Braun, Tatjana and Vos, Matthijn R. and Kalisman, Nir and Sherman, Nicholas E. and Rachel, Reinhard and Wirth, Reinhard and Schroeder, Gunnar F. and Egelman, Edward H. (2016) Archaeal flagellin combines a bacterial type IV pilin domain with an Ig-like domain. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 113 (37). pp. 10352-10357. ISSN 0027-8424,
Full text not available from this repository. (Request a copy)Abstract
The bacterial flagellar apparatus, which involves similar to 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 similar to 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 similar to 4-angstrom resolution. We can now show that the archaeal flagellar filament contains a beta-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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ELECTRON-MICROSCOPY; CRYOELECTRON MICROSCOPY; IGNICOCCUS-HOSPITALIS; SALMONELLA FLAGELLA; HELICAL FILAMENTS; PROTEIN; MODEL; PILUS; RECONSTRUCTION; VISUALIZATION; archaea; flagellar filaments; helical polymers; cryo-EM |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie > Prof. Dr. Reinhard Wirth Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie > Prof. Dr. Reinhard Rachel |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 03 Apr 2019 12:07 |
| Last Modified: | 03 Apr 2019 12:10 |
| URI: | https://pred.uni-regensburg.de/id/eprint/3294 |
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