus transjugation.International microbiology : the official journal of the Spanish Society for Microbiology · 2025Article
- Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium.Nature communications · 2020Article
- The traffic ATPase PilF interacts with the inner membrane platform of the DNA translocator and type IV pili fromFEBS open bio · 2019Article
- Functional dissection of the three N-terminal general secretory pathway domains and the Walker motifs of the traffic ATPase PilF from Thermus thermophilus.Extremophiles : life under extreme conditions · 2018Article
- Article
- The type IV pilus assembly ATPase PilB functions as a signaling protein to regulate exopolysaccharide production in Myxococcus xanthus.Scientific reports · 2017Article
- Complete Genome Analysis ofFrontiers in microbiology · 2017Article
- Zinc coordination is essential for the function and activity of the type II secretion ATPase EpsE.MicrobiologyOpen · 2016Article
- Topology and Structure/Function Correlation of Ring- and Gate-forming Domains in the Dynamic Secretin Complex of Thermus thermophilus.The Journal of biological chemistry · 2016Article
- Article
- Editorial.FEMS microbiology reviews · 2015Article
- Exceptionally widespread nanomachines composed of type IV pilins: the prokaryotic Swiss Army knives.FEMS microbiology reviews · 2015Review
- Zinc and ATP binding of the hexameric AAA-ATPase PilF from Thermus thermophilus: role in complex stability, piliation, adhesion, twitching motility, and natural transformation.The Journal of biological chemistry · 2014Article
- Type IV pilus biogenesis, twitching motility, and DNA uptake in Thermus thermophilus: discrete roles of antagonistic ATPases PilF, PilT1, and PilT2.Applied and environmental microbiology · 2014Article
- Structure and assembly of an inner membrane platform for initiation of type IV pilus biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Phosphoproteomic analysis reveals the effects of PilF phosphorylation on type IV pilus and biofilm formation in Thermus thermophilus HB27.Molecular & cellular proteomics : MCP · 2013Article
- The DNA uptake ATPase PilF of Thermus thermophilus: a reexamination of the zinc content.Extremophiles : life under extreme conditions · 2013Article
- Structure and mechanism of the PilF DNA transformation ATPase from Thermus thermophilus.The Biochemical journal · 2013Article
- Unusual N-terminal ααβαββα fold of PilQ from Thermus thermophilus mediates ring formation and is essential for piliation.The Journal of biological chemistry · 2012Article
- Structure and function of PilQ, a secretin of the DNA transporter from the thermophilic bacterium Thermus thermophilus HB27.The Journal of biological chemistry · 2011Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermus thermophilus is a model strain to unravel the molecular basis of horizontal gene transfer in hot environments. Previous genetic studies led to the identification of a macromolecular transport machinery mediating DNA uptake in an energy-dependent manner. Here, we have addressed how the transporter is energized. Inspection of the genome sequence revealed four putative transport (AAA) ATPases but only the deletion of one, PilF, led to a transformation defect. PilF is similar to transport ATPases of type IV and type II secretions systems but has a unique N-terminal sequence that carries a triplicated GSPII domain. To characterize PilF biochemically it was produced in Escherichia coli and purified. The recombinant protein displayed NTPase activity with a preference for ATP. Gel filtration analyses combined with dynamic light scattering demonstrated that PilF is monodispersed in solution and forms a complex of 590 ± 30 kDa, indicating a homooligomer of six subunits. It contains a tetracysteine motif, previously shown to bind Zn(2+) in related NTPases. Using atomic absorption spectroscopy, indeed Zn(2+) was detected in the enzyme, but in contrast to all known zinc-binding traffic NTPases only one zinc atom was bound to the hexamer. Deletion of the four cysteine residues led to a loss of Zn(2+). Nevertheless, the mutant protein retained ATPase activity and hexameric complex formation.
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