ArticlePloS one2013
Type IV pilus proteins form an integrated structure extending from the cytoplasm to the outer membrane.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed.
- Structural insights into the Thermus thermophilus type IV pilus machinery assembling two distinct pili.Communications biology · 2026Article
- Natural transformation in Gram-negative bacteria thriving in extreme environments: from genes and genomes to proteins, structures and regulation.Extremophiles : life under extreme conditions · 2021Review
- Electron Cryotomography of Bacterial Secretion Systems.Microbiology spectrum · 2019Article
- The traffic ATPase PilF interacts with the inner membrane platform of the DNA translocator and type IV pili fromFEBS open bio · 2019Article
- The type IV pilus assembly ATPase PilB functions as a signaling protein to regulate exopolysaccharide production in Myxococcus xanthus.Scientific reports · 2017Article
- Reconstitution of a minimal machinery capable of assembling periplasmic type IV pili.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- A Genotypic Analysis of FiveFrontiers in microbiology · 2017Article
- The Type IV Pilus Assembly ATPase PilB of Myxococcus xanthus Interacts with the Inner Membrane Platform Protein PilC and the Nucleotide-binding Protein PilM.The Journal of biological chemistry · 2016Article
- Architecture of the type IVa pilus machine.Science (New York, N.Y.) · 2016Article
- Appendages of the cyanobacterial cell.Life (Basel, Switzerland) · 2015Review
- Outside-in assembly pathway of the type IV pilus system in Myxococcus xanthus.Journal of bacteriology · 2014Article
- Composition of the DNA-uptake complex ofMobile genetic elements · 2014Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial type IV pilus (T4P) is the strongest biological motor known to date as its retraction can generate forces well over 100 pN. Myxococcus xanthus, a δ-proteobacterium, provides a good model for T4P investigations because its social (S) gliding motility is powered by T4P. In this study, the interactions among M. xanthus T4P proteins were investigated using genetics and the yeast two-hybrid (Y2H) system. Our genetic analysis suggests that there is an integrated T4P structure that crosses the inner membrane (IM), periplasm and the outer membrane (OM). Moreover, this structure exists in the absence of the pilus filament. A systematic Y2H survey provided evidence for direct interactions among IM and OM proteins exposed to the periplasm. For example, the IM lipoprotein PilP interacted with its cognate OM protein PilQ. In addition, interactions among T4P proteins from the thermophile Thermus thermophilus were investigated by Y2H. The results indicated similar protein-protein interactions in the T4P system of this non-proteobacterium despite significant sequence divergence between T4P proteins in T. thermophilus and M. xanthus. The observations here support the model of an integrated T4P structure in the absence of a pilus in diverse bacterial species.
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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.