ArticleFEBS letters2022
The archaeal division protein CdvB1 assembles into polymers that are depolymerized by CdvC.
Article in FEBS letters, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- The evolution and mechanism of bacterial and archaeal ESCRT-III-like systems.Current opinion in structural biology · 2025Review
- The Archaeal Cell Cycle.Annual review of cell and developmental biology · 2024Review
- Roles of ESCRT-III polymers in cell division across the tree of life.Current opinion in cell biology · 2023Review
- The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division.Science advances · 2023Article
- Viruses of theFrontiers in microbiology · 2023Review
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Authors and funding
5 authors.
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Abstract
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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