The mechanism of cell-cycle-dependent proteasomal degradation of archaeal ESCRT-III homolog CdvB in Sulfolobus

ABSTRACT: Protein degradation orders events in the cell division cycle in eukaryotes, bacteria and archaea. In eukaryotes, chromosome segregation and mitotic exit are triggered by proteasome-dependent degradation of securin and cyclin B, respectively. Recent findings show that the archaeal proteasome also targets substrates, including CdvB, for degradation in a cell-cycle-dependent manner in Sulfolobus acidocaldarius - an experimentally tractable archaeal relative of eukaryotes. Here, using CdvB as a model substrate to explore the mechanism of cyclic protein degradation, we demonstrate that the C-terminal broken-winged helix of CdvB, previously shown to bind CdvA, is sufficient to render a fusion protein unstable as cells progress through division. We show that the rate of CdvB degradation accelerat

SUBMITTER: Yin-Wei Kuo 

PROVIDER: S-SCDT-10_1038-S44318-025-00688-7 | biostudies-other |

REPOSITORIES: biostudies-other