Gene Ontology annotation through association of InterPro records with GO terms
UniProtKB/TrEMBL entry A4YHE8 (A4YHE8_METS5)
Msed_1695 paralog assignment (pairwise alignment and synteny against S. acidocaldarius Cdv paralogs)
Live Imaging of a Hyperthermophilic Archaeon Reveals Distinct Roles for Two ESCRT-III Homologs in Ensuring a Robust and Symmetric Division.
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CdvB2 keeps the ESCRT-III division ring correctly positioned as it constricts.
"These data suggested that CdvB2 is recruited (along with CdvB1) to the correct position at the cell center by the CdvB ring and functions, following the loss of CdvB, to prevent the division ring from slipping as it constricts."
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CdvB1 and CdvB2 are close paralogs.
"close paralogs that share 65% amino-acid identity and 80% similarity"
The proteasome controls ESCRT-III-mediated cell division in an archaeon.
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CdvB templates a contractile CdvB1:CdvB2 ESCRT-III copolymer.
"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"
The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division.
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Membrane scission depends on disassembly of polymeric CdvB2.
"membrane scission depends on disassembly of polymeric CdvB2 from the cytokinetic bridge"
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CdvB2 coats the membrane bridge between daughter cells.
"CdvB2 was seen coating the membrane bridge connecting the two daughter cells"
Molecular structure of the ESCRT-III-based archaeal CdvAB cell division machinery.
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CdvB2 binds archaeal-lipid liposomes in vitro.
"CdvB and CdvB2 efficiently pelleted with archaeal liposomes, while CdvB1 remained mainly in the soluble fraction"
The archaeal division protein CdvB1 assembles into polymers that are depolymerized by CdvC.
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M. sedula CdvB1 is Msed_2179.
"The gene for CdvB1 from Metallosphaera sedula (Msed_2179, UniProtID A4YIR6) was obtained from the Gen Bank database"
Crenarchaeal CdvA forms double-helical filaments containing DNA and interacts with ESCRT-III-like CdvB.
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M. sedula Cdv biochemistry covers the cdv gene cluster proteins.
"Here, we report the biochemical and biophysical characterization of the three Cdv proteins from the hyperthermophilic archaeon Metallosphaera sedula, a member of the order Sulfolobales."