Crenactin forms actin-like double helical filaments regulated by arcadin-2
- MRC Laboratory of Molecular Biology, United Kingdom
Abstract
The similarity of eukaryotic actin to crenactin, a filament-forming protein from the crenarchaeon Pyrobaculum calidifontis supports the theory of a common origin of Crenarchaea and Eukaryotes. Monomeric structures of crenactin and actin are similar, although their filament architectures were suggested to be different. Here we report that crenactin forms bona fide double helical filaments that show exceptional similarity to eukaryotic F-actin. With cryo-electron microscopy and helical reconstruction we solved the structure of the crenactin filament to 3.8 Å resolution. When forming double filaments, the 'hydrophobic plug' loop in crenactin rearranges. Arcadin-2, also encoded by the arcade gene cluster, binds tightly with its C-terminus to the hydrophobic groove of crenactin. Binding is reminiscent of eukaryotic actin modulators such as cofilin and thymosin β4 and arcadin-2 is a depolymeriser of crenactin filaments. Our work further supports the theory of shared ancestry of Eukaryotes and Crenarchaea.
Article and author information
Author details
Stephen H McLaughlin
Funding
Medical Research Council (U105184326)
- Danguole Kureisaite-Ciziene
- Stephen H McLaughlin
- Jan Löwe
Wellcome (095514/Z/11/Z)
- Thierry Izoré
- Jan Löwe
European Molecular Biology Organization (ALTF 1379-2011)
- Thierry Izoré
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Copyright
© 2016, Izoré et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Crenactin forms actin-like double helical filaments regulated by arcadin-2
eLife 5:e21600.
https://doi.org/10.7554/eLife.21600
