ArticleProceedings of the National Academy of Sciences of the United States of America2016
Archaeal flagellin combines a bacterial type IV pilin domain with an Ig-like domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 49 citations in OpenAlex.
- Tat-fimbriae ("tafi"): An unusual type of haloarchaeal surface structure depending on the twin-arginine translocation pathway.iScience · 2025Article
- Perturbed N-glycosylation of Halobacterium salinarum archaellum filaments leads to filament bundling and compromised cell motility.Nature communications · 2024Article
- Two distinct archaeal type IV pili structures formed by proteins with identical sequence.Nature communications · 2024Article
- Cell surface architecture of the cultivated DPANN archaeonJournal of bacteriology · 2024Article
- The evolution of archaeal flagellar filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Candidatus Alkanophaga archaea from Guaymas Basin hydrothermal vent sediment oxidize petroleum alkanes.Nature microbiology · 2023Article
- Functional compartmentalization and metabolic separation in a prokaryotic cell.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Principles and Current Clinical Landscape of Multispecific Antibodies against Cancer.International journal of molecular sciences · 2021Review
- On Origin and Evolution of the Antibody Molecule.Biology · 2021Review
- A Unique Gene Module inFrontiers in microbiology · 2021Article
- The structures of two archaeal type IV pili illuminate evolutionary relationships.Nature communications · 2020Article
- Interaction of two strongly divergent archaellins stabilizes the structure of the Halorubrum archaellum.MicrobiologyOpen · 2020Article
- Advances in methods for atomic resolution macromolecular structure determination.F1000Research · 2020Review
- Architecture and modular assembly ofProceedings of the National Academy of Sciences of the United States of America · 2019Article
- An extensively glycosylated archaeal pilus survives extreme conditions.Nature microbiology · 2019Article
- High-resolution archaellum structure reveals a conserved metal-binding site.EMBO reports · 2019Article
- Igni18, a novel metallo-hydrolase from the hyperthermophilic archaeon Ignicoccus hospitalis KIN4/I: cloning, expression, purification and X-ray analysis.Acta crystallographica. Section F, Structural biology communications · 2019Article
- DNA Uptake by Type IV Filaments.Frontiers in molecular biosciences · 2019Review
- Validation of a Hypothesis: Colonization of Black Smokers by Hyperthermophilic Microorganisms.Frontiers in microbiology · 2018Article
- Article
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
The bacterial flagellar apparatus, which involves ∼40 different proteins, has been a model system for understanding motility and chemotaxis. The bacterial flagellar filament, largely composed of a single protein, flagellin, has been a model for understanding protein assembly. This system has no homology to the eukaryotic flagellum, in which the filament alone, composed of a microtubule-based axoneme, contains more than 400 different proteins. The archaeal flagellar system is simpler still, in some cases having ∼13 different proteins with a single flagellar filament protein. The archaeal flagellar system has no homology to the bacterial one and must have arisen by convergent evolution. However, it has been understood that the N-terminal domain of the archaeal flagellin is a homolog of the N-terminal domain of bacterial type IV pilin, showing once again how proteins can be repurposed in evolution for different functions. Using cryo-EM, we have been able to generate a nearly complete atomic model for a flagellar-like filament of the archaeon Ignicoccus hospitalis from a reconstruction at ∼4-Å resolution. We can now show that the archaeal flagellar filament contains a β-sandwich, previously seen in the FlaF protein that forms the anchor for the archaeal flagellar filament. In contrast to the bacterial flagellar filament, where the outer globular domains make no contact with each other and are not necessary for either assembly or motility, the archaeal flagellin outer domains make extensive contacts with each other that largely determine the interesting mechanical properties of these filaments, allowing these filaments to flex.
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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.