4.5 Article

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

Journal

FEBS LETTERS
Volume 596, Issue 7, Pages 958-969

Publisher

WILEY
DOI: 10.1002/1873-3468.14324

Keywords

Archaea; Cdv system; CdvB1; cell division; ESCRT-III

Funding

  1. BaSyC program of NWO-OCW [024.003.019]
  2. ERC Advanced Grant LoopingDNA [883684]
  3. FRISBI [ANR-10-INBS-05-02]
  4. GRAL, a project of the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS [ANR-17-EURE-0003]
  5. European Research Council (ERC) [883684] Funding Source: European Research Council (ERC)

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In this study, using TEM imaging and biochemical assays, the researchers investigated CdvB1, a major component of the cell division system in Crenarchaea. They found that CdvB1 self-assembles into filaments and can be detached from lipid membranes by the action of 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.

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