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Crenactin forms actin-like double helical filaments regulated by arcadin-2

DOI: 10.7554/eLife.21600 DOI Help

Authors: Thierry Izore (MRC Laboratory of Molecular Biology) , Danguole Kureisaite-ciziene (MRC Laboratory of Molecular Biology) , Stephen H Mclaughlin (MRC Laboratory of Molecular Biology) , Jan Lowe (MRC Laboratory of Molecular Biology)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Elife , VOL 5

State: Published (Approved)
Published: November 2016
Diamond Proposal Number(s): 11235

Open Access Open Access

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.

Journal Keywords: Crenarchaea; F-actin; MreB; Pyrobaculum calidifontis; arcade cluster; bacterial cytoskeleton; biophysics; cell biology; structural biology

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Added On: 18/01/2017 13:43

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