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          Institute: MPI für Entwicklungsbiologie     Collection: Abteilung 1 - Protein Evolution (A. Lupas)     Display Documents

ID: 460628.0, MPI für Entwicklungsbiologie / Abteilung 1 - Protein Evolution (A. Lupas)
Two unique membrane-bound AAA proteins from Sulfolobus solfataricus
Authors:Serek-Heuberger, J.; Hobel, C. F.; Dunin-Horkawicz, S.; Rockel, B.; Martin, J.; Lupas, A. N.
Date of Publication (YYYY-MM-DD):2009-02
Title of Journal:Biochem Soc Trans
Issue / Number:Pt 1
Start Page:118
End Page:122
Review Status:not specified
Audience:Not Specified
Abstract / Description:Thermoacidophilic crenarchaea of the genus Sulfolobus contain six AAA (ATPase associated with various cellular activities) proteins, including a proteasome-associated ATPase, a Vps4 (vacuolar protein sorting 4) homologue, and two Cdc48 (cell-division cycle 48)-like proteins. The last two AAA proteins are deeply branching divergent members of this family without close relatives outside the Sulfolobales. Both proteins have two nucleotide-binding domains and, unlike other members of the family, they seem to lack folded N-terminal domains. Instead, they contain N-terminal extensions of approx. 50 residues, which are predicted to be unstructured, except for a single transmembrane helix. We have analysed the two proteins, MBA (membrane-bound AAA) 1 and MBA2, by computational and experimental means. They appear to be monophyletic and to share a common ancestor with the Cdc48 clade. Both are membrane-bound and active as nucleotidases upon heterologous expression in Escherichia coli. They form ring complexes, which are stable after solubilization in a mild detergent and whose formation is dependent on the presence of the N-terminal extensions.
Free Keywords:Adenosine Triphosphatases/chemistry/*metabolism/ultrastructure; Amino Acid Sequence; Archaeal Proteins/chemistry/*metabolism/ultrastructure; Biochemical Phenomena; Cell Membrane/*enzymology; Computational Biology; Cryoelectron Microscopy; Molecular Sequence Data; Mutant Proteins/chemistry/metabolism; Sulfolobus solfataricus/*enzymology
External Publication Status:published
Document Type:Article
Affiliations:MPI für Entwicklungsbiologie/Abteilung 1 - Proteinevolution (Andrei Lupas)
External Affiliations:%G eng
Identifiers:ISSN:1470-8752 (Electronic) 0300-5127 (Linking) %R BST0... [ID No:1]
URL: [ID No:2]
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