In:
eLife, eLife Sciences Publications, Ltd, Vol. 5 ( 2016-11-17)
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.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.21600.001
DOI:
10.7554/eLife.21600.002
DOI:
10.7554/eLife.21600.003
DOI:
10.7554/eLife.21600.004
DOI:
10.7554/eLife.21600.005
DOI:
10.7554/eLife.21600.006
DOI:
10.7554/eLife.21600.007
DOI:
10.7554/eLife.21600.008
DOI:
10.7554/eLife.21600.009
DOI:
10.7554/eLife.21600.010
DOI:
10.7554/eLife.21600.011
DOI:
10.7554/eLife.21600.012
DOI:
10.7554/eLife.21600.013
DOI:
10.7554/eLife.21600.014
DOI:
10.7554/eLife.21600.015
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2016
detail.hit.zdb_id:
2687154-3
