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The archaeal division protein CdvB1 assembles into polymers that are depolymerized by CdvC
Author(s) -
Blanch Jover Alberto,
De Franceschi Nicola,
Fenel Daphna,
Weissenhorn Winfried,
Dekker Cees
Publication year - 2022
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.14324
Subject(s) - cell division , chemistry , archaea , atpase , division (mathematics) , microbiology and biotechnology , membrane , biochemistry , lipid ii , membrane protein , escrt , biophysics , lipid bilayer , cell , biology , cell wall , enzyme , gene , vesicle , arithmetic , mathematics , peptidoglycan
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.