title: The UbL protein UBTD1 stably interacts with the UBE2D family of E2 ubiquitin conjugating enzymes.
abstract: UBTD1 is a previously uncharacterized ubiquitin-like (UbL) domain containing protein with high homology to the mitochondrial Dc-UbP/UBTD2 protein. Here we show that UBTD1 and UBTD2 belong to a family of proteins that is conserved through evolution and found in metazoa, funghi, and plants. To gain further insight into the function of UBTD1, we screened for interacting proteins. In a yeast-2-hybrid (Y2H) screen, we identified several proteins involved in the ubiquitylation pathway, including the UBE2D family of E2 ubiquitin conjugating enzymes. An affinity capture screen for UBTD1 interacting proteins in whole cell extracts also identified members of the UBE2D family. Biochemical characterization of recombinant UBTD1 and UBE2D demonstrated that the two proteins form a stable, stoichiometric complex that can be purified to near homogeneity. We discuss the implications of these findings in light of the ubiquitin proteasome system (UPS).
authors.affiliation: Department of Medical Biochemistry and Cell Biology, University of Gothenburg, P.O. Box 440, Sweden. Electronic address: jennifer.uhler@medkem.gu.se.
authors.forename: Jay P
authors.initials: JP
authors.lastname: Uhler
authors.affiliation: Max-Planck-Institut für Biologie des Alterns, Gleueler Str. 50a, D-50931 Cologne, Germany.
authors.forename: Henrik
authors.initials: H
authors.lastname: Spåhr
authors.affiliation: Clermont Université, Université Blaise Pascal, BP 10448, F-63000 Clermont-Fd, France.
authors.forename: Géraldine
authors.initials: G
authors.lastname: Farge
authors.affiliation: IBV Institute, CNRS UMR7277/INSERM U1091/University of Nice Sophia-Antipolis, Parc Valrose, 06108 Nice Cedex 2, France.
authors.forename: Stéphan
authors.initials: S
authors.lastname: Clavel
authors.affiliation: Max-Planck-Institut für Biologie des Alterns, Gleueler Str. 50a, D-50931 Cologne, Germany.
authors.forename: Nils-Göran
authors.initials: NG
authors.lastname: Larsson
authors.affiliation: Department of Medical Biochemistry and Cell Biology, University of Gothenburg, P.O. Box 440, Sweden; Max-Planck-Institut für Biologie des Alterns, Gleueler Str. 50a, D-50931 Cologne, Germany.
authors.forename: Maria
authors.initials: M
authors.lastname: Falkenberg
authors.affiliation: Department of Medical Biochemistry and Cell Biology, University of Gothenburg, P.O. Box 440, Sweden.
authors.forename: Tore
authors.initials: T
authors.lastname: Samuelsson
authors.affiliation: Department of Medical Biochemistry and Cell Biology, University of Gothenburg, P.O. Box 440, Sweden; Max-Planck-Institut für Biologie des Alterns, Gleueler Str. 50a, D-50931 Cologne, Germany.
authors.forename: Claes M
authors.initials: CM
authors.lastname: Gustafsson
mesh_terms: D000595:Amino Acid Sequence; D017124:Conserved Sequence; D006801:Humans; D053858:Metabolic Networks and Pathways; D008969:Molecular Sequence Data; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D020798:Two-Hybrid System Techniques; D044763:Ubiquitin-Conjugating Enzymes / Q000235:genetics / Q000378:metabolism*; D054875:Ubiquitination; D014452:Ubiquitins / Q000145:classification / Q000235:genetics / Q000378:metabolism*
chemical_list: C588185:UBTD1 protein, human; D014452:Ubiquitins; C097308:UBE2D1 protein, human; D044763:Ubiquitin-Conjugating Enzymes
keywords: E2 ligase; Mitochondrion; Proteolysis; Ubiquitin; Ubiquitin-like domain