Insights into the evolution of regulated actin dynamics via characterization of primitive gelsolin/cofilin proteins from Asgard archaea (original) (raw)
ADS
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- Tran, Linh T. ;
- Orhant-Prioux, Magali ;
- Baskaran, Yohendran ;
- Manser, Edward ;
- Blanchoin, Laurent ;
- Robinson, Robert C.
Abstract
Eukaryotic gelsolin superfamily proteins generally comprise three or more related domains. Here we characterize single- and double-domain gelsolins from Thorarchaeota (Thor). Similar domain architectures are present in Heimdall-, Loki-, and Odinarchaeota. Thor gelsolins are functional in regulating rabbit actin in in vitro assays, showing a range of activities including actin filament severing and bundling. These gelsolins bind to the eukaryotic gelsolin/cofilin-binding site on actin. Two-domain, but not one-domain, gelsolins are calcium regulated. Thor gelsolins appear to have the characteristics and structure consistent with primitive gelsolins/cofilins, suggesting that these single- and double-domain gelsolins are a record of a nascent preeukaryotic actin-regulation machinery.
Publication:
Proceedings of the National Academy of Science
Pub Date:
August 2020
DOI:
Bibcode: