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  The Sulfolobus solfataricus AAA protein Sso0909, a homologue of the eurkaryotic ESCRT Vps4 ATPase

Hobel, C., Albers, S., Driessen, A., & Lupas, A. (2008). The Sulfolobus solfataricus AAA protein Sso0909, a homologue of the eurkaryotic ESCRT Vps4 ATPase. Biochemical Society Transactions, 36, 94-98.

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 Creators:
Hobel, C., Author
Albers, S.1, Author           
Driessen, A., Author
Lupas, A., Author
Affiliations:
1Max Planck Research Group Molecular Biology of Archaea, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266317              

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Free keywords: ATPase associated with various cellular activities (AAA), bioinformatics, protein biochemistry, Sulfolobus solfataricus, Vps4 homologue.
 Abstract: Sso0909 is a protein of the thermo-acidophilic crenarchaeon Sulfolobus solfataricus, annotated as a p60 katanin-like ATPase. We present here results supporting the hypothesis that Sso0909 is an orthologue of the eukaryotic ESCRT (endosomal sorting complex required for transport) ATPase Vps4 (vacular protein sorting 4). The spectrum of Sso0909 homologues is limited to several orders of Crenarchaea and to three euryarchaeal Thermoplasmata species, where they were presumably acquired by lateral gene transfer. Almost invariably, Sso0909 homologues occur in the genomic vicinity of homologues of eukaryotic ESCRT-III components, which are the targets of disassembly by Vps4, as well as with a creanarchaeal-specific coiled-coil protein. S. solfataricus sso0909 is constitutively expressed under normal growth conditions and appears to be essential, as judged by the failure to obtain stable deletion mutants. We expressed Sso0909 in Escherichia coli and S. solfataricus, but have not obtained preparations with ATPase activity so far.

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Language(s): eng - English
 Dates: 2008
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 439341
 Degree: -

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Title: Biochemical Society Transactions
Source Genre: Journal
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Pages: - Volume / Issue: 36 Sequence Number: - Start / End Page: 94 - 98 Identifier: -