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  The UbL protein UBTD1 stably interacts with the UBE2D family of E2 ubiquitin conjugating enzymes

Uhler, J. P., Spahr, H., Farge, G., Clavel, S., Larsson, N., Falkenberg, M., et al. (2013). The UbL protein UBTD1 stably interacts with the UBE2D family of E2 ubiquitin conjugating enzymes. Biochem Biophys Res Commun, 443(1), 7-12. doi:10.1016/j.bbrc.2013.10.137.

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https://www.ncbi.nlm.nih.gov/pubmed/24211586 (beliebiger Volltext)
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 Urheber:
Uhler, J. P., Autor
Spahr, H.1, Autor           
Farge, G., Autor
Clavel, S., Autor
Larsson, N.G.1, Autor           
Falkenberg, M., Autor
Samuelsson, T., Autor
Gustafsson, C. M., Autor
Affiliations:
1Department Larsson - Mitochondrial Biology, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_1942286              

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Schlagwörter: Amino Acid Sequence Conserved Sequence Humans Metabolic Networks and Pathways Molecular Sequence Data Phylogeny Protein Structure, Tertiary Two-Hybrid System Techniques Ubiquitin-Conjugating Enzymes/genetics/*metabolism Ubiquitination Ubiquitins/classification/genetics/*metabolism E2 ligase Mitochondrion Proteolysis Ubiquitin Ubiquitin-like domain
 Zusammenfassung: 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).

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 Datum: 2013-01-032013-11-12
 Publikationsstatus: Erschienen
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 Identifikatoren: Anderer: 24211586
DOI: 10.1016/j.bbrc.2013.10.137
ISSN: 0006-291x
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Titel: Biochem Biophys Res Commun
  Alternativer Titel : Biochemical and biophysical research communications
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 443 (1) Artikelnummer: - Start- / Endseite: 7 - 12 Identifikator: -