Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
UniProtKB/Swiss-Prot entry Q4J924 (CDVB_SULAC)
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The SubCell line encodes the location as "Cytoplasm, nucleoid", while the accompanying note describes bands between segregating nucleoids and mid-cell localization.
"Forms, with CdvA, colocalized band-like structures between segregating nucleoids"
A unique cell division machinery in the Archaea.
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Cdv proteins polymerize between segregating nucleoids and form a successively smaller structure during constriction.
"the Cdv proteins then polymerize between segregating nucleoids and persist throughout cell division, forming a successively smaller structure during constriction"
A role for the ESCRT system in cell division in archaea.
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Saci1373 (CdvB) localizes as a band between separated nucleoids at the site of membrane ingression.
"a band or belt of Saci1373 (ESCRT-III) was detected between the two nucleoids, correlating with the site of membrane ingression"
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Residues 183-193 of CdvB bind the MIT domain of Vps4 (CdvC).
"The minimal interaction sites comprised residues 183 to 193 of Saci1373 (ESCRT-III)"
Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.
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CdvB did not bind liposomes alone in this assay but was recruited by CdvA.
"although the archaeal ESCRT-III does not bind to liposomes on its own, in the presence of CdvA, it is recruited to liposomes"
The proteasome controls ESCRT-III-mediated cell division in an archaeon.
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CdvB templates the CdvB1:CdvB2 contractile copolymer and prevents its constriction; proteasomal degradation of CdvB triggers division.
"CdvB both templates the assembly of a contractile ESCRT-III copolymer, composed of the paralogs CdvB1 (Saci_0451) and CdvB2 (Saci_1416), and prevents their constriction"
Live Imaging of a Hyperthermophilic Archaeon Reveals Distinct Roles for Two ESCRT-III Homologs in Ensuring a Robust and Symmetric Division.
The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division.
The mechanism of cell-cycle-dependent proteasomal degradation of archaeal ESCRT-III homolog CdvB in Sulfolobus.
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The CdvB C-terminal broken-winged helix suffices to confer division-coupled instability.
"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"
Molecular structure of the ESCRT-III-based archaeal CdvAB cell division machinery.
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CdvB pellets with archaeal liposomes in vitro.
"CdvB and CdvB2 efficiently pelleted with archaeal liposomes, while CdvB1 remained mainly in the soluble fraction"
A relay race of ESCRT-III paralogs drives cell division in a hyperthermophilic archaeon.
Deletion of cdvB paralogous genes of Sulfolobus acidocaldarius impairs cell division.