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

Thierry Izore, Danguole Kureisaite-Ciziene, Stephen H. McLaughlin, Jan Lowe

Research output: Contribution to journalArticleResearchpeer-review

13 Citations (Scopus)

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 b4 and arcadin-2 is a depolymeriser of crenactin filaments. Our work further supports the theory of shared ancestry of Eukaryotes and Crenarchaea.

Original languageEnglish
Article numbere21600
Number of pages18
JournaleLife
Volume5
DOIs
Publication statusPublished - 17 Nov 2016
Externally publishedYes

Keywords

  • Cryo electron microscopy

Cite this

Izore, Thierry ; Kureisaite-Ciziene, Danguole ; McLaughlin, Stephen H. ; Lowe, Jan. / Crenactin forms actin-like double helical filaments regulated by arcadin-2. In: eLife. 2016 ; Vol. 5.
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Crenactin forms actin-like double helical filaments regulated by arcadin-2. / Izore, Thierry; Kureisaite-Ciziene, Danguole; McLaughlin, Stephen H.; Lowe, Jan.

In: eLife, Vol. 5, e21600, 17.11.2016.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Izore, Thierry

AU - Kureisaite-Ciziene, Danguole

AU - McLaughlin, Stephen H.

AU - Lowe, Jan

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N2 - 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 b4 and arcadin-2 is a depolymeriser of crenactin filaments. Our work further supports the theory of shared ancestry of Eukaryotes and Crenarchaea.

AB - 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 b4 and arcadin-2 is a depolymeriser of crenactin filaments. Our work further supports the theory of shared ancestry of Eukaryotes and Crenarchaea.

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