ArticlePloS one2013
Common evolutionary origin for the rotor domain of rotary ATPases and flagellar protein export apparatus.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Insight Into Distinct Functional Roles of the Flagellar ATPase Complex for Flagellar Assembly inFrontiers in microbiology · 2022Review
- FliIScientific reports · 2020Article
- Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry.Nature communications · 2019Article
- Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.Molecules (Basel, Switzerland) · 2019Review
- Structural Insight Into Conformational Changes Induced by ATP Binding in a Type III Secretion-Associated ATPase FromFrontiers in microbiology · 2018Article
- Phytochemical derivatives targeting fliJ flagellar protein fromBioinformation · 2018Article
- Power Stroke Angular Velocity Profiles of Archaeal A-ATP Synthase Versus Thermophilic and Mesophilic F-ATP Synthase Molecular Motors.The Journal of biological chemistry · 2016Article
- Rotation of artificial rotor axles in rotary molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- FliH and FliI ensure efficient energy coupling of flagellar type III protein export in Salmonella.MicrobiologyOpen · 2016Article
- Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Flagellar region 3b supports strong expression of integrated DNA and the highest chromosomal integration efficiency of the Escherichia coli flagellar regions.Microbial biotechnology · 2015Article
- The ingenious structure of central rotor apparatus in VoV1; key for both complex disassembly and energy coupling between V1 and Vo.PloS one · 2015Article
- The bacterial flagellar protein export apparatus processively transports flagellar proteins even with extremely infrequent ATP hydrolysis.Scientific reports · 2014Article
- Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus.Scientific reports · 2014Article
- Building a flagellum outside the bacterial cell.Trends in microbiology · 2014Review
- Crystallization and preliminary X-ray analysis of the periplasmic domain of FliP, an integral membrane component of the bacterial flagellar type III protein-export apparatus.Acta crystallographica. Section F, Structural biology communications · 2014Article
- F-subunit reinforces torque generation in V-ATPase.European biophysics journal : EBJ · 2014Article
- EscO, a functional and structural analog of the flagellar FliJ protein, is a positive regulator of EscN ATPase activity of the enteropathogenic Escherichia coli injectisome.Journal of bacteriology · 2014Article
- Building a secreting nanomachine: a structural overview of the T3SS.Current opinion in structural biology · 2014Review
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The V1- and F1- rotary ATPases contain a rotor that rotates against a catalytic A3B3 or α3β3 stator. The rotor F(1-γ) or V1-DF is composed of both anti-parallel coiled coil and globular-loop parts. The bacterial flagellar type III export apparatus contains a V1/F1-like ATPase ring structure composed of FliI6 homo-hexamer and FliJ which adopts an anti-parallel coiled coil structure without the globular-loop part. Here we report that FliJ of Salmonella enterica serovar Typhimurium shows a rotor like function in Thermus thermophilus A3B3 based on both biochemical and structural analysis. Single molecular analysis indicates that an anti-parallel coiled-coil structure protein (FliJ structure protein) functions as a rotor in A3B3. A rotary ATPase possessing an F1-γ-like protein generated by fusion of the D and F subunits of V1 rotates, suggesting F(1-γ) could be the result of a fusion of the genes encoding two separate rotor subunits. Together with sequence comparison among the globular part proteins, the data strongly suggest that the rotor domains of the rotary ATPases and the flagellar export apparatus share a common evolutionary origin.
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