The archaeal division protein CdvB1 assembles into polymers that are depolymerized by CdvC.

The Cdv proteins constitute the cell division system of the Crenarchaea, a machinery closely related to the ESCRT system of eukaryotes. Using a combination of TEM imaging and biochemical assays, we here present an in vitro study of Metallosphaera sedula CdvB1, the Cdv protein that is believed to play a major role in the constricting ring that drives cell division in the Crenarchaea. We show that CdvB1 self-assembles into filaments that are depolymerized by the Vps4-homolog ATPase CdvC. Furthermore, we find that CdvB1 binds to negatively charged lipid membranes and can be detached from the membrane by the action of CdvC. Our findings provide novel insight into one of the main components of the archaeal cell division machinery. © 2022 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

Citation

Alberto Blanch Jover, Nicola De Franceschi, Daphna Fenel, Winfried Weissenhorn, Cees Dekker. The archaeal division protein CdvB1 assembles into polymers that are depolymerized by CdvC. FEBS letters. 2022 Mar 09;596(7):958-969

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PMID: 35238034

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